56,994 research outputs found
Time-resolved fluorescence study during denaturation and renaturation of curcumin-myoglobin complex
No full textCurcumin influences the transition point, the concentration of denaturant required to effect 50percent of the total change, of myoglobin denaturation. Curcumin enhances absorbance of myoglobin at 280nm with a binding constant K=3.0×104M-1 whereas fluorescence of curcumin is quenched by myoglobin with a Stern-Volmer association constant of 2.5×105M-1. Unfolding process of myoglobin-curcumin induces a recovery in fluorescence lifetime loss. The gain in time-resolved fluorescence lifetime during unfolding has been again lost during refolding of curcumin-myoglobin complex by dilution process suggesting partial reversibility of unfolding process for both myoglobin and curcumin-myoglobin complex. © 2012 Elsevier B.V.Abou-Zied OK, 2008, J AM CHEM SOC, V130, P10793, DOI 10.1021-ja8031289; Baglole KN, 2005, J PHOTOCH PHOTOBIO A, V173, P230, DOI 10.1016-j.jphotochem.2005.04.002; Barakat C., 2012, LUMINESCENCE 0207, DOI [10.1002-bio.2354, DOI 10.1002-BIO.2354]; Barakat C., 2010, KALAHANDI RENAISSANC, VV, P64; Barik A, 2003, PHOTOCHEM PHOTOBIOL, V77, P597, DOI 10.1562-0031-8655(2003)0770597:PSOBOC2.0.CO;2; Barik A, 2007, CHEM PHYS LETT, V436, P239, DOI 10.1016-j.cplett.2007.01.006; Benesi M. L., 1949, J AM CHEM SOC, V71, P2703; Bisht S., 2007, J NANOBIOTECHNOL, V5, P1; Bourassa P, 2010, J PHYS CHEM B, V114, P3348, DOI 10.1021-jp9115996; Cantor C.R., 1980, BIOPHYSICAL CHEM 2; CHIGNELL CF, 1994, PHOTOCHEM PHOTOBIOL, V59, P295, DOI 10.1111-j.1751-1097.1994.tb05037.x; Chowdhry B, 1997, J CHEM EDUC, V74, P236; Clifford NW, 2008, J MATER CHEM, V18, P162, DOI 10.1039-b715100d; Connors K. A., 1987, MEASUREMENTS MOL COM; Creighton T. E., 1993, PROTEIN STRUCTURE; Creighton T. E., 1992, PROTEIN FOLDING; DAUTREVA.M, 1969, EUR J BIOCHEM, V11, P267, DOI 10.1111-j.1432-1033.1969.tb00769.x; Devasenam T, 2003, PHARM RES, V27, P133; DILL KA, 1991, ANNU REV BIOCHEM, V60, P795, DOI 10.1146-annurev.biochem.60.1.795; EFTINK MR, 1994, BIOPHYS J, V66, P482; EVANS SV, 1990, J MOL BIOL, V213, P885, DOI 10.1016-S0022-2836(05)80270-0; Feng W, 2006, J FLUORESC, V16, P53; GOLDBERG ME, 1991, TRENDS BIOCHEM SCI, V16, P358, DOI 10.1016-0968-0004(91)90148-O; Jones CM, 1997, J CHEM EDUC, V74, P1306; Jovanovic SV, 2001, J AM CHEM SOC, V123, P3064, DOI 10.1021-ja003823x; Jovanovic SV, 1999, J AM CHEM SOC, V121, P9677, DOI 10.1021-ja991446m; Leung MHM, 2008, LANGMUIR, V24, P5672, DOI 10.1021-la800780w; Lin YG, 2007, CLIN CANCER RES, V13, P3423, DOI 10.1158-1078-0432.CCR-06-3072; Pace C N, 1986, Methods Enzymol, V131, P266; Pace N.C., 1989, PROTEIN STRUCTURE PR; Patra D, 2012, LUMINESCENCE, V27, P11, DOI 10.1002-bio.1313; Patra D, 2011, SPECTROCHIM ACTA A, V79, P1034, DOI 10.1016-j.saa.2011.04.016; Patra D, 2011, SPECTROCHIM ACTA A, V79, P1823, DOI 10.1016-j.saa.2011.05.064; Patra D., PHOTOCHEM P IN PRESS; Privalov P.L., 1990, BIOCH MOL BIOL, V25, P281; PUETT D, 1973, J BIOL CHEM, V248, P4623; Rankin MA, 2004, SUPRAMOL CHEM, V16, P513, DOI 10.1080-10610270412331283583; SCHECHTE.AN, 1968, J MOL BIOL, V35, P567, DOI 10.1016-S0022-2836(68)80015-4; Schmid F.X., 1989, PROTEIN STRUCTURE PR; SHARMA OP, 1976, BIOCHEM PHARMACOL, V25, P1811, DOI 10.1016-0006-2952(76)90421-4; SRIVASTAVA KC, 1995, PROSTAG LEUKOTR ESS, V52, P223, DOI 10.1016-0952-3278(95)90040-3; Sun YM, 2002, ORG LETT, V4, P2909, DOI 10.1021-ol0262789; TANFORD C, 1964, J AM CHEM SOC, V86, P2050, DOI 10.1021-ja01064a028; Tourkina E, 2004, AM J RESP CELL MOL, V31, P28, DOI 10.1165-rcmb.2003-03540C; Vemula PK, 2006, J AM CHEM SOC, V128, P8932, DOI 10.1021-ja062650u; WARE WR, 1962, J PHYS CHEM-US, V66, P455, DOI 10.1021-j100809a02044
Study on effect of lipophilic curcumin on sub-domain IIA site of human serum albumin during unfolded and refolded states: A synchronous fluorescence spectroscopic study
No full textCurcumin having pharmaceutical application as anti-oxidant, anti-inflammatory and anti-carcinogenic drug necessitates studying interaction of this molecule with native, unfolded and refolded state of human serum albumin (HSA), carrier protein in the blood. We proposed a simultaneous static and dynamic fluorescence quenching mechanism operating in the complex formation between HSA and curcumin. Location of curcumin in the close proximity of tryptophan with respect to tyrosine was further evident from the observation of two fold increase in rate of depletion of SFS intensity for tryptophan with respect to tyrosine in HSA in SFS spectrum. Alteration of SFS spectral peak position, electronic absorbance, fluorescence intensity and lifetime suggested chemical denaturation by urea expectedly unfold the protein molecule in the absence and presence of curcumin. Denatured HSA had similar fluorescence peak position and lifetime to that of l-tryptophan in the polar environment. During unfolding of HSA the spectral change of tyrosine and tryptophan was resolved through synchronous fluorescence spectra at two different Δλ in absence and presence of curcumin. It is found that curcumin remained bound to unfolded state of HSA and facilitated the process by pushing tryptophan moiety to more polar environment in the unfolded state. Dilution of the denatured protein by phosphate buffer reversibly refolded the sub-domain IIA, by also recovering fluorescence lifetime loss, but it was slow in the presence of curcumin. k q values indicate that curcumin-HSA complex is formed in the unfolded and refolded states as observed for native state. © 2012 Elsevier B.V.Abert WC, 1993, ANAL BIOCHEM, V213, P407; Abou-Zied OK, 2008, J AM CHEM SOC, V130, P10793, DOI 10.1021-ja8031289; Baglole KN, 2005, J PHOTOCH PHOTOBIO A, V173, P230, DOI 10.1016-j.jphotochem.2005.04.002; Barik A, 2003, PHOTOCHEM PHOTOBIOL, V77, P597, DOI 10.1562-0031-8655(2003)0770597:PSOBOC2.0.CO;2; Barik A, 2007, CHEM PHYS LETT, V436, P239, DOI 10.1016-j.cplett.2007.01.006; Benesi M. L., 1949, J AM CHEM SOC, V71, P2703; BERDE CB, 1979, J BIOL CHEM, V254, P391; Bisht S., 2007, J NANOBIOTECHNOL, V5, P1; Bourassa P, 2010, J PHYS CHEM B, V114, P3348, DOI 10.1021-jp9115996; CARTER DC, 1994, ADV PROTEIN CHEM, V45, P153; CHIGNELL CF, 1994, PHOTOCHEM PHOTOBIOL, V59, P295, DOI 10.1111-j.1751-1097.1994.tb05037.x; Clifford NW, 2008, J MATER CHEM, V18, P162, DOI 10.1039-b715100d; Colmenarejo G, 2003, MED RES REV, V23, P275, DOI 10.1002-med.10039; Devasenam T, 2003, PHARM RES, V27, P133; DOWEIKO JP, 1991, JPEN-PARENTER ENTER, V15, P207, DOI 10.1177-0148607191015002207; Feng W, 2006, J FLUORESC, V16, P53; Fiirster T., 1996, MODERN QUANTUM CHEM, V3; FORSTER T, 1959, DISCUSS FARADAY SOC, P7; GEHLEN MH, 1993, CHEM REV, V93, P199, DOI 10.1021-cr00017a010; HE XM, 1992, NATURE, V358, P209, DOI 10.1038-358209a0; JACOBSEN J, 1983, J BIOL CHEM, V258, P6319; Jovanovic SV, 2001, J AM CHEM SOC, V123, P3064, DOI 10.1021-ja003823x; Jovanovic SV, 1999, J AM CHEM SOC, V121, P9677, DOI 10.1021-ja991446m; JUSKO WJ, 1976, DRUG METAB REV, V5, P43, DOI 10.3109-03602537608995839; Kapoor S, 2001, BIOPHYS CHEM, V92, P119, DOI 10.1016-S0301-4622(01)00188-0; KRAGHHANSEN U, 1981, PHARMACOL REV, V33, P17; KRAGHHANSEN U, 1990, EUR J BIOCHEM, V193, P169, DOI 10.1111-j.1432-1033.1990.tb19319.x; Lakowicz J. R., 1999, PRINCIPLES FLUORESCE; Leung MHM, 2008, LANGMUIR, V24, P5672, DOI 10.1021-la800780w; Lin YG, 2007, CLIN CANCER RES, V13, P3423, DOI 10.1158-1078-0432.CCR-06-3072; Mandeville JS, 2009, J PHARMACEUT BIOMED, V49, P468, DOI 10.1016-j.jpba.2008.11.035; Mendez C.M., 2005, J NUTR CLIN PRACT, V20, P314; MINCHIOTTI L, 1995, EUR J BIOCHEM, V228, P155, DOI 10.1111-j.1432-1033.1995.tb20244.x; Patra D, 2012, LUMINESCENCE, V27, P11, DOI 10.1002-bio.1313; Patra D, 2011, SPECTROCHIM ACTA A, V79, P1034, DOI 10.1016-j.saa.2011.04.016; Patra D, 2011, SPECTROCHIM ACTA A, V79, P1823, DOI 10.1016-j.saa.2011.05.064; Patra D, 2009, TALANTA, V77, P1549, DOI 10.1016-j.talanta.2008.09.007; Patra D, 2010, BIOSENS BIOELECTRON, V25, P1149, DOI 10.1016-j.bios.2009.09.041; Patra D, 2000, ANALYST, V125, P1383, DOI 10.1039-b003876h; Patra D, 2003, LUMINESCENCE, V18, P97, DOI 10.1002-bio.712; Patra D, 2002, TRAC-TREND ANAL CHEM, V21, P787, DOI 10.1016-S0165-9936(02)01201-3; PETERS T, 1985, ADV PROTEIN CHEM, V37, P161, DOI 10.1016-S0065-3233(08)60065-0; Rankin MA, 2004, SUPRAMOL CHEM, V16, P513, DOI 10.1080-10610270412331283583; Reddy ACP, 1999, LIPIDS, V34, P1025, DOI 10.1007-s11745-999-0453-x; Saquib Q, 2010, INT J BIOL MACROMOL, V47, P60, DOI 10.1016-j.ijbiomac.2010.03.020; SHARMA OP, 1976, BIOCHEM PHARMACOL, V25, P1811, DOI 10.1016-0006-2952(76)90421-4; SRIVASTAVA KC, 1995, PROSTAG LEUKOTR ESS, V52, P223, DOI 10.1016-0952-3278(95)90040-3; SUDLOW G, 1976, MOL PHARMACOL, V12, P1052; SUDLOW G, 1975, MOL PHARMACOL, V11, P824; Sulkowska A, 2002, J MOL STRUCT, V614, P227, DOI 10.1016-S0022-2860(02)00256-9; Sun YM, 2002, ORG LETT, V4, P2909, DOI 10.1021-ol0262789; Tang JH, 2006, BIOORGAN MED CHEM, V14, P3210, DOI 10.1016-j.bmc.2005.12.034; Tourkina E, 2004, AM J RESP CELL MOL, V31, P28, DOI 10.1165-rcmb.2003-03540C; Vemula PK, 2006, J AM CHEM SOC, V128, P8932, DOI 10.1021-ja062650u; Wang Y, 1997, TALANTA, V44, P1319, DOI 10.1016-S0039-9140(97)00028-3; WARE WR, 1962, J PHYS CHEM-US, V66, P455, DOI 10.1021-j100809a020; Zsila F, 2003, BIOCHEM BIOPH RES CO, V301, P776, DOI 10.1016-S0006-291X(03)00030-521222
Revoking excited state intra-molecular hydrogen transfer by size dependent tailor-made hierarchically ordered nanocapsules
No full textCurcumin associated poly(allylamine hydrochloride) cross-links with dipotassium phosphate and subsequently is assembled with ∼24 nm SiO 2 nanoparticles to form hierarchically ordered nanocapsule structures, which are 100-1000 nm in size depending on the concentration of dipotassium phosphate. These structures reverse the excited state intra-molecular hydrogen transfer in curcumin depending on the size of the nanocapsules. © 2014 The Royal Society of Chemistry.Adhikary R, 2010, J PHYS CHEM B, V114, P2997, DOI 10.1021-jp9101527; Adhikary R, 2009, J PHYS CHEM B, V113, P5255, DOI 10.1021-jp901234z; Amali AJ, 2011, ANAL CHIM ACTA, V708, P75, DOI 10.1016-j.aca.2011.10.001; Anker JN, 2008, NAT MATER, V7, P442, DOI 10.1038-nmat2162; Bailey RC, 2003, J AM CHEM SOC, V125, P13541, DOI 10.1021-ja035479k; Baiz CR, 2007, J PHYS CHEM A, V111, P10139, DOI 10.1021-jp074290i; Bong PH, 2000, B KOR CHEM SOC, V21, P81; Demchenko AP, 2013, CHEM SOC REV, V42, P1379, DOI 10.1039-c2cs35195a; Elsasser T., 2002, ULTRAFAST HYDROGEN B; Erez Y, 2011, J PHYS CHEM A, V115, P10962, DOI 10.1021-jp206176p; Galasso V, 2008, J PHYS CHEM A, V112, P2331, DOI 10.1021-jp7108303; Hammes-Schiffer S, 2010, CHEM REV, V110, P6937, DOI 10.1021-cr100367q; Jovanovic SV, 1999, J AM CHEM SOC, V121, P9677, DOI 10.1021-ja991446m; Kee TW, 2011, AUST J CHEM, V64, P23, DOI 10.1071-CH10417; Khopde SM, 2000, PHOTOCHEM PHOTOBIOL, V72, P625, DOI 10.1562-0031-8655(2000)0720625:EOSOTE2.0.CO;2; Kong L, 2004, J MOL STRUC-THEOCHEM, V684, P111, DOI 10.1016-j.theochem.2004.06.034; Liu ZS, 2000, ADV MATER, V12, P288, DOI 10.1002-(SICI)1521-4095(200002)12:4288::AID-ADMA2883.0.CO;2-1; Mendes PM, 2008, CHEM SOC REV, V37, P2512, DOI 10.1039-b714635n; Meyer TJ, 2007, ANGEW CHEM INT EDIT, V46, P5284, DOI 10.1002-anie.200600917; Nayak S, 2004, ANGEW CHEM INT EDIT, V43, P6706, DOI 10.1002-anie.200461090; Patra D, 2011, SPECTROCHIM ACTA A, V79, P1034, DOI 10.1016-j.saa.2011.04.016; Patra D, 2012, COLLOID SURFACE B, V94, P354, DOI 10.1016-j.colsurfb.2012.02.017; Patra D, 2012, PHOTOCHEM PHOTOBIOL, V88, P317, DOI 10.1111-j.1751-1097.2011.01067.x; Patra D, 2013, MICROCHIM ACTA, V180, P59, DOI 10.1007-s00604-012-0903-5; Patra D, 2009, J MATER CHEM, V19, P4017, DOI 10.1039-b822358k; Pischel U, 2006, PHOTOCHEM PHOTOBIOL, V82, P310, DOI 10.1562-2005-02-07-RA-434; Presiado I, 2012, J PHOTOCH PHOTOBIO A, V247, P42, DOI 10.1016-j.jphotochem.2012.08.007; Rana RK, 2005, ADV MATER, V17, P1145, DOI 10.1002-adma.200401612; Roy D, 2009, CHEM COMMUN, P2106, DOI 10.1039-b900374f; Shen L, 2005, ORG LETT, V7, P243, DOI 10.1021-ol047766e; Shen L, 2007, SPECTROCHIM ACTA A, V67, P619, DOI 10.1016-j.saa.2006.08.018; Soppimath KS, 2005, ADV MATER, V17, P318, DOI 10.1002-adma.200401057; TONNESEN HH, 1982, ACTA CHEM SCAND B, V36, P475, DOI 10.3891-acta.chem.scand.36b-0475; Yallapu MM, 2012, DRUG DISCOV TODAY, V17, P71, DOI 10.1016-j.drudis.2011.09.009; Yun C, 2009, J PHOTOCH PHOTOBIO C, V10, P111, DOI 10.1016-j.jphotochemrev.2009.05.002; Zsila F, 2003, TETRAHEDRON-ASYMMETR, V14, P2433, DOI 10.1016-S0957-4166(03)00486-50
Study on interaction of bile salts with curcumin and curcumin embedded in dipalmitoyl-sn-glycero-3-phosphocholine liposome
No full textCurcumin, often used as a food spice, is a natural polyphenol that has various medicinal benefits such as anti-cancer, anti-amyloid, anti-oxidant, and anti-inflammatory properties, among others. The interaction between bile salts having physiological significance and curcumin suggests the aggregation of bile salts dramatically alters the absorption and fluorescence parameters of curcumin. The fluorescence emission maximum as well as the intensity can easily detect critical micellar concentration of sodium cholate and sodium deoxycholate respectively to be 16 and 6. mM at room temperature. The mechanism of interaction of curcumin with bile salts has been presented at low, intermediate and high bile salt concentrations and depends on temperature. In the presence of bile salts the DPPH scavenging activity was preserved, though less than in the presence of curcumin alone. The effect of submicellar concentration, 5-50. μM, of bile salt with 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) liposomes in solid gel and liquid crystalline phases has been investigated using curcumin as an embedded probe in the membrane. The curcumin based fluorescence probing method indicates even at very low concentration, ~5. μM, incorporation of monomeric bile salt molecules disorders the membrane properties. Expulsion of curcumin from the membrane in the presence of bile salt is ruled out, suggesting wetting of membrane. Alteration of membrane fluidity by bile salts is found to have an opposing effect in the liquid crystalline phase compared to in the solid gel phase, and is sensitive to the nature of bile salt. The permeability in the liquid crystalline phase decreases in the presence of bile salt. The phase transition temperature of the membrane is influenced by bile salt. © 2013 Elsevier B.V.Aggarwal BB, 2009, INT J BIOCHEM CELL B, V41, P40, DOI 10.1016-j.biocel.2008.06.010; ALPER HE, 1993, J CHEM PHYS, V99, P5547, DOI 10.1063-1.465947; AMMON HPT, 1991, PLANTA MED, V57, P1, DOI 10.1055-s-2006-960004; Barry J, 2009, J AM CHEM SOC, V131, P4490, DOI 10.1021-ja809217u; Ben Mouaz B., 2001, COLLOID SURFACE B, V20, P119; Bisht S, 2010, MOL CANCER THER, V9, P2255, DOI 10.1158-1535-7163.MCT-10-0172; Cardenas M, 2008, CHEM PHYS LIPIDS, V151, P10, DOI 10.1016-j.chemphyslip.2007.09.002; Chantres JR, 1996, INT J PHARM, V138, P139, DOI 10.1016-0378-5173(96)04530-9; CHIU YC, 1992, J DISPER SCI TECHNOL, V13, P587, DOI 10.1080-01932699208943341; Coello A, 1996, J PHARM SCI, V85, P9, DOI 10.1021-js950326j; Duan RD, 2006, BBA-MOL CELL BIOL L, V1761, P281, DOI 10.1016-j.bbalip.2006.03.007; Erlinger S., 1987, PHYSL BILE SECRETION; Goel A, 2008, BIOCHEM PHARMACOL, V75, P787, DOI 10.1016-j.bcp.2007.08.016; Gouin S, 1998, LANGMUIR, V14, P4025, DOI 10.1021-la971155w; Gridel P., 2007, MOLECULES, V12, P2292; Hildebrand A, 2003, COLLOID SURFACE B, V32, P335, DOI 10.1016-j.colsurfb.2003.08.001; Hung WC, 2008, BIOPHYS J, V94, P4331, DOI 10.1529-biophysj.107.126888; Im E, 2005, CANCER LETT, V229, P49, DOI 10.1016-j.canlet.2004.11.055; Jordan WC, 1996, J NATL MED ASSOC, V88, P333; Jovanovic SV, 1999, J AM CHEM SOC, V121, P9677, DOI 10.1021-ja991446m; Ke D, 2011, LANGMUIR, V27, P14112, DOI 10.1021-la203592j; LASCH J, 1995, BBA-REV BIOMEMBRANES, V1241, P269, DOI 10.1016-0304-4157(95)00010-O; Lee YK, 2009, J AGR FOOD CHEM, V57, P305, DOI 10.1021-jf802737z; LI G, 1994, J PHYS CHEM-US, V98, P13711, DOI 10.1021-j100102a043; Li L, 2005, CANCER, V104, P1322, DOI 10.1002-cncr.21300; Lopez-Lazaro M, 2008, MOL NUTR FOOD RES, V52, pS103, DOI 10.1002-mnfr.200700238; MAZER NA, 1979, BIOCHEMISTRY-US, V18, P3064, DOI 10.1021-bi00581a024; Mohapatra M, 2010, J PHYS CHEM B, V114, P14934, DOI 10.1021-jp103855q; Mohapatra M, 2011, LANGMUIR, V27, P13461, DOI 10.1021-la203028s; Mondal S, 2012, J PHOTOCH PHOTOBIO B, V115, P9, DOI 10.1016-j.jphotobiol.2012.06.004; Mourtas S, 2011, BIOMATERIALS, V32, P1635, DOI 10.1016-j.biomaterials.2010.10.027; New RC, 1990, LIPOSOMES PRACTICAL; NORMAN A, 1960, ACTA CHEM SCAND, V14, P1295, DOI 10.3891-acta.chem.scand.14-1295; OCONNOR CJ, 1985, ADV COLLOID INTERFAC, V22, P1, DOI 10.1016-0001-8686(85)80002-6; Ozcelik B, 2003, J FOOD SCI, V68, P487, DOI 10.1111-j.1365-2621.2003.tb05699.x; Patra D, 2011, SPECTROCHIM ACTA A, V79, P1034, DOI 10.1016-j.saa.2011.04.016; Patra D, 2012, COLLOID SURFACE B, V94, P354, DOI 10.1016-j.colsurfb.2012.02.017; Patra D, 2012, PHOTOCHEM PHOTOBIOL, V88, P317, DOI 10.1111-j.1751-1097.2011.01067.x; Patra D., 2011, SPECTROCHIM ACTA A, V79; PAULA S, 1995, J PHYS CHEM-US, V99, P11742, DOI 10.1021-j100030a019; Perez-Lara A, 2010, J PHYS CHEM B, V114, P9778, DOI 10.1021-jp101045p; Pizzo P, 2010, J CELL MOL MED, V14, P970, DOI 10.1111-j.1582-4934.2009.00681.x; Re F, 2011, NANOMED-NANOTECHNOL, V7, P551, DOI 10.1016-j.nano.2011.05.004; Resi S., 2004, ANAL BIOCHEM, V334, P117; Sasaki J., 2012, CURCUMIN BIOSYNTHESI; SHAW R, 1991, MIKROCHIM ACTA, V3, P137; Shekels LL, 1996, J LAB CLIN MED, V127, P57, DOI 10.1016-S0022-2143(96)90166-3; Shishodia S, 2007, CURR PROB CANCER, V31, P243, DOI 10.1016-j.currproblcancer.2007.04.001; Simonovic BR, 1997, MIKROCHIM ACTA, V127, P101, DOI 10.1007-BF01243172; Sneharani AH, 2010, J AGR FOOD CHEM, V58, P11130, DOI 10.1021-jf102826q; Subuddhi U, 2007, COLLOID SURFACE B, V57, P102, DOI 10.1016-j.colsurfb.2007.01.009; Subuddhi U, 2007, J CHEM SCI, V119, P169, DOI 10.1007-s12039-007-0024-6; Sugioka H, 2003, J COLLOID INTERF SCI, V259, P156, DOI 10.1016-S0021-9797(02)00191-1; Sugiyama Y, 1996, BIOCHEM PHARMACOL, V52, P519, DOI 10.1016-0006-2952(96)00302-4; Tanford C., 1980, HYDROPHOBIC EFFECT F, P94; Thangapazham RL, 2008, INT J ONCOL, V32, P1119; Tonnesen HH, 2002, PHARMAZIE, V57, P820; UENO M, 1987, J COLLOID INTERF SCI, V117, P179, DOI 10.1016-0021-9797(87)90181-0; Wahlstrom B., 1978, PHARMACOL TOXICOL, V43, P86; Wang D, 2008, CLIN CANCER RES, V14, P6228, DOI 10.1158-1078-0432.CCR-07-5177; Wang DQH, 2009, J LIPID RES, V50, pS406, DOI 10.1194-jlr.R800075-JLR200; Wilken R, 2011, MOL CANCER, V10, DOI 10.1186-1476-4598-10-12; Yallapu MM, 2010, J COLLOID INTERF SCI, V351, P19, DOI 10.1016-j.jcis.2010.05.02233
Application and new developments in fluorescence spectroscopic techniques in studying individual molecules
No full textTechniques based on fluorescence have played a variety of roles in chemistry, physics, spectroscopy, medicine, nanotechnology, and biotechnology due to their high selectivity, sensitivity, simplicity, and fastness in spectroscopic and imaging measurements. While detecting fluorescence from individual molecules by fluorescence-based techniques, poor signal, limited lifespan of fluorophores, trade-off between time resolution, and the level of detail of information were few major concerns. Ultrasensitive detectors permit the combination of the high time resolution of single photon counting devices with the large field of view and spectral resolution allowed by two-dimensional detectors. Photobleaching and on-off blinking of fluorophores can be improved dramatically by chemical modifications or changing the reagents. New ways of controlling local fields such as optic, electric, magnetic, chemical, or biochemical environments take advantage of the noninvasiveness and high temporal and spatial resolution of single-molecule fluorescence (SMF) to get a direct feedback of events at the nanometer scale in various domains of research. Some of the applications and new developments in fluorescence spectroscopic techniques in detecting, investigating, and-or manipulating individual molecules have been discussed.Adachi K, 2000, P NATL ACAD SCI USA, V97, P7243, DOI 10.1073-pnas.120174297; Adachi K, 2007, CELL, V130, P309, DOI 10.1016-j.cell.2007.05.020; Adhikary A, 2003, NUCLEIC ACIDS RES, V31, P2178, DOI 10.1093-nar-gkg308; Anger P, 2006, PHYS REV LETT, V96, DOI 10.1103-PhysRevLett.96.113002; Bacia K, 2006, NAT METHODS, V3, P83, DOI 10.1038-NMETH822; Barbara PF, 2005, ACCOUNTS CHEM RES, V38, P602, DOI 10.1021-ar040141w; Bartko AP, 1999, J PHYS CHEM B, V103, P3053, DOI 10.1021-jp9846330; Bartko AP, 1999, J PHYS CHEM B, V103, P11237, DOI 10.1021-jp993364q; Baudendistel N, 2005, CHEMPHYSCHEM, V6, P984, DOI 10.1002-cphc.200400639; Bel G, 2006, J PHYS CHEM B, V110, P19066, DOI 10.1021-jp062345v; Blum C, 2002, CHEM PHYS LETT, V362, P355, DOI 10.1016-S0009-2614(02)01014-X; Boehmer M., 2003, J OPT SOC AM B, V20, P554; BOEHMER M, 2002, CHEM PHYS LETT, V353, P439; Boehmer M., 2003, CHEMPHYSCHEM, V4, P792; Bokinsky G, 2003, P NATL ACAD SCI USA, V100, P9302, DOI 10.1073-pnas.1133280100; Boukobza E, 2001, J PHYS CHEM B, V105, P12165, DOI 10.1021-jp012016x; Bowen B, 2003, PHOTOCHEM PHOTOBIOL, V77, P362, DOI 10.1562-0031-8655(2003)0770362:SFLAAM2.0.CO;2; Brokmann X, 2005, CHEM PHYS LETT, V406, P210, DOI 10.1016-j.cplett.2005.03.007; Burghardt TP, 2006, BIOCHEMISTRY-US, V45, P4058, DOI 10.1021-bi052097d; Cannone F, 2006, J PHYS CHEM B, V110, P16491, DOI 10.1021-jp0625816; Cao JS, 2006, J PHYS CHEM B, V110, P19040, DOI 10.1021-jp061302b; Cha A, 1999, NATURE, V402, P809; Chanda B, 2005, NATURE, V436, P852, DOI 10.1038-nature03888; Chattopadhyay K, 2002, P NATL ACAD SCI USA, V99, P14171, DOI 10.1073-pnas.172524899; Chirico G, 2001, MICROSC RES TECHNIQ, V55, P359, DOI 10.1002-jemt.10003; Chung IH, 2003, P NATL ACAD SCI USA, V100, P405, DOI 10.1073-pnas.0133507100; Churchman LS, 2005, P NATL ACAD SCI USA, V102, P1419, DOI 10.1073-pnas.0409487102; Cognet L, 2000, APPL PHYS LETT, V77, P4052, DOI 10.1063-1.1332414; Cotlet M, 2001, J PHYS CHEM B, V105, P4999, DOI 10.1021-jp003813i; Cotlet M, 2001, P NATL ACAD SCI USA, V98, P14398, DOI 10.1073-pnas.251532698; Dedecker P, 2007, OPT EXPRESS, V15, P3372, DOI 10.1364-OE.15.003372; Dertinger T, 2007, CHEMPHYSCHEM, V8, P433, DOI 10.1002-cphc.200600638; Eggeling C, 1998, ANAL CHEM, V70, P2651, DOI 10.1021-ac980027p; Empedocles SA, 1999, NATURE, V399, P126; Enderlein J, 2004, CURR PHARM BIOTECHNO, V5, P155, DOI 10.2174-1389201043377020; Enderlein J, 2006, OPT EXPRESS, V14, P8111, DOI 10.1364-OE.14.008111; Enderlein J, 1999, CHEM PHYS LETT, V308, P263, DOI 10.1016-S0009-2614(99)00595-3; Enderlein J, 2005, CHEMPHYSCHEM, V6, P2324, DOI 10.1002-cphc.200500414; Enderlein J, 2005, J FLUORESC, V15, P415, DOI 10.1007-s10895-005-2633-0; Enderlein J, 2005, P SOC PHOTO-OPT INS, V5699, P167, DOI 10.1117-12.588527; Forkey JN, 2003, NATURE, V422, P399, DOI 10.1038-nature01529; Galletto R, 2006, NATURE, V443, P875, DOI 10.1038-nature05197; Garcia-Parajo MF, 2005, CHEMPHYSCHEM, V6, P819, DOI 10.1002-cphc.200400630; Gensch T, 2005, J PHYS CHEM A, V109, P6652, DOI 10.1021-jp0510847; Gersen H, 2000, PHYS REV LETT, V85, P5312, DOI 10.1103-PhysRevLett.85.5312; Gordon MP, 2004, P NATL ACAD SCI USA, V101, P6462, DOI 10.1073-pnas.0401638101; Gregor I, 2007, PHOTOCH PHOTOBIO SCI, V6, P13, DOI 10.1039-b610310c; Gregor I, 2005, CHEMPHYSCHEM, V6, P164, DOI 10.1002-cphc.200400319; Grey JK, 2005, ANGEW CHEM INT EDIT, V44, P6207, DOI 10.1002-anie.200501388; Grey JK, 2006, J PHYS CHEM B, V110, P18898, DOI 10.1021-jp057361r; Gronheid R, 2002, J AM CHEM SOC, V124, P2418, DOI 10.1021-ja017442a; Ha T, 1999, P NATL ACAD SCI USA, V96, P9077, DOI 10.1073-pnas.96.16.9077; Ha T, 2001, METHODS, V25, P78, DOI 10.1006-meth.2001.1217; Hammer NI, 2006, J PHYS CHEM B, V110, P14167, DOI 10.1021-jp062065f; Harms GS, 2001, BIOPHYS J, V80, P2396; Heilemann M, 2004, J AM CHEM SOC, V126, P6514, DOI 10.1021-ja049351u; Hess ST, 2002, BIOPHYS J, V83, P2300; Hou YW, 2002, J PHYS CHEM B, V106, P10306, DOI 10.1021-jp021200v; Hwang LC, 2006, BIOPHYS J, V91, P715, DOI 10.1529-biophysj.105.074120; Iino R, 2001, BIOPHYS J, V80, P2667; Jasny J, 1997, CHEM PHYS LETT, V273, P439, DOI 10.1016-S0009-2614(97)00621-0; KAHN F, 2002, CHEMPHYSCHEM, V3, P1005; Kapanidis AN, 2004, P NATL ACAD SCI USA, V101, P8936, DOI 10.1073-pnas.0401690101; Kapusta P, 2007, J FLUORESC, V17, P43, DOI 10.1007-s10895-006-0145-1; Kerssemakers J, 2006, P NATL ACAD SCI USA, V103, P15812, DOI 10.1073-pnas.0510400103; Kiel A, 2007, ANGEW CHEM INT EDIT, V46, P3363, DOI 10.1002-anie.200604965; Kreiter M, 2002, J CHEM PHYS, V117, P9430, DOI 10.1063-1.1515732; Kubitscheck U, 2000, BIOPHYS J, V78, P2170; Kuehn S., 2006, PHYS REV LETT, V97, DOI DOI 10.1103-PHYSREVLETT.97.017402; Kural C, 2005, SCIENCE, V308, P1469, DOI 10.1126-science.1108408; Lagerholm BC, 2006, BIOPHYS J, V91, P3050, DOI 10.1529-biophysj.105.079178; Lang E, 2005, CHEMPHYSCHEM, V6, P935, DOI 10.1002-cphc.200400555; Langer JD, 2008, TRAFFIC, V9, P597, DOI 10.1111-j.1600-0854.2007.00697.x; Lee NK, 2007, BIOPHYS J, V92, P303, DOI 10.1529-biophysj.106.093211; Lenne PF, 2002, APPL PHYS LETT, V80, P4106, DOI 10.1063-1.1483116; Li HT, 2006, J AM CHEM SOC, V128, P5711, DOI 10.1021-ja056997t; Lieb MA, 2004, J OPT SOC AM B, V21, P1210, DOI 10.1364-JOSAB.21.001210; Link S, 2006, PHYS REV LETT, V96, DOI 10.1103-PhysRevLett.96.017801; Lipman EA, 2003, SCIENCE, V301, P1233, DOI 10.1126-science.1085399; Lounis B, 2001, J PHYS CHEM B, V105, P5048, DOI 10.1021-jp010116x; Margolin G, 2006, J PHYS CHEM B, V110, P19053, DOI 10.1021-jp061487m; Moerner WE, 2003, REV SCI INSTRUM, V74, P3597, DOI 10.1063-1.1589587; NICOLET A, 2006, J CHEM PHYS, V124, P1; Noji H, 1997, NATURE, V386, P299, DOI 10.1038-386299a0; Palacios RE, 2006, J AM CHEM SOC, V128, P9028, DOI 10.1021-ja062848e; Park SJ, 2004, J AM CHEM SOC, V126, P4116, DOI 10.1021-ja031929x; Patra D., 2002, RES J CHEM ENVIRON, V6, P73; PATRA D, 2004, J APPL SPECTROS, V71, P307; Patra D., 2006, CHEM BIOCH FLUORESCE, V2, P139; Patra D, 2005, APPL PHYS LETT, V87, DOI 10.1063-1.2037194; Patra D, 2004, J PHYS CHEM A, V108, P6836, DOI 10.1021-jp048188m; Peterman EJG, 2004, ANNU REV PHYS CHEM, V55, P79, DOI 10.1146-annurev.physchem.55.091602.094340; Qu XH, 2004, P NATL ACAD SCI USA, V101, P11298, DOI 10.1073-pnas.0402155101; Ram S, 2006, P NATL ACAD SCI USA, V103, P4457, DOI 10.1073-pnas.0508047103; Rasnik I, 2006, NAT METHODS, V3, P891, DOI 10.1038-NMETH934; Ray K, 2006, J AM CHEM SOC, V128, P8998, DOI 10.1021-ja061762i; Roeffaers MBJ, 2006, NATURE, V439, P572, DOI 10.1038-nature04502; Rosenberg SA, 2005, ACCOUNTS CHEM RES, V38, P583, DOI 10.1021-ar040137k; Schaffer J, 1999, J PHYS CHEM A, V103, P331, DOI 10.1021-jp9833597; Schenk A, 2004, BIOPHYS J, V86, P384, DOI 10.1016-S0006-3495(04)74114-4; Schindler F, 2006, CHEM PHYS LETT, V428, P405, DOI 10.1016-j.cplett.2006.07.056; Schmidt T, 1996, P NATL ACAD SCI USA, V93, P2926, DOI 10.1073-pnas.93.7.2926; Schroeyers W, 2004, J AM CHEM SOC, V126, P14310, DOI 10.1021-ja0474603; Schuler B, 2002, NATURE, V419, P743, DOI 10.1038-nature01060; Semrau S, 2007, BIOPHYS J, V92, P613, DOI 10.1529-biophysj.106.092577; Sengupta P, 2002, METHODS, V27, P374, DOI 10.1016-S1046-2023(02)00096-8; Sengupta P, 2003, BIOPHYS J, V84, P1977; Sepiol J, 1997, CHEM PHYS LETT, V273, P444, DOI 10.1016-S0009-2614(97)00622-2; Shi J, 2006, P NATL ACAD SCI USA, V103, P5775, DOI 10.1073-pnas.0510482103; Shiroguchi K, 2007, SCIENCE, V316, P1208, DOI 10.1126-science.1140468; Sick B, 2000, PHYS REV LETT, V85, P4482, DOI 10.1103-PhysRevLett.85.4482; Sinha D, 2006, APPL PHYS LETT, V88, DOI 10.1063-1.2183358; Sonehara T, 2002, ANAL CHEM, V74, P5121, DOI 10.1021-ac0201326; Sonnleitner M, 1999, CHEM PHYS LETT, V300, P221, DOI 10.1016-S0009-2614(98)01330-X; Stevens BC, 2004, J CHEM PHYS, V120, P3030, DOI 10.1063-1.1640349; SUNA WY, 2002, J LUMIN, V98, P41; Tani T, 2004, J LUMIN, V107, P42, DOI 10.1016-j.jlumin.2003.12.001; Tinnefeld P, 2002, J AM CHEM SOC, V124, P14310, DOI 10.1021-ja027343c; Toprak E, 2007, NANO LETT, V7, P2043, DOI 10.1021-nl0709120; Toprak E, 2006, P NATL ACAD SCI USA, V103, P6495, DOI 10.1073-pnas.0507134103; Uji-i H, 2006, POLYMER, V47, P2511, DOI 10.1016-j.polymer.2005.11.094; Bout D. A. V., 1997, Science, V277, DOI 10.1126-science.277.5329.1074; Verbrugge S, 2007, BIOPHYS J, V92, P2536, DOI 10.1529-biophysj.106.093575; von der Hocht I, 2007, EXP MOL PATHOL, V82, P142, DOI 10.1016-j.yexmp.2006.12.009; Vosch T, 2001, ANGEW CHEM INT EDIT, V40, P4643, DOI 10.1002-1521-3773(20011217)40:244643::AID-ANIE46433.0.CO;2-N; Werley CA, 2006, J PHYS CHEM B, V110, P18939, DOI 10.1021-jp057570b; Widengren J, 2001, J PHYS CHEM A, V105, P6851, DOI 10.1021-jp010301a; Witkoskie JB, 2006, J PHYS CHEM B, V110, P19009, DOI 10.1021-jp061471w; Xie XS, 1999, J BIOL CHEM, V274, P15967, DOI 10.1074-jbc.274.23.15967; Xie Z, 2004, P NATL ACAD SCI USA, V101, P534, DOI 10.1073-pnas.2636333100; Yang H, 2003, SCIENCE, V302, P262, DOI 10.1126-science.1086911; Yang H, 2002, CHEM PHYS, V284, P423, DOI 10.1016-S0301-0104(02)00672-9; Yao J, 2005, P NATL ACAD SCI USA, V102, P14284, DOI 10.1073-pnas.0506523102; Yasuda R, 2003, P NATL ACAD SCI USA, V100, P9314, DOI 10.1073-pnas.1637860100; Yeow EKL, 2006, J PHYS CHEM A, V110, P1726, DOI 10.1021-jp055496r; Yildiz A, 2004, J BIOL CHEM, V279, P37223, DOI 10.1074-jbc.C400252200; Yildiz A, 2003, SCIENCE, V300, P2061, DOI 10.1126-science.1084398; Yildiz A, 2004, SCIENCE, V303, P676, DOI 10.1126-science.1093753; Yildiz A, 2005, ACCOUNTS CHEM RES, V38, P574, DOI 10.1021-ar040136s; Yu J, 2006, SCIENCE, V311, P1600, DOI 10.1126-science.1119623; Yu J, 2000, SCIENCE, V289, P1327, DOI 10.1126-science.289.5483.1327; Zander C., 2002, SINGLE MOL DETECTION; Zettl H, 2007, PHYS REV E, V75, DOI 10.1103-PhysRevE.75.061804; Zhuang XW, 2002, SCIENCE, V296, P1473, DOI 10.1126-science.106901355
Synchronous fluorescence based biosensor for albumin determination by cooperative binding of fluorescence probe in a supra-biomolecular host-protein assembly
No full textA synchronous fluorescence probe based biosensor for estimation of albumin with high sensitivity and selectivity was developed. Unlike conventional fluorescence emission or excitation spectral measurements, synchronous fluorescence measurement offered exclusively a new synchronous fluorescence peak in the shorter wavelength range upon binding of chrysene with protein making it an easy identification tool for albumin determination. The cooperative binding of a fluorescence probe, chrysene, in a supramolecular host-protein assembly during various albumin assessments was investigated. The presence of supramolecular host molecules such as β-cyclodextrin, curucurbit[6]uril or curucurbit[7]uril have little influence on sensitivity or limit of detection during albumin determination but reduced dramatically interference from various coexisting metal ion quenchers-enhancers. Using the present method the limit of detection for BSA and γ-Globulin was found to be 0.005 μM which is more sensitive than reported values. © 2009 Elsevier B.V. All rights reserved.Abraham W, 2002, J INCL PHENOM MACRO, V43, P159, DOI 10.1023-A:1021288303104; AGUIRRE MJ, 1987, J PHOTOCHEM, V36, P177, DOI 10.1016-0047-2670(87)87074-0; Babic N, 2006, CLIN CHEM, V52, P2155, DOI 10.1373-clinchem.2006.072892; BACZYNSKYJ L, 1994, RAPID COMMUN MASS SP, V8, P280, DOI 10.1002-rcm.1290080311; Bhasikuttan AC, 2007, ANGEW CHEM INT EDIT, V46, P4120, DOI 10.1002-anie.200604757; BORTOLUS P, 1996, ADV PHOTOCH, V21, P1; Busby Douglas E, 2004, J Clin Hypertens (Greenwich), V6, P8, DOI 10.1111-j.1524-6175.2004.04237.x; Chan OTM, 2006, CLIN CHEM, V52, P2141, DOI 10.1373-clinchem.2006.072801; Comper WD, 2005, ADV CHRONIC KIDNEY D, V12, P170, DOI 10.1053-j.ackd.2005.01.012; Diamond D, 1996, CHEM SOC REV, V25, P15, DOI 10.1039-cs9962500015; Hennig A, 2007, NAT METHODS, V4, P629, DOI 10.1038-NMETH1064; HIRAYAMA K, 1990, BIOCHEM BIOPH RES CO, V173, P639, DOI 10.1016-S0006-291X(05)80083-X; HIRAYAMA K, 1990, BIOCHEM BIOPH RES CO, V14, P173; HOLMES AS, 1993, BIOPHYS CHEM, V48, P193, DOI 10.1016-0301-4622(93)85010-F; Ikeda A, 1997, CHEM REV, V97, P1713, DOI 10.1021-cr960385x; KLEINPETER MA, 2007, CARDIOMETAB SYNDR, V2, P63; Koner AL, 2007, SUPRAMOL CHEM, V19, P55, DOI 10.1080-10610270600910749; MAIRQUEZ C, 2001, ANGEW CHEM INT EDIT, V40, P3155; Marquez C, 2004, J AM CHEM SOC, V126, P5806, DOI 10.1021-ja0319846; MASUHARA H, 1984, J PHYS CHEM-US, V88, P5868, DOI 10.1021-j150668a026; Meier MAR, 2005, CHEM COMMUN, P4610, DOI 10.1039-b505409e; Mohanty J, 2005, ANGEW CHEM INT EDIT, V44, P3750, DOI 10.1002-anie.200500502; Mohanty J, 2004, PHOTOCH PHOTOBIO SCI, V3, P1026, DOI 10.1039-b412936a; Mohanty J, 2006, J PHYS CHEM B, V110, P5132, DOI 10.1021-jp056411p; Mohanty J, 2007, CHEMPHYSCHEM, V8, P54, DOI 10.1002-cphc.200600625; NAKAMURA T, 1983, J PHYS CHEM-US, V87, P3122, DOI 10.1021-j100239a033; Nau WM, 2005, INT J PHOTOENERGY, V7, P133, DOI 10.1155-S1110662X05000206; Patra D., 2006, ENCY SENSORS, V2, P139; Patra D, 2009, TALANTA, V77, P1549, DOI 10.1016-j.talanta.2008.09.007; Patra D, 2001, TALANTA, V53, P783, DOI 10.1016-S0039-9140(00)00568-3; Patra D, 2002, ANAL BIOANAL CHEM, V373, P304, DOI 10.1007-s00216-002-1330-y; Patra D, 2000, ANALYST, V125, P1383, DOI 10.1039-b003876h; Patra D, 2000, ANAL LETT, V33, P2293, DOI 10.1080-00032710008543190; Patra D, 2002, TRAC-TREND ANAL CHEM, V21, P787, DOI 10.1016-S0165-9936(02)01201-3; Rankin MA, 2004, SUPRAMOL CHEM, V16, P513, DOI 10.1080-10610270412331283583; RUHN PF, 1994, ANAL CHEM, V66, P4265, DOI 10.1021-ac00095a023; Shaikh M, 2008, PHOTOCH PHOTOBIO SCI, V7, P408, DOI 10.1039-b715815g; Singh R, 2007, CLIN CHEM, V53, P540, DOI 10.1373-clinchem.2006.078832; Toto Robert D, 2004, J Clin Hypertens (Greenwich), V6, P2, DOI 10.1111-j.1524-6175.2004.4064.x; TUCKER SA, 1992, POLYCYCL AROMAT COMP, V3, P1, DOI 10.1080-10406639208048321; Wagner BD, 2003, J PHYS CHEM B, V107, P10741, DOI 10.1021-jp034891j; Wagner BD, 2001, CAN J CHEM, V79, P1101, DOI 10.1139-cjc-79-7-1101; Walcher W, 2003, J PROTEOME RES, V2, P534, DOI 10.1021-pr034034s; Wang LY, 2002, ANAL CHIM ACTA, V466, P87, DOI 10.1016-S0003-2670(02)00553-6; Zhang GA, 2003, ANAL BIOCHEM, V313, P327, DOI 10.1016-S0003-2697(02)00588-2; Zhang XY, 2002, J AM CHEM SOC, V124, P254, DOI 10.1021-ja011866n56
Synchronous fluorescence spectroscopic study of solvatochromic curcumin dye
No full textCurcumin, the main yellow bioactive component of turmeric, has recently acquired attention by chemists due its wide range of potential biological applications as an antioxidant, an anti-inflammatory, and an anti-carcinogenic agent. This molecule fluoresces weakly and poorly soluble in water. In this detailed study of curcumin in thirteen different solvents, both the absorption and fluorescence spectra of curcumin was found to be broad, however, a narrower and simple synchronous fluorescence spectrum of curcumin was obtained at Δλ = 10-20 nm. Lippert-Mataga plot of curcumin in different solvents illustrated two sets of linearity which is consistent with the plot of Stokes' shift vs. the E T30. When Stokes's shift in wavenumber scale was replaced by synchronous fluorescence maximum in nanometer scale, the solvent polarity dependency measured by λSFSmax vs. Lippert-Mataga plot or E T30 values offered similar trends as measured via Stokes' shift for protic and aprotic solvents for curcumin. Better linear correlation of λSFSmax vs. π* scale of solvent polarity was found compared to λabsmax or λemmax or Stokes' shift measurements. In Stokes' shift measurement both absorption-excitation as well as emission (fluorescence) spectra are required to compute the Stokes' shift in wavenumber scale, but measurement could be done in a very fast and simple way by taking a single scan of SFS avoiding calculation and obtain information about polarity of the solvent. Curcumin decay properties in all the solvents could be fitted well to a double-exponential decay function. © 2011 Elsevier B.V. All rights reserved.ALMOUSTAFA RM, 2009, J PHYS CHEM A, V113, P1235; Baglole KN, 2005, J PHOTOCH PHOTOBIO A, V173, P230, DOI 10.1016-j.jphotochem.2005.04.002; Barik A, 2003, PHOTOCHEM PHOTOBIOL, V77, P597, DOI 10.1562-0031-8655(2003)0770597:PSOBOC2.0.CO;2; Barik A, 2007, CHEM PHYS LETT, V436, P239, DOI 10.1016-j.cplett.2007.01.006; Bisht S., 2007, J NANOBIOTECHNOL, V5, P1; Chattopadhyay I, 2004, CURR SCI INDIA, V87, P44; CHIGNELL CF, 1994, PHOTOCHEM PHOTOBIOL, V59, P295, DOI 10.1111-j.1751-1097.1994.tb05037.x; Clifford NW, 2008, J MATER CHEM, V18, P162, DOI 10.1039-b715100d; Degheili JA, 2009, J PHYS CHEM A, V113, P1244, DOI 10.1021-jp8098363; Feng W, 2006, J FLUORESC, V16, P53; Galasso V, 2008, J PHYS CHEM A, V112, P2331, DOI 10.1021-jp7108303; JACQUES P, 1986, J PHYS CHEM-US, V90, P5535, DOI 10.1021-j100280a012; Jovanovic SV, 2001, J AM CHEM SOC, V123, P3064, DOI 10.1021-ja003823x; Jovanovic SV, 1999, J AM CHEM SOC, V121, P9677, DOI 10.1021-ja991446m; KAMLET MJ, 1977, J AM CHEM SOC, V99, P6027, DOI 10.1021-ja00460a031; KAMLET MJ, 1983, J ORG CHEM, V48, P2877, DOI 10.1021-jo00165a018; Khopde SM, 2000, PHOTOCHEM PHOTOBIOL, V72, P625, DOI 10.1562-0031-8655(2000)0720625:EOSOTE2.0.CO;2; Lakowicz J. R., 1999, PRINCIPLES FLUORESCE; Leung MHM, 2008, LANGMUIR, V24, P5672, DOI 10.1021-la800780w; Lippert E., 1957, ELECTROCHEMISTRY, V61, P962; Markov P., 1991, CHEM ENOLS, P69; MATAGA N, 1956, B CHEM SOC JPN, V29, P465, DOI 10.1246-bcsj.29.465; Patra D, 2009, TALANTA, V77, P1549, DOI 10.1016-j.talanta.2008.09.007; Patra D, 2001, TALANTA, V53, P783, DOI 10.1016-S0039-9140(00)00568-3; Patra D, 2002, ANAL BIOANAL CHEM, V373, P304, DOI 10.1007-s00216-002-1330-y; Patra D, 2000, ANALYST, V125, P1383, DOI 10.1039-b003876h; Patra D, 2000, ANAL LETT, V33, P2293, DOI 10.1080-00032710008543190; Patra D, 2002, TRAC-TREND ANAL CHEM, V21, P787, DOI 10.1016-S0165-9936(02)01201-3; Rankin MA, 2004, SUPRAMOL CHEM, V16, P513, DOI 10.1080-10610270412331283583; Reichardt C., 1988, SOLVENTS SOLVENT EFF; REICHARDT C, 1994, CHEM REV, V94, P2319, DOI 10.1021-cr00032a005; SHARMA OP, 1976, BIOCHEM PHARMACOL, V25, P1811, DOI 10.1016-0006-2952(76)90421-4; Shyamala T, 2006, CHEM PHYS, V330, P469, DOI 10.1016-j.chemphys.2006.09.018; SRIVASTAVA KC, 1995, PROSTAG LEUKOTR ESS, V52, P223, DOI 10.1016-0952-3278(95)90040-3; St Nikolov G., 1981, J PHOTOCH PHOTOBIO A, V16, P93, DOI 10.1016-0047-2670(81)80023-8; Subuddhi U, 2006, PHOTOCH PHOTOBIO SCI, V5, P459, DOI 10.1039-b600009f; Sun YM, 2002, ORG LETT, V4, P2909, DOI 10.1021-ol0262789; TONNESEN HH, 1985, Z LEBENSM UNTERS FOR, V180, P402, DOI 10.1007-BF01027775; Vemula PK, 2006, J AM CHEM SOC, V128, P8932, DOI 10.1021-ja062650u; Wang Y, 1997, TALANTA, V44, P1319, DOI 10.1016-S0039-9140(97)00028-330333
Going Beyond Counting First Authors in Author Co-citation Analysis
No full textThe present study examines one of the fundamental aspects of author co-citation analysis (ACA) - the way co-citation
counts are defined. Co-citation counting provides the data on which all subsequent statistical analyses and mappings
are based, and we compare ACA results based on two different types of co-citation counting - the traditional type that
only counts the first one among a cited work's authors on the one hand and a non-traditional type that takes into
account the first 5 authors of a cited work on the other hand. Results indicate that the picture produced through this non-traditional author co-citation counting contains more coherent author groups and is therefore considerably clearer. However, this picture represents fewer specialties in the research field being studied than that produced through the traditional first-author co-citation counting when the same number of top-ranked authors is selected and analyzed. Reasons for these effects are discussed
Measurement of the ratio of branching fractions B(B0→K∗0γ )/B(B0s→φγ ) and the directCP asymmetry inB 0→K∗0γ
No full textThe ratio of branching fractions of the radiative B decays B0→K⁎0γ and B0s→ϕγ has been measured using an integrated luminosity of 1.0 fb−1 of pp collision data collected by the LHCb experiment at a centre-of-mass energy of s√=7TeV. The value obtained is
B(B0→K⁎0γ)B(B0s→ϕγ)=1.23±0.06(stat.)±0.04(syst.)±0.10(fs/fd),
where the first uncertainty is statistical, the second is the experimental systematic uncertainty and the third is associated with the ratio of fragmentation fractions fs/fd. Using the world average value for B(B0→K⁎0γ), the branching fraction B(B0s→ϕγ) is measured to be (3.5±0.4)×10−5.
The direct CP asymmetry in B0→K⁎0γ decays has also been measured with the same data and found to be
ACP(B0→K⁎0γ)=(0.8±1.7(stat.)±0.9(syst.))%.
Both measurements are the most precise to date and are in agreement with the previous experimental results and theoretical expectations
Branching fraction and CP asymmetry of the decays B+→K0Sπ+ and B+→K0SK+
No full textAn analysis of B+ → K0
Sπ+ and B+ → K0
S K+ decays is performed with the LHCb experiment. The pp
collision data used correspond to integrated luminosities of 1 fb−1 and 2 fb−1 collected at centre-ofmass
energies of
√
s = 7 TeV and
√
s = 8 TeV, respectively. The ratio of branching fractions and the
direct CP asymmetries are measured to be B(B+ → K0
S K+
)/B(B+ → K0
Sπ+
) = 0.064 ± 0.009 (stat.) ±
0.004 (syst.), ACP(B+ → K0
Sπ+
) = −0.022 ± 0.025 (stat.) ± 0.010 (syst.) and ACP(B+ → K0
S K+
) =
−0.21 ± 0.14 (stat.) ± 0.01 (syst.). The data sample taken at
√
s = 7 TeV is used to search for
B+
c
→ K0
S K+ decays and results in the upper limit ( fc · B(B+
c
→ K0
S K+
))/( fu · B(B+ → K0
Sπ+
)) <
5.8 × 10−2 at 90% confidence level, where fc and fu denote the hadronisation fractions of a ¯b
quark
into a B+
c or a B+ meson, respectively
- …
