1,721,039 research outputs found
Commentary: Single-molecule fluorescence spectroscopy
No full text[No abstract available]Arbour TJ, 2010, LAB CHIP, V10, P1286, DOI 10.1039-b924594d; Blank K., 2011, SINGLE MOL SPECTROSC, P495; Chizhik A, 2009, PHYS REV LETT, V102, DOI 10.1103-PhysRevLett.102.073002; Dertinger T, 2009, P NATL ACAD SCI USA, V106, P22287, DOI 10.1073-pnas.0907866106; Goldsmith RH, 2010, NAT CHEM, V2, P179, DOI [10.1038-nchem.545, 10.1038-NCHEM.545]; Jain A, 2011, NATURE, V473, P484, DOI 10.1038-nature10016; Patra D, 2008, CURR CHEM BIOL, V2, P267, DOI 10.2174-187231308785739783; Patra D, 2008, APPL SPECTROSC REV, V43, P389, DOI 10.1080-05704920802108115; Yasuda M, 2012, PHYS CHEM CHEM PHYS, V14, P345, DOI 10.1039-c1cp22207d; Zhang RB, 2011, NANO LETT, V11, P4074, DOI 10.1021-nl201225r0
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
Application of synchronous fluorescence scan spectroscopy for size dependent simultaneous analysis of CdTe nanocrystals and their mixtures
No full textIn this paper, synchronous fluorescence scan (SFS) spectroscopy has been applied for the first time for the simultaneous determination of a mixture of CdTe fluorescent nanocrystals (NCs) of various sizes without a pre-separation step. It is observed that synchronous fluorescence maximum correlates well with the size of the nanocrystals, i.e.; the λSFSmax is useful to determine size dependency of NCs. Synchronous fluorescence maximum along with the second derivative can identify individual NCs in a mixture in water. The method is found to be simple, sensitive, selective and fast for NCs determination in aqueous media. © 2008 Elsevier B.V. All rights reserved.Alivisatos AP, 1996, SCIENCE, V271, P933, DOI 10.1126-science.271.5251.933; Somers RC, 2007, CHEM SOC REV, V36, P579, DOI 10.1039-b517613c; BLANCO CC, 1995, TALANTA, V42, P1037, DOI 10.1016-0039-9140(95)01506-7; CAPITAN F, 1992, TALANTA, V39, P21, DOI 10.1016-0039-9140(92)80045-F; Chen M, 2007, MATER CHEM PHYS, V101, P317, DOI 10.1016-j.matchemphys.2006.06.003; Dong WT, 2003, OPT MATER, V22, P227, DOI 10.1016-S0925-3467(02)00269-0; Dyadyusha L, 2005, CHEM COMMUN, P3201, DOI 10.1039-b500664c; Eychmuller A, 2000, J PHYS CHEM B, V104, P6514, DOI 10.1021-jp9943676; Falcon SG, 1996, TALANTA, V43, P659; Hardman R, 2006, ENVIRON HEALTH PERSP, V114, P165, DOI 10.1289-ehp.8284; Huang CP, 2008, SENSOR ACTUAT B-CHEM, V130, P338, DOI 10.1016-j.snb.2007.08.021; Kapitonov AM, 1999, J PHYS CHEM B, V103, P10109, DOI 10.1021-jp9921809; Konstantianos DG, 1996, ANALYST, V121, P909, DOI 10.1039-an9962100909; Lannoo M, 1996, J LUMIN, V70, P170, DOI 10.1016-0022-2313(96)00053-1; Masala O, 2004, ANNU REV MATER RES, V34, P41, DOI 10.1146-annurev.matsci.34.052803.090949; PANADERO S, 1993, TALANTA, V40, P225, DOI 10.1016-0039-9140(93)80326-M; Patra D, 2001, TALANTA, V55, P143, DOI 10.1016-S0039-9140(01)00404-0; Patra D, 2005, APPL PHYS LETT, V87, DOI 10.1063-1.2037194; 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, 2002, ANAL CHIM ACTA, V454, P209, DOI 10.1016-S0003-2670(01)01568-9; Patra D, 2002, TRAC-TREND ANAL CHEM, V21, P787, DOI 10.1016-S0165-9936(02)01201-3; Singh S, 2007, J NANOSCI NANOTECHNO, V7, P3048, DOI 10.1166-jnn.2007.922; Sondi I, 2004, J COLLOID INTERF SCI, V275, P503, DOI 10.1016-j.jcis.2004.02.005; VOSSMEYER T, 1994, J PHYS CHEM-US, V98, P7665, DOI 10.1021-j100082a044; Yamashita I, 2004, CHEM LETT, V33, P1158, DOI 10.1246-cl.2004.1158; Zheng J, 2004, PHYS REV LETT, V93, DOI 10.1103-PhysRevLett.93.07740219202
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
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
Acridine orange and silica nanoparticles facilitated novel robust fluorescent hollow microcapsules toward DNA bio-sensor
No full textTuning optical properties by nanotechnology has become a topic of larger interest as these materials can be of extraordinary sensitivity, selectivity and robustness toward sensing applications. Here we report novel fluorescent hollow microcapsules via congregation of poly (l-lysine) interceded by silica nanoparticles and acridine orange. Scanning tunneling microscope images confirm spherical nature of microcapsules with size of 1-3μm. The hollow structures are verified by fluorescent images, which indicate acridine orange is intermingled in the shell wall of the microcapsules. The excitation fluorescence spectra reveal that acridine orange exists in monomeric and aggregated form within the microcapsules. But at pH 8.5, monomeric acridine orange diffuses out of microcapsules. Association of acridine orange with poly (l-lysine) and SiO2 nanoparticles in monomeric or aggregated form does not limit intercalation of acridine orange with DNA. Thus, the acridine orange based fluorescent hollow microcapsule could easily sense DNA in 100ngmL-1 concentration ranges. The excited state lifetime of fluorescent hollow microcapsules is shorter than acridine orange in neutral form, which further establishes a strong association of acridine orange with poly (l-lysine). However, the excited state lifetime is marginally quenched in the presence of DNA but independent of DNA concentration that rules out the possibility of intercalation in the excited state rather than a ground state complex formation. © 2013 .Ahmad H., 2013, J COLLOID SCI BIOTEC, V2, P153; Amali AJ, 2011, ANAL CHIM ACTA, V708, P75, DOI 10.1016-j.aca.2011.10.001; Amali AJ, 2012, CHEM COMMUN, V48, P856, DOI 10.1039-c1cc15209b; Bagaria HG, 2011, J MATER CHEM, V21, P9454, DOI 10.1039-c1jm10712g; Bi SY, 2006, SENSOR ACTUAT B-CHEM, V119, P199, DOI 10.1016-j.snb.2005.12.014; Boal AK, 2000, NATURE, V404, P746; BRUN AM, 1992, J AM CHEM SOC, V114, P3656, DOI 10.1021-ja00036a013; Carmona P.A.O., 2013, J COLLOID SCI BIOTEC, V2, P130; Connors KA., 1987, BINDING CONSTANTS ME; Du H, 1998, PHOTOCHEM PHOTOBIOL, V68, P141, DOI 10.1111-j.1751-1097.1998.tb02480.x; Kitazawa N, 2011, J MATER SCI, V46, P2036, DOI 10.1007-s10853-010-5035-x; Luchowski R, 2003, CHEM PHYS, V293, P155, DOI 10.1016-S0301-0104(03)00301-X; Lyles MB, 2002, BIOPHYS CHEM, V96, P53, DOI 10.1016-S0301-4622(02)00036-4; Manju S, 2011, COLLOID SURFACE B, V82, P588, DOI 10.1016-j.colsurfb.2010.10.021; Mann S, 1996, NATURE, V382, P313, DOI 10.1038-382313a0; Medintz IL, 2005, NAT MATER, V4, P435, DOI 10.1038-nmat1390; MURRAY CB, 1995, SCIENCE, V270, P1335, DOI 10.1126-science.270.5240.1335; Patra D, 2009, TALANTA, V77, P1549, DOI 10.1016-j.talanta.2008.09.007; 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; Rahman MM, 2012, J MATER CHEM, V22, P1173, DOI 10.1039-c1jm13882k; Ribeiro L. F. V., 2013, J COLLOID SCI BIOTEC, V2, P78; Shaikh M, 2008, PHOTOCH PHOTOBIO SCI, V7, P408, DOI 10.1039-b715815g; Shenhar R, 2003, ACCOUNTS CHEM RES, V36, P549, DOI 10.1021-ar020083j; Veyret R, 2005, J MAGN MAGN MATER, V293, P171, DOI 10.1016-j.jmmm.2005.01.057; Vitzthum F, 1999, ANAL BIOCHEM, V276, P59, DOI 10.1006-abio.1999.4298; Whitesides GM, 2002, P NATL ACAD SCI USA, V99, P4769, DOI 10.1073-pnas.082065899; Wong MS, 2002, NANO LETT, V2, P583, DOI 10.1021-nl020244c0
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. 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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. 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Fluorometric sensing of DNA using curcumin encapsulated in nanoparticle-assembled microcapsules prepared from poly(diallylammonium chloride-co-sulfur dioxide)
No full textWe report on the synthesis of microcapsules (MCs) containing self-assembled nanoparticles formed from poly[diallylammonium chloride-co-(sulfur dioxide)] in the presence of citrate and silica sol nanoparticles. The MCs are spherical, and SEM and optical microscopy reveal them to have micrometer size. The fluorescent probe curcumin was encapsulated in the MCs and found to be located in the shell. The fluorescence of curcumin in the MCs is altered depending on their microenvironment. Effects of pH and ammonia on the fluorescence of curcumin in the MCs also were studied. The brightness of the probe in the MCs increases on addition of DNA. The effect was used to determine DNA from fish sperm by fluorometry. The association constant (K) is 4 000 mL. g-1, and the number of binding sites is ~1. 0. © 2012 Springer-Verlag Wien.Amali AJ, 2011, ANAL CHIM ACTA, V708, P75, DOI 10.1016-j.aca.2011.10.001; Amali AJ, 2012, CHEM COMMUN, V48, P856, DOI 10.1039-c1cc15209b; AMMON HPT, 1991, PLANTA MED, V57, P1, DOI 10.1055-s-2006-960004; Ausubel FM, 1998, CURRENT PROTOCOLS MO, pA3D1; Bagaria HG, 2011, J MATER CHEM, V21, P9454, DOI 10.1039-c1jm10712g; Boal AK, 2000, NATURE, V404, P746; Connors KA., 1987, BINDING CONSTANTS ME; Gong H, 2012, MICROCHIM ACTA, V177, P95, DOI 10.1007-s00604-011-0754-5; Hassenkam T, 2002, ADV MATER, V14, P1126, DOI 10.1002-1521-4095(20020816)14:161126::AID-ADMA11263.0.CO;2-A; KARSTEN U, 1977, ANAL BIOCHEM, V77, P464, DOI 10.1016-0003-2697(77)90259-7; Lao Christopher D, 2006, BMC Complement Altern Med, V6, P10, DOI 10.1186-1472-6882-6-10; Mann S, 1996, NATURE, V382, P313, DOI 10.1038-382313a0; MURRAY CB, 1995, SCIENCE, V270, P1335, DOI 10.1126-science.270.5240.1335; 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, 2011, SPECTROCHIM ACTA A, V79, P1823, DOI 10.1016-j.saa.2011.05.064; Patra D, 2012, INT J BIOL MACROMOL, V50, P885, DOI 10.1016-j.ijbiomac.2012.02.010; Patra D, 2012, PHOTOCHEM PHOTOBIOL, V88, P317, DOI 10.1111-j.1751-1097.2011.01067.x; Patra D, 2009, J MATER CHEM, V19, P4017, DOI 10.1039-b822358k; Pizzo P, 2010, J CELL MOL MED, V14, P970, DOI 10.1111-j.1582-4934.2009.00681.x; QURESHI S, 1992, PLANTA MED, V58, P124, DOI 10.1055-s-2006-961412; Shen L, 2007, SPECTROCHIM ACTA A, V67, P619, DOI 10.1016-j.saa.2006.08.018; Shenhar R, 2003, ACCOUNTS CHEM RES, V36, P549, DOI 10.1021-ar020083j; Shishodia S, 2007, CURR PROB CANCER, V31, P243, DOI 10.1016-j.currproblcancer.2007.04.001; Singer VL, 1997, ANAL BIOCHEM, V249, P228, DOI 10.1006-abio.1997.2177; Sugiyama Y, 1996, BIOCHEM PHARMACOL, V52, P519, DOI 10.1016-0006-2952(96)00302-4; Tanious A, 1992, BIOCHEMISTRY-US, V31, P3103; Vitzthum F, 1999, ANAL BIOCHEM, V276, P59, DOI 10.1006-abio.1999.4298; Whitesides GM, 2002, P NATL ACAD SCI USA, V99, P4769, DOI 10.1073-pnas.082065899; Wong MS, 2002, NANO LETT, V2, P583, DOI 10.1021-nl020244c; Yang FS, 2005, J BIOL CHEM, V280, P5892, DOI 10.1074-jbc.M40475120077
Ionic liquid expedites partition of curcumin into solid gel phase but discourages partition into liquid crystalline phase of 1,2-dimyristoyl-sn- glycero-3-phosphocholine liposomes
No full textThe hydrolysis of curcumin in alkaline and neutral buffer conditions is of interest because of the therapeutic applicability of curcumin. We show that hydrolysis of curcumin can be remarkably suppressed in 1,2-dimyristoyl-sn- glycero-3-phosphocholine (DMPC) liposomes. The fluorescence of curcumin sensitively detects the phase transition temperature of liposomes. However, at greater concentrations, curcumin affects the phase transition temperature, encouraging fusion of two membrane phases. The interaction of curcumin with DMPC is found to be strong, with a partition coefficient value of Kp = 2.78 × 105 in the solid gel phase, which dramatically increases in the liquid crystalline phase to Kp = 1.15 × 106. The importance of ionic liquids as green solvents has drawn interest because of their toxicological effect on human health; however, the impact of ionic liquids (ILs) on liposomes is not yet understood. The present study establishes that ILs such as 1-methyl-3-octylimidazolium chloride (moic) affect the permeability and fluidity of liposomes and thus influence parition of curcumin into DMPC liposomes, helping in the solid gel phase but diminishing in the liquid crystalline phase. The Kp value of curcumin does not change appreciably with moic concentration in the solid gel state but decreases with moic concentration in the liquid crystalline phase. Curcumin, a rotor sensitive to detect phase transition temperature, is applied to investigate the influence of ionic liquids such as 1-methyl-3-octylimidazolium chloride, 1-buytl-3-methyl imadazolium tetrafluoroborate, and 1-benzyl-3-methyl imidazolium tetrafluoroborate on DMPC liposome properties. 1-Methyl-3-octylimidazolium chloride lowers the phase transition temperature, but 1-buytl-3-methyl imidazolium tetrafluoroborate and 1-benzyl-3-methyl imidazolium tetrafluoroborate do not perceptibly modify the phase transition temperature; rather, they broaden the phase transition. © 2013 American Chemical Society.Aggarwal BB, 2009, INT J BIOCHEM CELL B, V41, P40, DOI 10.1016-j.biocel.2008.06.010; Anderson JL, 2003, CHEM COMMUN, P2444, DOI 10.1039-b307516h; Wang YJ, 1997, J PHARMACEUT BIOMED, V15, P1867, DOI 10.1016-S0731-7085(96)02024-9; Barry J, 2009, J AM CHEM SOC, V131, P4490, DOI 10.1021-ja809217u; Basniwal R.K., 2011, J AGR FOOD CHEM, V59, P2056; Bernabe-Pineda M, 2004, SPECTROCHIM ACTA A, V60, P1091, DOI 10.1016-S1386-1425(03)00342-1; Bisht S., 2007, J NANOBIOTECHNOL, V5, P1; Bisht S, 2010, MOL CANCER THER, V9, P2255, DOI 10.1158-1535-7163.MCT-10-0172; CHAPMAN D., 1967, CHEM PHYS LIPIDS, V1, P445, DOI 10.1016-0009-3084(67)90023-0; CHIGNELL CF, 1994, PHOTOCHEM PHOTOBIOL, V59, P295, DOI 10.1111-j.1751-1097.1994.tb05037.x; Fletcher KA, 2004, LANGMUIR, V20, P33, DOI 10.1021-la035596t; Fletcher KA, 2003, J PHYS CHEM B, V107, P13532, DOI 10.1021-jp0276754; Funston AM, 2007, J PHYS CHEM B, V111, P4963, DOI 10.1021-jp068298o; Galinski M, 2006, ELECTROCHIM ACTA, V51, P5567, DOI 10.1016-j.electacta.2006.03.016; Gardikis K, 2006, THERMOCHIM ACTA, V447, P1, DOI 10.1016-j.tca.2006.03.007; Heimburg T, 2000, BIOPHYS J, V78, P1154; HUANG ZJ, 1991, BIOCHEM BIOPH RES CO, V181, P166, DOI 10.1016-S0006-291X(05)81396-8; Hung WC, 2008, BIOPHYS J, V94, P4331, DOI 10.1529-biophysj.107.126888; Ingolfsson HI, 2007, BIOCHEMISTRY-US, V46, P10384, DOI 10.1021-bi701013n; Iwata K, 2007, J PHYS CHEM B, V111, P4914, DOI 10.1021-jp067196v; Jacob A, 2013, IMMUNOLOGY, V139, P328, DOI 10.1111-imm.12079; Lee YK, 2009, J AGR FOOD CHEM, V57, P305, DOI 10.1021-jf802737z; Leung MHM, 2008, LANGMUIR, V24, P5672, DOI 10.1021-la800780w; Li N, 2007, CHEMPHYSCHEM, V8, P2211, DOI 10.1002-cphc.200700382; Lin YG, 2007, CLIN CANCER RES, V13, P3423, DOI 10.1158-1078-0432.CCR-06-3072; Lu JM, 2009, PROG POLYM SCI, V34, P431, DOI 10.1016-j.progpolymsci.2008.12.001; Luo SC, 2008, CHINESE SCI BULL, V53, P1337, DOI 10.1007-s11434-007-0526-0; Mishra A, 2009, ANGEW CHEM INT EDIT, V48, P2474, DOI 10.1002-anie.200804709; Miskolczy Z, 2004, CHEM PHYS LETT, V400, P296, DOI 10.1016-j.cplett.2004.10.127; Mohapatra M, 2011, J PHYS CHEM B, V115, P9962, DOI 10.1021-jp1123212; 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, 2012, PHOTOCHEM PHOTOBIOL, V88, P317, DOI 10.1111-j.1751-1097.2011.01067.x; Paul A, 2007, J PHYS CHEM B, V111, P1957, DOI 10.1021-jp067481e; 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; Seddon KR, 2002, GREEN CHEM, V4, pG25, DOI 10.1039-b202711a; SHARMA OP, 1976, BIOCHEM PHARMACOL, V25, P1811, DOI 10.1016-0006-2952(76)90421-4; Shobini J, 2000, SPECTROCHIM ACTA A, V56, P2239, DOI 10.1016-S1386-1425(00)00308-5; Shyamala T, 2004, PHOTOCHEM PHOTOBIOL, V80, P309, DOI 10.1562-2004-03-07-RA-104.1; SRIMAL RC, 1973, J PHARM PHARMACOL, V25, P447; Sugiyama Y, 1996, BIOCHEM PHARMACOL, V52, P519, DOI 10.1016-0006-2952(96)00302-4; Sujatha J, 1998, LANGMUIR, V14, P2256, DOI 10.1021-la9702749; Tonnesen HH, 2002, PHARMAZIE, V57, P820; TONNESEN HH, 1985, Z LEBENSM UNTERS FOR, V180, P402, DOI 10.1007-BF01027775; Wasserscheid P., 2003, IONIC LIQUIDS SYNTHE; Welton T, 1999, CHEM REV, V99, P2071, DOI 10.1021-cr980032t; Yallapu MM, 2010, J COLLOID INTERF SCI, V351, P19, DOI 10.1016-j.jcis.2010.05.022; Yang FS, 2005, J BIOL CHEM, V280, P5892, DOI 10.1074-jbc.M404751200; Yang J, 2010, MED ONCOL, V27, P1114, DOI 10.1007-s12032-009-9344-3; Yang SC, 2009, MATER LETT, V63, P1465, DOI 10.1016-j.matlet.2009.03.042; Zhang CY, 2013, BIOTECHNOL LETT, V35, P995, DOI 10.1007-s10529-013-1173-y34
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