1,721,002 research outputs found
Epoxysuccinyl peptide-derived cathepsin B inhibitors: Modulating membrane permeability by conjugation with the C-terminal heptapeptide segment of penetratin
Full text linkSchaschke N, Deluca D, Assfalg-Machleidt I, Hohneke C, Sommerhoff CP, Machleidt W. Epoxysuccinyl peptide-derived cathepsin B inhibitors: Modulating membrane permeability by conjugation with the C-terminal heptapeptide segment of penetratin. BIOLOGICAL CHEMISTRY. 2002;383(5):849-852
Calpastatin exon 1B-derived peptide, a selective inhibitor of calpain: Enhancing cell permeability by conjugation with penetratin
Full text linkGil-Parrado S, Assfalg-Machleidt I, Fiorino F, et al. Calpastatin exon 1B-derived peptide, a selective inhibitor of calpain: Enhancing cell permeability by conjugation with penetratin. BIOLOGICAL CHEMISTRY. 2003;384(3):395-402
beta-cyclodextrin/epoxysuccinyl peptide conjugates: new drug targeting system for tumor cells
No full textSchaschke N, Assfalg-Machleidt I, Machleidt W, Lassleben T, Sommerhoff CP, Moroder L. beta-cyclodextrin/epoxysuccinyl peptide conjugates: new drug targeting system for tumor cells. BIOORGANIC & MEDICINAL CHEMISTRY LETTERS. 2000;10(7):677-680
Epoxysuccinyl peptide-derived affinity labels for cathepsin B
No full textSchaschke N, Assfalg-Machleidt I, Lassleben T, Sommerhoff CP, Moroder L, Machleidt W. Epoxysuccinyl peptide-derived affinity labels for cathepsin B. FEBS LETTERS. 2000;482(1-2):91-96
Primed-site probing of papain-like cysteine proteases
No full textPfizer JM, Assfalg-Machleidt I, Machleidt W, Moroder L, Schaschke N. Primed-site probing of papain-like cysteine proteases. INTERNATIONAL JOURNAL OF PEPTIDE RESEARCH AND THERAPEUTICS. 2007;13(1-2):93-104
Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors
No full textSchaschke N, Assfalg-Machleidt I, Machleidt W, Moroder L. Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors. FEBS LETTERS. 1998;421(1):80-82
Inhibition of human mu-calpain by conformationally constrained calpastatin peptides
Full text linkPfizer J, Assfalg-Machleidt I, Machleidt W, Schaschke N. Inhibition of human mu-calpain by conformationally constrained calpastatin peptides. BIOLOGICAL CHEMISTRY. 2008;389(1):83-90.The 27-mer peptide CP1 B-[1-27] derived from exon 1B of calpastatin stands out among the known inhibitors for mu- and m-calpain due to its high potency and selectivity. By systematical truncation, a 20-mer peptide, CP1B-[4-23], was identified as the core sequence required to maintain the affinity/selectivity profile of CP1B-[1-27]. Starting with this peptide, the turn-like region Glu(10)(i)-Leu(11)(i+1)-Gly(12)(i+2)-Lys(13)(i +3) was investigated. Sequence alignment of subdomains 1B, 2B, 3B and 4B from different mammalians revealed that the amino acid residues in position i+1 and i+2 are almost invariably flanked by oppositely charged residues, pointing towards a turn-like conformation stabilized by salt bridge/H-bond interaction. Accordingly, using different combinations of acidic and basic residues in position i and i+3, a series of conformationally constrained variants of CP1 B-[4-23] were synthesized by macrolactamization utilizing the side chain functionalities of these residues. With the combination of Glu(i)/Dab(i+3), the maximum of conformational rigidity without substantial loss in affinity/selectivity was reached. These results clearly demonstrate that the linear peptide chain corresponding to subdomain 1B reverses its direction in the region Glu(10)-Lys(13) upon binding to mu-calpain, and thereby adopts a loop-like rather than a tight turn conformation at this site
Inhibition of cathepsin L by epoxysuccinyl peptides simultaneously addressing active-site and remote-site regions
No full textSchaschke N, Assfalg-Machleidt I, Machleidt W. Inhibition of cathepsin L by epoxysuccinyl peptides simultaneously addressing active-site and remote-site regions. CHEMBIOCHEM. 2008;9(11):1721-1724
The role of lysosomal cysteine proteinases as markers of macrophage activation and as non-specific mediators of inflammation
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