- A Facile Synthesis of NODASA-Functionalized Peptide
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Herein, we report a mild and efficient synthesis of a NODASA-functionalized peptide, which was initiated with a Michael addition reaction between monomethyl fumarate and 1,4,7-triazacyclononane.
- Dutta, Jyotibon,Chinthakindi, Praveen K.,Arvidsson, Per I.,De La Torre, Beatriz G.,Kruger, Hendrik G.,Govender, Thavendran,Naicker, Tricia,Albericio, Fernando
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- Increased stability of peptidesulfonamide peptidomimetics towards protease catalyzed degradation
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Replacement of amide bonds in peptides by sulfonamide moieties resulted in peptidosulfonamides with an increased stability towards protease catalyzed degradation. In addition to protection of the protease cleavage site, it was found that introduction of a sulfonamide also influenced the stability of adjacent amide bonds. Copyright (C) 1999 Elsevier Science Ltd.
- De Bont, Dries B.A.,Sliedregt-Bol, Karen M.,Hofmeyer, Lovina J. F.,Liskamp, Rob M. J.
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p. 1043 - 1047
(2007/10/03)
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- SPECIFICITY AND MOLECULAR PROPERTIES OF PENICILLOLYSIN, A METALLOPROTEINASE FROM PENICILLUM CITRINUM
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The specificity and mode of action of penicillolysin, a metalloproteinase from Penicillum citrinum, were investigated with several bioactive-oligopeptides.The enzyme showed a high affinity toward the Pro-X (X = Gln, Lys, Leu or Arg) bonds of substance P, dynorphin A (1-13), neurotensin and chicken brain pentapeptide, and the R-R bonds in dynorphin A and neurotensin.Preferential cleavages of bonds by the enzyme with hydrophobic amino acid residues at the P1 position were observed on the peptides used.The specificity of penicillolysin differs from that of other metallopropteinases.The Mr and pI were determined as 18000 and 9.6, respectively.The first 50 amino acids in the N-terminal region were TKETCSNASRKSALEKALSNTVKLANAAATAARSGSASKFSEYEKTTSSS.CD spectra on the hollo- and apo-enzymes of penicillolysin were studied.
- Yamaguchi, Megumi,Hanzawa, Satoshi,Hirano, Ken-Ichi,Yamagata, Youhei,Ichishima, Eiji
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p. 1317 - 1322
(2007/10/02)
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