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Synthesis and diuretic activities of pseudoproline‐containing analogues of the insect kinin core pentapeptide
Author(s) -
Zhang Bo,
Gong Junbin,
Yang Yinliang,
Dong Shouliang
Publication year - 2011
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1396
Subject(s) - thiazolidine , chemistry , pentapeptide repeat , stereochemistry , peptide bond , peptide , carboxylic acid , population , biochemistry , medicine , environmental health
C‐2 dimethylated/unmethylated thiazolidine‐4‐carboxylic acid and C‐2 dimethylated oxazolidine‐4‐carboxylic acid were introduced into the insect kinin core pentapeptide in place of Pro 3 , yielding three new analogues. NMR analysis revealed that the peptide bond of Phe 2 ‐pseudoproline (ΨPro) 3 is practically 100% in cis conformation in the case of dimethylated pseudoproline‐containing analogues, about 50% cis for the thiazolidine‐4‐carboxylic acid analogue and about 33% cis for the parent Pro 3 peptide. The diuretic activities are consistent with the population of cis conformation of the Phe 2 ‐ΨPro 3 /Pro 3 peptide bonds, and the results confirm a cis Phe‐Pro bond as bioactive conformation. Copyright © 2011 European Peptide Society and John Wiley & Sons, Ltd.