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Non‐sequential vasopressin peptides. Stereochemistry and biological activity
Author(s) -
Zaoral M.,
Bláha I.,
Budeĕšínský M.,
Machová A.,
Slaninová J.
Publication year - 2000
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/(sici)1099-1387(200003)6:3<123::aid-psc233>3.0.co;2-h
Subject(s) - uterotonic , chemistry , stereochemistry , peptide , amino acid , side chain , in vivo , vasopressin , cyclic peptide , biological activity , peptide synthesis , amino acid residue , antidiuretic , in vitro , biochemistry , peptide sequence , hormone , oxytocin , biology , organic chemistry , endocrinology , microbiology and biotechnology , gene , polymer
Two cyclic disulfides of structure tsqb">Cys‐Tyr‐Arg‐Arg‐Tyr‐C ys‐NH 2 ( 1 ) and tsqb">Cys‐Tyr(Me)‐Arg‐Arg‐Tyr(Me)‐C ys‐NH 2 ( 2 ), two nonapeptide derivatives of 1 extended at the C ‐terminal with Pro‐Arg‐Gly‐NH 2 ( 3 ) or Pro‐ D ‐Arg‐Gly‐NH 2 ( 4 ) and derivatives of 3 and 4 having Mpr in position 1, i.e. analogs ( 5 ) and ( 6 ), respectively, were synthesized, and their stereochemistry and biological activity were studied. All the peptides displayed low dose‐dependent uterotonic activity in vitro and antidiuretic activity in vivo . None of the peptides increased the blood pressure of the experimental animals. Compounds 2 , 4 and 6 showed a low inhibitory effect on AVP pressor activity; compound 6 , in addition, displays a significant and long‐lasting vasodepressor effect. NMR measurements indicated the existence of hydrogen bond between the amino acid residues in positions 2,5 and 3,4 of peptides 1 and 2 , and side‐chain interactions between amino acid residues in positions 2,3 and 4,5 of peptide 1 . No such side‐chain interactions were detected in peptide 2 . Copyright © 2000 European Peptide Society and John Wiley & Sons, Ltd.