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BIOLOGICAL ACTIVITY OF SYNTHETIC POLYPEPTIDES WITH BRADYKININ‐LIKE PROPERTIES
Author(s) -
KONZETT H.,
STÜRMER E.
Publication year - 1960
Publication title -
british journal of pharmacology and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0366-0826
DOI - 10.1111/j.1476-5381.1960.tb00278.x
Subject(s) - bradykinin , chemistry , trypsin , biological activity , peptide , bradykinin receptor , amino acid , biochemistry , stereochemistry , enzyme , in vitro , receptor
The biological activity of synthetic polypeptides containing the amino acids of natural pure trypsin‐bradykinin and snake‐venom‐bradykinin has been investigated. A series of tests for bradykinin‐like activity in stimulating plain muscle, depressing the blood pressure and increasing capillary permeability was used on various species. A nonapeptide with the following structure: H‐L‐Arg‐L‐Pro‐L‐Pro‐Gly‐L‐Phe‐L‐Ser‐L‐Pro‐L‐Phe‐L‐Arg‐OH elicited qualitatively and quantitatively the effects of the pure natural bradykinins. An octapeptide with the following structure: H‐L‐Arg‐L‐Pro‐Gly‐L‐Phe‐L‐Ser‐L‐Pro‐L‐Phe‐L‐Arg‐OH also exerted bradykinin‐like effects but was 50 to 100 times less active than the nonapeptide. Three other octapeptides and a heptapeptide were without any significant effect. Further work will demonstrate if the nonapeptide A is synthetic bradykinin or a peptide with bradykinin‐like activity. Note added since submission of this paper: The data from this investigation were personally precommunicated to Elliott, Lewis, and Horton, who have since found that the structure of pure trypsin‐bradykinin is identical with the structure of the nonapeptide A. Therefore, this synthetic nonapeptide is in fact synthetic bradykinin.