Structural requirements of bioactive peptides for interaction with endopeptidase 22.19.

Abstract:

:A series of biologically active peptides and related compounds (opioid peptides, neurotensin, and bradykinin) were used as substrates or competitive inhibitors to study the structural requirements for peptide interaction with endopeptidase 22.19. The kinetics of hydrolysis of these peptides indicated that, in contrast to other proteases, the substrate specificity of endopeptidase 22.19 is not determined by the amino acids flanking the sensitive bonds of the substrates. The competition between bioactive peptide analogues and the quenched fluorescence substrate of endopeptidase 22.19 indicated that their length and their flexibility may be the dominant factors to explain their binding specificities. These peculiar features of endopeptidase 22.19 may be of importance to understand the physiological processes of conversion and inactivation of biologically active peptides.

journal_name

Neuropeptides

journal_title

Neuropeptides

authors

Camargo AC,Gomes MD,Toffoletto O,Ribeiro MJ,Ferro ES,Fernandes BL,Suzuki K,Sasaki Y,Juliano L

doi

10.1016/0143-4179(94)90083-3

subject

Has Abstract

pub_date

1994-04-01 00:00:00

pages

281-7

issue

4

eissn

0143-4179

issn

1532-2785

pii

0143-4179(94)90083-3

journal_volume

26

pub_type

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