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Distance between the basic group of the amino acid residue's side chain in position P1 of trypsin inhibitor CMTI-III and Asp189 in the substrate pocket of trypsin has an essential influence on the inhibitory activity.

Abstract：

:Three new analogues of trypsin inhibitor CMTI-III were synthesized by the solid-phase method: [Lys5]-CMTI-III, [Orn5]CMTI-III and [Dab5]CMTI-III. Only one analogue with L-lysine residue in position P1 showed inhibitory activity of the same order of magnitude as did wild CMTI-III. Two remaining analogues were completely inactive. A conclusion was drawn that the distance between the basic group of the amino acid residue's side chain in position P1 of the trypsin inhibitor CMTI-III and Asp189 in the substrate pocket of trypsin plays an essential role for the trypsin-inhibitor interaction.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Jaśkiewicz A,Lesner A,Rózycki J,Rodziewicz S,Rolka K,Ragnarsson U,Kupryszewski G

doi

10.1006/bbrc.1997.7752

subject

Has Abstract

pub_date

1997-11-26 00:00:00

pages

869-71

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(97)97752-4

journal_volume

240

pub_type

杂志文章

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