The design, synthesis, and characterization of tight-binding inhibitors of calmodulin.

Abstract:

:Based on a consideration of the probable structure of calmodulin and some natural peptides known to interact with it, two calmodulin-binding peptides were designed. These peptides bind to calmodulin in helical conformations and are capable of forming electrostatic and hydrophobic interactions with calmodulin. Their dissociation constants for binding (less than or equal to 210 and 400 pM) place them as the tightest-binding inhibitors of calmodulin thus far reported. The study of the interactions of these and similar peptides with calmodulin will provide valuable insights into the mechanisms whereby calmodulin binds to target enzymes, and it also serves as an excellent model system for exploring the physical chemistry of protein-protein interaction.

journal_name

J Cell Biochem

authors

DeGrado WF,Prendergast FG,Wolfe HR Jr,Cox JA

doi

10.1002/jcb.240290204

subject

Has Abstract

pub_date

1985-01-01 00:00:00

pages

83-93

issue

2

eissn

0730-2312

issn

1097-4644

journal_volume

29

pub_type

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