Importance of the spatial display of charged residues in heparin-peptide interactions.

Abstract:

:Many studies have examined consensus sequences required for protein-glycosaminoglycan interactions. Through the synthesis of helical heparin binding peptides, this study probes the relationship between spatial arrangement of positive charge and heparin binding affinity. Peptides with a linear distribution of positive charge along one face of the alpha-helix had the highest affinity for heparin. Moving the basic residues away from a single face resulted in drastic changes in heparin binding affinity of up to three orders of magnitude. These findings demonstrate that amino acid sequences, different from the known heparin binding consensus sequences, will form high affinity protein-heparin binding interactions when the charged residues are aligned linearly.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Rullo A,Nitz M

doi

10.1002/bip.21339

subject

Has Abstract

pub_date

2010-03-01 00:00:00

pages

290-8

issue

3

eissn

0006-3525

issn

1097-0282

journal_volume

93

pub_type

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