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
Biopolymersjournal_title
Biopolymersauthors
Rullo A,Nitz Mdoi
10.1002/bip.21339subject
Has Abstractpub_date
2010-03-01 00:00:00pages
290-8issue
3eissn
0006-3525issn
1097-0282journal_volume
93pub_type
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