| Title | Importance of the spatial display of charged residues in heparin-peptide interactions. | | Author(s) | Rullo A, Nitz M | | Institution | Department of Chemistry, University of Toronto, Toronto, ON, Canada, M5S 3H6. | | Source | Biopolymers 2009 Nov 2. | | 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 3 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. (c) 2009 Wiley Periodicals, Inc. Biopolymers, 2009. | | Language | ENG | | Pub Type(s) | JOURNAL ARTICLE
| | PubMed ID | 19885920 |
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