Premium
Identifying and characterizing peptides that bind to specific heparan sulfate disaccharides
Author(s) -
Thomas Ajay,
Kramer Kenneth L
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.6.a1009-c
Subject(s) - surface plasmon resonance , chemistry , heparan sulfate , oligosaccharide , biochemistry , fibroblast growth factor , cell , peptide , computational biology , receptor , biology , nanotechnology , materials science , nanoparticle
Many cell‐cell signaling pathways that control early development are regulated by heparan sulfate (HS), an unbranched oligosaccharide chain that is composed of at least twenty‐four repeated disaccharides and is attached to most cell surfaces. Understanding the molecular mechanisms by which HS functions has been hindered by an inability to distinguish specific HS structures. The main objective of this project is to identify peptides that bind to specific disaccharides with the hope that we will be able to combine these peptides into longer polypeptide chains that can specifically bind to larger HS saccharides. We are screening a library of peptides to identify components that bind to disaccharides with high affinity and specificity. Several kinetics studies using Surface Plasmon Resonance (SPR) will be used to characterize these designed peptides on the basis of binding affinity and specificity. Control experiments are being conducted using HS hexasaccharide that is recognized by Fibroblast Growth Factor‐1 to test the efficacy of the gold surface functionalization and SPR technique. These peptides will be valuable reagents in probing the role of HS in mediating cell‐cell signaling. This research is supported by the Intramural Research Program of the NIH, NHLBI.