Characterization of heparan sulfate N-sulfated domains binding fibroblast growth factor-2.

摘要

We have screened a heparan sulfate library for hexasaccharides that have the ability to bind FGF2 using SEC. Hexasaccharides originating from internal NS domains constitute 99percent of the library compositions. Only the highly sulfated compositions are enriched in the bound fraction at 100mM salt concentration. However, non-reducing end (NRE) hexasaccharides constituting only 1percent of the library compositions are enriched to 10percent of binding oligosaccharides. NRE oligosaccharides are the major oligosaccharides that remain bound after a higher salt concentration wash (200mM) and constitute 73percent of the high affinity bound fraction. This suggest that the NRE dp6 have high affinity to FGF2. SEC and mass spectrometry show that the ratio of binding of FGF2 to internal and NRE NS domains of degree of polymerization 6 is 1:1 .