Identification and characterization of a novel heparin‐binding peptide for promoting osteoblast adhesion and proliferation by screening anEscherichia colicell surface display peptide library
作者:
Hyoun‐Ee Kim,
Hae‐Won Kim,
Jun‐Hyeog Jang,
期刊:
Journal of Peptide Science
(WILEY Available online 2009)
卷期:
Volume 15,
issue 1
页码: 43-47
ISSN:1075-2617
年代: 2009
DOI:10.1002/psc.1098
出版商: John Wiley&Sons, Ltd.
关键词: heparin;cell adhesion;titanium;BIAcore;osteoblast
数据来源: WILEY
摘要:
AbstractHeparin/heparan sulfate (HS) plays a key role in cellular adhesion. In this study, we utilized a 12‐mer randomEscherichia colicell surface display library to identify the sequence, which binds to heparin. Isolated insert analysis revealed a novel heparin‐binding peptide sequence, VRRSKHGARKDR, designated as HBP12. Our analysis of the sequence alignment of heparin‐binding motifs known as the Cardin–Weintraub consensus (BBXB, where B is a basic residue) indicates that the HBP12 peptide sequence contains two consecutive heparin‐binding motifs (i.e. RRSK and RKDR). SPR‐based BIAcore technology demonstrated that the HBP12 peptide binds to heparin with high affinity (KD= 191 nM). The HBP12 peptide is found to bind the cell surface HS expressed by osteoblastic MC3T3 cells and promote HS‐dependent cell adhesion. Moreover, the surface‐immobilized HBP12 peptide on titanium substrates shows significant increases in the osteoblastic MC3T3‐E1 cell adhesion and proliferation. Copyright © 2008 European Peptide Society and Jo
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