Identification and characterization of a novel heparin‐binding peptide for promoting osteoblast adhesion and proliferation by screening an Escherichia coli cell surface display peptide library |
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Authors: | Hyoun‐Ee Kim Hae‐Won Kim Jun‐Hyeog Jang |
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Institution: | 1. School of Materials Science and Engineering, Seoul National University, Seoul 151‐742, Republic of Korea;2. Department of Biomaterial Science and Institute of Tissue Regeneration Engineering, Dankook University School of Dentistry, Cheonan 330‐714, Republic of Korea;3. Department of Biochemistry, Inha University School of Medicine, Incheon 400‐712, Republic of Korea |
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Abstract: | Heparin/heparan sulfate (HS) plays a key role in cellular adhesion. In this study, we utilized a 12‐mer random Escherichia coli cell 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 John Wiley & Sons, Ltd. |
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Keywords: | heparin cell adhesion titanium BIAcore osteoblast |
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