Affinity binding peptides were examined for surface fabrication of synthetic polymeric materials. Peptides possessing strong binding affinities toward polyurethane (PU) were discovered via biopanning of M13 phage peptide library. The apparent binding constant (Kapp) was as high as 2.68 × 109 M-1 with surface peptide density exceeded 1.8 g/cm2. Structural analysis showed that the ideal peptide had a high content (75%) of H-donor amino acid residues, and that intensified hydrogen bond interaction was the key driving force for the highly stable binding of peptides on PU. PU treated with such affinity peptides promises applications as low-fouling materials, as peptides increased its wettability and substantially reduced protein adsorption and cell adhesion. These results demonstrated a facile but highly efficient one-step strategy for surface property modification of polymeric materials for biotechnological applications.
Bibliographical noteFunding Information:
Wang thanks the University of Minnesota for support for sabbatical leave research.
This work was supported by National Natural Science Foundation of China [grant number 21303050], [grant number 31471659]; Tianhong Biotech Inc., and the Fundamental Research Funds for the Central Universities [grant number 13PJD012].
© 2015 © 2015 Taylor & Francis.
- affinity binding peptide
- interfacial interactions
- protein adsorption