The repeating decapeptides of the mussel adhesive protein (MAP) were considered as the basis for mussel adhesion in wet environment for it contains L-3, 4-dihydroxyphenylalanine (DOPA). However, DOPA residue in the Perna viridis foot protein-1 (Pvfp-1) do not exist in the repeating decapeptide sequence but present in the non-repeating region. Therefore, it is quite necessary to evaluate the adhesive capacity of the repeating and non-repeating regions of Pvfp-1. In this study, the sequence of eight repeating decapeptides (R-240) and the sequence of the non-repeating region (C-237) of Pvfp-1 was amplified and expressed, respectively. With adsorption, adhesion and coating analysis, it was found that the recombinant C-237 has comparable adhesion and coating ability compared with that of Cell-Tak™ (the positive control) and it was also much better than that of R-240, especially on the non-adhesive PTFE surface. Moreover, C-237 exhibited no cytotoxicity and showed better cell adhesion and spreading abilities than that of R-240 on both glass and PTFE surfaces. Therefore, the recombinant C-237 could be used as bioadhesive for medical purpose and be potentially used as an improver for bio-inert materials when applied in biomedical areas.
A novel recombinant bioadhesive designed from the non-repeating region of Perna viridis foot protein-1
- 期刊:Materials Science & Engineering C-Materials for Biological Applications
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