Phage Display, Peptide Production and Biological Assessment of Key Sequence of TGF-β1

Abstract

To isolate key sequences of transforming growth factor-beta 1 (TGF-β1) from the phage display 12-mer peptide library, synthesize the bioactive peptides, and evaluate their biological effects on fibroblasts. Using monoclonal anti-human TGF-β1 antibody as the target, a phage display 12-mer peptide library was screened to isolate target sequences. The key sequences of TGF-β1 were chosen through alignment analysis. Based on these sequences, bioactive peptides were produced. After being purified, structurally modified and fluorescence labeled, the peptides were added to the cultured fibroblasts. The effects of the biosynthesized peptides on fibroblasts were evaluated. Ten specific sequences similar to that of TGF-β1 were isolated from a phage display 12-mer peptide library. Seven key sequences were chosen to generate bioactive peptides of TGF-β1. Only one model peptide could bind to fibroblast and promote its proliferation. The result of quantitative real-time PCR analysis and Western blot analysis indicated the model peptide could promote both the mRNA expression and protein expression of TGF-β RII in fibroblasts. The key sequences of TGF-β1 can be screened from a phage display 12-mer peptide library. One of the bioactive peptides generated from the sequences can bind to and play biological effect on fibroblasts. The results are expected to help promoting wound healing.