Sequence-structure characterization of recombinant polypeptides derived from silk fibroin heavy chain.

Abstract

The molecular conformation of a biomedical material plays a major role in the stability, bioactivity and controlled release of drugs. In order to identify the impact of fragments derived from Bombyx mori silk fibroin on their structures and to develop a new strategy for controlling drug release, we designed several hydrophobic-hydrophilic recombinants (GS16F1, GS16F4, and GS16F8), and investigated their molecular conformations and conformational changes induced by different storage temperatures and pH values. The results showed that the α-helix characteristic peaks were prominent in the fresh freeze-dried powder with increasing F1 repeats. During storage at 4°C, 37°C or 60°C, the β-turns (especially in GS16F8) and α-helixes turned into β-sheets. The β-sheet content in the polypeptides increased with increasing temperature and F1 repeats. Following induction by different pH values, their molecular conformations changed significantly, but not the same as that of powder storage. The content of β-sheets was GS16F1>GS16F4>GS16F8 near the isoelectric point of each polypeptide. With increasing pH value, the β-sheet content of GS16F1 decreased more slowly compared with GS16F4 and GS16F8. These results were satisfactory for structural regulation in the field of drug controlled release research.