Chemical Modification of Silk Fibroin through Serine Amino Acid Residues.

Abstract

Silk fibroin (SF) is a natural protein polymer and promising biomaterial. Chemical modifications have attracted growing interest in expanding SF applications. However, the majority of amino acid residues in SF are non-reactive and most of the reactive ones are in the crystalline region. Herein, a modification was conducted to investigate the possibility of direct modification on the surface of natural SF by a reagent with a mild reactivity, the type and quantity of the residues involved in the reactions, and the structural changes upon modification. Infrared spectrum, 1H NMR, titration and amino acid analyses, X-ray diffraction, and hemolysis test were used to analyze the materials. The results showed that sulfonic acid groups were grafted onto SF and the reaction occurred mainly at serine residues through hydroxyl groups. In total, 0.0958 mmol/g of residues participated in the modification with a modification efficiency of 7.6%. Moreover, the crystallinity and the content of β-sheet structure in SF increased upon modification. The modified material had good blood-compatibility. In conclusion, surface modification on native SF through serine residues was practicable and had the advantage of increased β-sheet structure. This will provide an alternative way for the modification of fibroin for the desired application in the biomedical field.