Antioxidant Activity of Silk Peptide and Co-initiation Behavior in Free Radical Photopolymerization of Acrylamide

다국어 초록 (Multilingual Abstract)

A water-soluble silk peptide (SP) was fractioned to a series of SP fractions with different molecular weight. Theantioxidant activity of these fractions was investigated by the ABTS and DPPH assays, and the co-initiating ability of eachfraction in type II photoinitiator was evaluated in photopolymerization of acrylamide, using camphorquinone as thesensitizer. Gel permeation chromatograph was used to investigate molecular weight distributions of SP fractions. The resultsshowed that with the increase of the proportion of the component with molecular weight of about 200 in SP fractions,antioxidant activity and co-initiation ability became poor. Four essential amino acids, Ala, Gly, Ser and Tyr of SP and theirrespective pentapeptides were also assessed for these two functions. Among them, pentatyrosine exhibited the most excellentperformance in two functions, which might be ascribed to its excellent electron/hydrogen donation capability. Andpentaglycine had good behavior in these two functions, suggesting that the polypeptide chain was responsible for electron/hydrogen donation. By 1H NMR analysis, it was speculated that the photoinitiation active center was located on themethylene group of pentaglycine. The electron/hydrogen donor of SP is the inherent reason for antioxidant function andphotoinitiation performance of SP.

참고문헌 (Reference)

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