作者: Chikako Tanaka , Tetsuo Asakura
DOI: 10.1021/BM801439T
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摘要: New silk-like recombinant proteins, [(AAG)(6)ASTGRGDSPAAS](n) and [(AG)(9)ASTGRGDSPAAS](n), with high cell adhesive activities were designed produced from E. coli. These are proteins characteristic sequences the silk fibroin of a wild silkworm, Anaphe , region, including sequence RGD derived fibronectin. They showed higher adhesion activity than parent protein, without sequence. In addition, very similar to that collagen, which acted as positive control. Thus, it is demonstrated primary structure fibroin, composed largely alanine glycine residues, can be used platform for basic structures proteins. The structural characterization was performed (13)C CP/MAS NMR.