{"title":"丝质生物材料的设计灵感来自于贻贝黏附蛋白。","authors":"Mingying Yang, Kazuo Yamauchi, Masato Kurokawa, Tetsuo Asakura","doi":"10.1089/ten.2006.0448","DOIUrl":null,"url":null,"abstract":"<p><p>To develop biomaterials for tissue engineering, a silk-like protein inspired by mussel-adhesive proteins (MAPs) was designed and prepared. The primary structure of this silk-like protein is designed as TS[AKPSYPPTYKAS (GAGAGS)(3)](10) by combining the sequences (GAGAGS)(3), the crystalline region of Bombyx mori silk fibroin, and AKPSYPPTYK, the adhesive sequence of MAP from Mytilus edulis. This protein was synthesized by the genetic engineering method. Solid-state (13)C NMR spectra showed that this silk-like protein adopts flexible conformation due to introduction of the sequence AKPSYPPTYK. Cell assay indicated that this silk-like protein has significantly higher cell adhesion activities in response to normal human dermal fibroblasts (NHDFs) than Pronectin F, which is available as commercialized cell-adhesive silk-like protein. Thus, combination of remarkably high cell-adhesive activity from MAP with superiority of silk fibroin provides potentiality for application to the field of biomaterials.</p>","PeriodicalId":23102,"journal":{"name":"Tissue engineering","volume":" ","pages":"2941-7"},"PeriodicalIF":0.0000,"publicationDate":"2007-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1089/ten.2006.0448","citationCount":"26","resultStr":"{\"title\":\"Design of silk-like biomaterials inspired by mussel-adhesive protein.\",\"authors\":\"Mingying Yang, Kazuo Yamauchi, Masato Kurokawa, Tetsuo Asakura\",\"doi\":\"10.1089/ten.2006.0448\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>To develop biomaterials for tissue engineering, a silk-like protein inspired by mussel-adhesive proteins (MAPs) was designed and prepared. The primary structure of this silk-like protein is designed as TS[AKPSYPPTYKAS (GAGAGS)(3)](10) by combining the sequences (GAGAGS)(3), the crystalline region of Bombyx mori silk fibroin, and AKPSYPPTYK, the adhesive sequence of MAP from Mytilus edulis. This protein was synthesized by the genetic engineering method. Solid-state (13)C NMR spectra showed that this silk-like protein adopts flexible conformation due to introduction of the sequence AKPSYPPTYK. Cell assay indicated that this silk-like protein has significantly higher cell adhesion activities in response to normal human dermal fibroblasts (NHDFs) than Pronectin F, which is available as commercialized cell-adhesive silk-like protein. Thus, combination of remarkably high cell-adhesive activity from MAP with superiority of silk fibroin provides potentiality for application to the field of biomaterials.</p>\",\"PeriodicalId\":23102,\"journal\":{\"name\":\"Tissue engineering\",\"volume\":\" \",\"pages\":\"2941-7\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2007-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1089/ten.2006.0448\",\"citationCount\":\"26\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Tissue engineering\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1089/ten.2006.0448\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Tissue engineering","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1089/ten.2006.0448","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Design of silk-like biomaterials inspired by mussel-adhesive protein.
To develop biomaterials for tissue engineering, a silk-like protein inspired by mussel-adhesive proteins (MAPs) was designed and prepared. The primary structure of this silk-like protein is designed as TS[AKPSYPPTYKAS (GAGAGS)(3)](10) by combining the sequences (GAGAGS)(3), the crystalline region of Bombyx mori silk fibroin, and AKPSYPPTYK, the adhesive sequence of MAP from Mytilus edulis. This protein was synthesized by the genetic engineering method. Solid-state (13)C NMR spectra showed that this silk-like protein adopts flexible conformation due to introduction of the sequence AKPSYPPTYK. Cell assay indicated that this silk-like protein has significantly higher cell adhesion activities in response to normal human dermal fibroblasts (NHDFs) than Pronectin F, which is available as commercialized cell-adhesive silk-like protein. Thus, combination of remarkably high cell-adhesive activity from MAP with superiority of silk fibroin provides potentiality for application to the field of biomaterials.