Model polypeptide of mussel adhesive protein. I. Synthesis and adhesive studies of sequential polypeptides (X-Tyr-Lys)n and (Y-Lys)n
2000; Wiley; Volume: 76; Issue: 6 Linguagem: Inglês
10.1002/(sici)1097-4628(20000509)76
ISSN1097-4628
AutoresHideki Tatehata, Akira Mochizuki, Toru Kawashima, Shuzo Yamashita, Hiroyuki Yamamoto,
Tópico(s)Marine Biology and Environmental Chemistry
ResumoJournal of Applied Polymer ScienceVolume 76, Issue 6 p. 929-937 Model polypeptide of mussel adhesive protein. I. Synthesis and adhesive studies of sequential polypeptides (X-Tyr-Lys)n and (Y-Lys)n Hideki Tatehata, Corresponding Author Hideki Tatehata Research and Development Center, Terumo Corporation, Inokuchi 1500, Nakai-machi, Ashigarakami-gun, Kanagawa 259-0151, JapanResearch and Development Center, Terumo Corporation, Inokuchi 1500, Nakai-machi, Ashigarakami-gun, Kanagawa 259-0151, Japan===Search for more papers by this authorAkira Mochizuki, Akira Mochizuki Research and Development Center, Terumo Corporation, Inokuchi 1500, Nakai-machi, Ashigarakami-gun, Kanagawa 259-0151, JapanSearch for more papers by this authorToru Kawashima, Toru Kawashima Research and Development Center, Terumo Corporation, Inokuchi 1500, Nakai-machi, Ashigarakami-gun, Kanagawa 259-0151, JapanSearch for more papers by this authorShuzo Yamashita, Shuzo Yamashita Research and Development Center, Terumo Corporation, Inokuchi 1500, Nakai-machi, Ashigarakami-gun, Kanagawa 259-0151, JapanSearch for more papers by this authorHiroyuki Yamamoto, Hiroyuki Yamamoto Institute of High Polymer Research, Faculty of Textile Science and Technology, Shinshu University, Tokida 3-15-1 Ueda-shi, Nagano 386-8567, JapanSearch for more papers by this author Hideki Tatehata, Corresponding Author Hideki Tatehata Research and Development Center, Terumo Corporation, Inokuchi 1500, Nakai-machi, Ashigarakami-gun, Kanagawa 259-0151, JapanResearch and Development Center, Terumo Corporation, Inokuchi 1500, Nakai-machi, Ashigarakami-gun, Kanagawa 259-0151, Japan===Search for more papers by this authorAkira Mochizuki, Akira Mochizuki Research and Development Center, Terumo Corporation, Inokuchi 1500, Nakai-machi, Ashigarakami-gun, Kanagawa 259-0151, JapanSearch for more papers by this authorToru Kawashima, Toru Kawashima Research and Development Center, Terumo Corporation, Inokuchi 1500, Nakai-machi, Ashigarakami-gun, Kanagawa 259-0151, JapanSearch for more papers by this authorShuzo Yamashita, Shuzo Yamashita Research and Development Center, Terumo Corporation, Inokuchi 1500, Nakai-machi, Ashigarakami-gun, Kanagawa 259-0151, JapanSearch for more papers by this authorHiroyuki Yamamoto, Hiroyuki Yamamoto Institute of High Polymer Research, Faculty of Textile Science and Technology, Shinshu University, Tokida 3-15-1 Ueda-shi, Nagano 386-8567, JapanSearch for more papers by this author First published: 14 March 2000 https://doi.org/10.1002/(SICI)1097-4628(20000509)76:6 3.0.CO;2-FCitations: 44Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Abstract The sequential polytripeptides and polydipeptides, (X-Tyr-Lys)n, (XGly, Ala, Pro, Ser, Leu, Ile, Phe), (Y-Lys)n, (YGly, Tyr), and (Gly-Tyr)n, which imitate a mussel adhesive protein, have been synthesized. The molecular weights of the polypeptides were estimated to be 7,200 ∼ 13,400 (19 ∼ 42 repeating units), and the polypeptides were found to have satisfactory amino acid sequences. The polypeptides were crosslinked by tyrosinase, and the optimal pH in the crosslinking reaction was 7.4 in the case of the polytripeptide, (Gly-Tyr-Lys)n. The optimal tyrosinase amount for the adhesive strength of (Gly-Tyr-Lys)n was 0.34 unit/mg (polypeptide) at pH 7.4. The shear adhesive strength of the polytripeptide increased with an increase in the polytripeptide concentration, and was not influenced by the third amino acid, X. The shear adhesive strengths of polytripeptides (X-Tyr-Lys)n were equal to one of the synthetic polydecapeptides, (Ala-Lys-Pro-Ser-Tyr-Pro-Pro-Thr-Tyr-Lys)n and (Gly-Pro-Lys-Thr-Tyr-Pro-Pro-Thr-Tyr-Lys)n which were the model polydecapeptides for blue mussel and Californian mussel, respectively. © 2000 John Wiley & Sons, Inc. J Appl Polym Sci 76: 929–937, 2000 Citing Literature Volume76, Issue69 May 2000Pages 929-937 RelatedInformation
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