Potentially functional polypeptides for modification of biomaterials

Abstract

Event Abstract Back to Event Potentially functional polypeptides for modification of biomaterials Jiannan Wang1, Mingyang Wu1, Yunfei Liu1 and Fangfang Tu1 1 Soochow University, National Engineering Laboratory for Modern Silk, China Potentially functional polypeptides for modification of biomaterials Mingyang Wu, Yunfei Liu, Fangfang Tu, Jiannan Wang* National Engineering Laboratory for Modern Silk, College of Textile and Clothing Engineering, Soochow University, No. 199 Ren-ai Road, Suzhou Industrial Park, Suzhou, Jiangsu Province, 215123, China *Corresponding author: Jiannan Wang, wangjn@suda.edu.cn Silk fibroin is a native protein with regular amino acid sequence. Such as, Bombyx mori silk fibroin is composed of 12 repetitive and 11 non-repetitive regions, with the non-repetitive domain consisting of a hydrophilic polypeptide chain. The RGD tripeptides distribute in Antheraea yamamai and Antheraea pernyi silk fibroins up to 14 and 12 repeats, respectively. In order to determine the biomedical function of these typical peptides or potentially use them to modify materials, we cloned and extended a gene motif (f(1)) encoding the non-repetitive domain of Bombyx mori silk fibroin and a gene motif (-rgd-) encoding RGD-contained domain of Antheraea yamamai or Antheraea pernyi silk fibroins. These motif and their multimers were inserted into a glutathione S-transferase (GST)-tagged fusion-protein expression vector. Motif (f(1)) and multimers (f(4), f(8), (-rgd-)4, and (-rgd-)8) were expressed in Escherichia coli BL21 cells following isopropyl β-D-1-thiogalactopyranoside induction, purified by GST-affinity chromatography. All express products (GST-F(1), GST-F(4), GST-F(8), GST-(-RGD-)4, and GST-(-RGD-)8) were successfully expressed confirmed by SDS-PAGE, mass spectrometry (MS), amino acid composition and charge assay. The peptides F(1), F(4), F(8), (-RGD-)4, and (-RGD-)8 were all cleaved clearly from the GST-fusion tag following thrombin digestion. The molecular weight by MS, amino acid composition and isoelectric points of released peptides were all consistent with the predicted values. The peptides F(1), F(4), and F(8) were used to modify dacron membrane. Results showed F(1), F(4), and F(8) significantly improved water contact angle of dacron, and increased rapid adhesion and proliferation ability of cells. Cell adhesion and cell proliferation on (-RGD-)4 and (-RGD-)8 modified Bombyx mori silk fibroin films were better than that on unmodified film. The study indicated that the express products of F(1), F(4), and F(8) could improve the hydrophilicity of hydrophobe materials for better application in biomaterials. F(1), F(4), and F(8) exhibited a negative ζ-potential and the measured pI was about 3.3, 3.2 and 3.0, respectively, expecting to be used in vascular tissue engineering. The express products (-RGD-)4 and (-RGD-)8 could be used to modify cellular interface materials to improve cell adhesion and growth on materials surface. Acknowledgements This work was supported by National Natural Science Foundation of China (Nos. 51173125 and 51473108), Natural Science Foundation of Jiangsu Province of China (No. BK2012633), College Natural Science Research Project of Jiangsu Province of China (No. 12KJA43004). Refences [1] Y. X. Yang, H. Y. Huang, Z. F. Tian, et al. Textile Bioengineering and Informatics Symposium Proceedings, 2012, 70-75. [2] H. Y. Huang, Z. F. Tian, Y. X. Yang, et al. Journal of Donghua University (English Edition ), 2012, 29: 26-29. [3] H. R. Zhao, Y. X. Yang, H. G. Yi, et al. Bio-Medical Materials and Engineering, 2014, 24: 2057–2064. Conference: 10th World Biomaterials Congress, Montréal, Canada, 17 May - 22 May, 2016. Presentation Type: Poster Topic: Adhesive biomaterials Citation: Wang J, Wu M, Liu Y and Tu F (2016). Potentially functional polypeptides for modification of biomaterials. Front. Bioeng. Biotechnol. Conference Abstract: 10th World Biomaterials Congress. doi: 10.3389/conf.FBIOE.2016.01.02647 Copyright: The abstracts in this collection have not been subject to any Frontiers peer review or checks, and are not endorsed by Frontiers. They are made available through the Frontiers publishing platform as a service to conference organizers and presenters. The copyright in the individual abstracts is owned by the author of each abstract or his/her employer unless otherwise stated. Each abstract, as well as the collection of abstracts, are published under a Creative Commons CC-BY 4.0 (attribution) licence (https://creativecommons.org/licenses/by/4.0/) and may thus be reproduced, translated, adapted and be the subject of derivative works provided the authors and Frontiers are attributed. For Frontiers’ terms and conditions please see https://www.frontiersin.org/legal/terms-and-conditions. Received: 27 Mar 2016; Published Online: 30 Mar 2016. Login Required This action requires you to be registered with Frontiers and logged in. To register or login click here. Abstract Info Abstract The Authors in Frontiers Jiannan Wang Mingyang Wu Yunfei Liu Fangfang Tu Google Jiannan Wang Mingyang Wu Yunfei Liu Fangfang Tu Google Scholar Jiannan Wang Mingyang Wu Yunfei Liu Fangfang Tu PubMed Jiannan Wang Mingyang Wu Yunfei Liu Fangfang Tu Related Article in Frontiers Google Scholar PubMed Abstract Close Back to top Javascript is disabled. Please enable Javascript in your browser settings in order to see all the content on this page.