NEXAFS STUDIES OF ORIENTATION IN ADSORBED PEPTIDE & PROTEIN FILMS

吸附肽方向的 NEXAFS 研究

• 批准号: 6345044
• 负责人: DAVID G CASTNER
• 金额: $ 4.54万
• 依托单位: UNIVERSITY OF WASHINGTON
• 依托单位国家: 美国
• 财政年份: 2000
• 资助国家: 美国
• 起止时间: 2000-09-01 至 2001-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6345044
• 关键词: animal tissue; bioengineering /biomedical engineering; biomaterials; biomedical resource; health care; hematology; medical rehabilitation related tag; prosthesis; proteins

Engineering the next generation of biomaterials with the specific surface biorecognition sites needed to improve healing requires developing surface analysis methods to characterize these materials. Recent studies have shown near edge X-ray absorption fine structure (NEXAFS) is an excellent technique for characterizing the structure and orientation of self-assembled monolayers (SAMs), adsorbed peptides, and adsorbed protein films. Studies in the coming year will focus on improving our ability to quantify the orientation of adsorbed peptides and proteins and understanding how substrate properties (roughness, composition, etc.) effect peptide and protein orientation. Alpha-helix and beta-sheet peptides were found to adsorb onto highly-ordered, rubbed poly(tetrafluoroethylene) (PTFE) substrates with their helical axis (alpha-helix) and backbone (beta-sheet) parallel to the substrate. In contrast, neither peptide exhibited significant ordering when adsorbed onto diso rdered, RF GD-deposited fluoropolymer surfaces. NEXAFS results from adsorbed protein films show that orientation of their peptide backbone is only observed for non-gobular proteins (fibrinogen, fibronectin, etc.). The relationship between PTFE structural parameters (FCF bond angle, helix unwinding, helix stretching, etc.) and NEXAFS spectra have been determined with theoretical calculations.

利用特定的技术设计下一代生物材料 改善愈合所需的表面生物识别部位需要 开发表面分析方法来表征这些材料。 最近的研究表明，近边X射线吸收精细结构 (NEXAFS)是表征结构的优秀技术 和吸附的自组装单分子膜(SAM)的取向 多肽和吸附蛋白质膜。来年的研究将会 专注于提高我们量化吸附取向的能力 多肽和蛋白质，并了解底物特性 (粗糙度、成分等)效应肽和蛋白质定位。 发现α-螺旋和β-折叠多肽可以吸附在 高度有序的摩擦聚四氟乙烯(PTFE)基板 及其螺旋轴(阿尔法螺旋)和主干(贝塔表) 与衬底平行。相反，两种多肽都没有表现出 吸附在DISSERED、RF Gd沉积上时的显著有序性 含氟聚合物表面。NEXAFS由吸附的蛋白质膜引起 表明它们的肽骨架的取向仅在 非肾小球蛋白(纤维蛋白原、纤维连接蛋白等)。两国关系 在聚四氟乙烯结构参数(FCF键合角度、螺旋展开、 螺旋伸展等)和NEXAFS光谱都是用 理论计算。