Department of Chemistry and Biochemistry, Magnetic Resonance Research Center, Arizona State University, Tempe, Arizona 85287-1604, USA.
Biomacromolecules. 2010 Jan 11;11(1):192-200. doi: 10.1021/bm9010672.
Synthetic spider silk holds great potential for use in various applications spanning medical uses to ultra lightweight armor; however, producing synthetic fibers with mechanical properties comparable to natural spider silk has eluded the scientific community. Natural dragline spider silks are commonly made from proteins that contain highly repetitive amino acid motifs, adopting an array of secondary structures. Before further advances can be made in the production of synthetic fibers based on spider silk proteins, it is imperative to know the percentage of each amino acid in the protein that forms a specific secondary structure. Linking these percentages to the primary amino acid sequence of the protein will establish a structural foundation for synthetic silk. In this study, nuclear magnetic resonance (NMR) techniques are used to quantify the percentage of Ala, Gly, and Ser that form both beta-sheet and helical secondary structures. The fraction of these three amino acids and their secondary structure are quantitatively correlated to the primary amino acid sequence for the proteins that comprise major and minor ampullate silk from the Nephila clavipes spider providing a blueprint for synthetic spider silks.
合成蛛丝在医学用途到超轻装甲等各种应用中具有巨大的潜力；然而，生产出机械性能可与天然蛛丝相媲美的合成纤维一直困扰着科学界。天然牵引丝蛛丝通常由含有高度重复的氨基酸模体的蛋白质组成，采用一系列二级结构。在进一步推进基于蛛丝蛋白的合成纤维生产之前，必须知道形成特定二级结构的蛋白质中每种氨基酸的百分比。将这些百分比与蛋白质的一级氨基酸序列联系起来，将为合成丝建立一个结构基础。在这项研究中，使用核磁共振（NMR）技术来定量确定形成β-折叠和螺旋二级结构的 Ala、Gly 和 Ser 的百分比。这三种氨基酸的分数及其二级结构与构成主要和次要壶腹丝的蛋白质的一级氨基酸序列定量相关，为合成蛛丝提供了蓝图。
