Stephens Jean S, Fahnestock Stephen R, Farmer Robin S, Kiick Kristi L, Chase D Bruce, Rabolt John F
Department of Materials Science and Engineering and Delaware Biotechnology Institute, University of Delaware, Newark, Delaware 19716, USA.
Biomacromolecules. 2005 May-Jun;6(3):1405-13. doi: 10.1021/bm049296h.
Micrometer and submicrometer diameter fibers of recombinant dragline spider silk analogues, synthesized via protein engineering strategies, have been electrospun from 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP) and compared with cast films via Raman spectroscopy in order to assess changes in protein conformation that may result from the electrospinning process. Although the solvent casting process was shown to result in predominantly beta-sheet conformation similar to that observed in the bulk, the electrospinning process causes a major change in conformation from beta-sheet to alpha-helix. A possible mechanism involving electric field-induced stabilization of alpha-helical segments in HFIP solution during the electrospinning process is discussed.
通过蛋白质工程策略合成的重组拖牵丝蜘蛛丝类似物的微米级和亚微米级直径纤维,已从1,1,1,3,3,3-六氟-2-丙醇(HFIP)中静电纺丝,并通过拉曼光谱与流延膜进行比较,以评估静电纺丝过程可能导致的蛋白质构象变化。尽管溶剂浇铸过程显示主要产生与在本体中观察到的类似的β-折叠构象,但静电纺丝过程导致构象从β-折叠主要转变为α-螺旋。讨论了一种可能的机制,该机制涉及在静电纺丝过程中电场诱导HFIP溶液中α-螺旋片段的稳定化。