Morelli M A, DeBiasi M, DeStradis A, Tamburro A M
Department of Chemistry, Universita' della Basilicata, Potenza, Italy.
J Biomol Struct Dyn. 1993 Aug;11(1):181-90. doi: 10.1080/07391102.1993.10508716.
Synthetic VGGVG, a "monomeric" unit of the glycine-rich regions of elastin, has been investigated for its molecular and supramolecular properties. In aqueous solution the pentapeptide showed conformational features strongly concentration-dependent. CD and NMR studies suggested a partial unfolding on increasing the concentration. Electron microscopy, on the other hand, evidenced extensive aggregation of the pentapeptide yielding elastin-like supramolecular structures constituted either by twisted ropes or by banded fibrils.
合成的VGGVG是弹性蛋白富含甘氨酸区域的“单体”单元，已对其分子和超分子性质进行了研究。在水溶液中，该五肽显示出强烈依赖于浓度的构象特征。圆二色光谱（CD）和核磁共振（NMR）研究表明，随着浓度增加会发生部分解折叠。另一方面，电子显微镜证明该五肽会大量聚集，形成由扭曲的绳索或带状纤维构成的类弹性蛋白超分子结构。
