Department of Chemistry, RCSI University of Medicine and Health Sciences, Dublin 2, Ireland.
Dutch-Belgian Beamline (DUBBLE), ESRF - The European Synchrotron Radiation Facility, CS 40220, Grenoble 38043 Cedex 9, France.
ACS Macro Lett. 2022 Mar 15;11(3):323-328. doi: 10.1021/acsmacrolett.1c00774. Epub 2022 Feb 16.
Statistical copolypeptides comprising lysine and tyrosine with unprecedented ion-induced gelation behavior are reported. Copolypeptides are obtained by one-step -carboxyanhydride (NCA) ring-opening polymerization. The gelation mechanism is studied by in situ SAXS analyses, in addition to optical spectroscopy and transmission electron microscopy (TEM). It is found that the gelation of these statistically polymerized polypeptides is due to the formation of stable intermolecular β-sheet secondary structures induced by the presence of salt ions as well as the aggregation of an α-helix between the copolypeptides. This behavior is unique to the statistical lysine/tyrosine copolypeptides and was not observed in any other amino acid combination or arrangement. Furthermore, the diffusion and mechanical properties of these hydrogels can be tuned through tailoring the polypeptide chain length and ion strength.
报告了一种具有赖氨酸和酪氨酸的统计共聚物，具有前所未有的离子诱导凝胶行为。共聚物通过一步 - 氰酸酯（NCA）开环聚合获得。通过原位小角 X 射线散射（SAXS）分析、光学光谱和透射电子显微镜（TEM）研究了凝胶化机制。结果发现，这些统计聚合多肽的凝胶化是由于盐离子存在诱导形成稳定的分子间β-折叠二级结构以及共聚物之间α-螺旋的聚集。这种行为是统计赖氨酸/酪氨酸共聚物所特有的，在任何其他氨基酸组合或排列中都没有观察到。此外，可以通过调整多肽链长度和离子强度来调节这些水凝胶的扩散和机械性能。
