Secondary Structure-Driven Self-Assembly of Thiol-Reactive Polypept(o)ides.

摘要: Secondary structure formation differentiates polypeptides from most of the other synthetic polymers, and transitions random coils to rod-like α-helices or β-sheets represent an additional parameter direct self-assembly morphology nanostructures. We investigated influence distinct secondary structures on reactive amphiphilic polypept(o)ides. The individual morphologies can be preserved by core cross-linking via chemoselective disulfide bond formation. A series thiol-responsive copolymers racemic polysarcosine-block-poly(S-ethylsulfonyl-dl-cysteine) (pSar-b-p(dl)Cys), enantiopure polysarcosine-block-poly(S-ethylsulfonyl-l-cysteine) (pSar-b-p(l)Cys), polysarcosine-block-poly(S-ethylsulfonyl-l-homocysteine) (pSar-b-p(l)Hcy) was prepared N-carboxyanhydride polymerization. peptide segment varies antiparallel (pSar-b-p(l)Cys) disrupted (pSar-b-p(dl)Cys). When subjected nanoprecipitation, with display strongest tendency self-assemble, whereas hardly induce aggregation. This translates worm-like micelles, solely spherical ellipsoidal structures, as analyzed atomic force microscopy cryogenic transmission electron microscopy, which underlines potential structure-driven polypeptides.