Year: 2021
Type: article
Abstract: High Resolution Image Download MS PowerPoint Slide Secondary structure formation differentiates polypeptides from most of the other synthetic polymers, and the transitions from random coils to rod-like α-helices or β-sheets represent an additional parameter to direct self-assembly and the morphology of nanostructures. We investigated the influence of distinct secondary structures on the self-assembly of reactive amphiphilic polypept(o)ides. The individual morphologies can be preserved by core cross-linking via chemoselective disulfide bond formation. A series of thiol-responsive copolymers of 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), and polysarcosine- block -poly( S -ethylsulfonyl- l -homocysteine) (pSar- b -p( l )Hcy) was prepared by N -carboxyanhydride polymerization. The secondary structure of the peptide segment varies from α-helices (pSar- b -p( l )Hcy) to antiparallel β-sheets (pSar- b -p( l )Cys) and disrupted β-sheets (pSar- b -p( dl )Cys). When subjected to nanoprecipitation, copolymers with antiparallel β-sheets display the strongest tendency to self-assemble, whereas disrupted β-sheets hardly induce aggregation. This translates to worm-like micelles, solely spherical micelles, or ellipsoidal structures, as analyzed by atomic force microscopy and cryogenic transmission electron microscopy, which underlines the potential of secondary structure-driven self-assembly of synthetic polypeptides.
Source: Biomacromolecules
Authors: Tobias A. Bauer, Jan Imschweiler, Christian Muhl, Benjamin Weber, Matthias Barz
Institutions: Leiden University, Johannes Gutenberg University Mainz
Language: English
Subfield: Organic Chemistry
Field: Chemistry
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $5,000
Funder: Deutsche Forschungsgemeinschaft
Award: G2684850905
OpenAlex ID: W3143926713