Ontology highlight
ABSTRACT:
SUBMITTER: Piedra-Arroni E
PROVIDER: S-EPMC6432093 | biostudies-literature | 2017 Jul
REPOSITORIES: biostudies-literature
Piedra-Arroni Estefania E Makni Fatma F Severac Laura L Stigliani Jean-Luc JL Pratviel Geneviève G Bonduelle Colin C
Polymers 20170711 7
Polypeptide polymers can adopt natural protein secondary structures such as α-helices or β-sheets, and this unique feature is at the origin of some intriguing physico⁻chemical properties. In this work, we present how side chain imidazoylation of a poly(l-lysine) scaffold affords the preparation of poly(histidine) counterparts exhibiting α-helix conformation. This structuring behavior is reversible and can be controlled by means of pH and or temperature changes. ...[more]