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Polymers (Basel) ; 9(7)2017 Jul 11.
Artículo en Inglés | MEDLINE | ID: mdl-30970954

RESUMEN

Polypeptide polymers can adopt natural protein secondary structures such as α-helices or ß-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.

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