Coordination to Zn species can be reversibly used to control the helix-to-coil transition of synthetic poly(l-glutamic acid) polymers at a neutral pH of 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.
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