© 2017 by the authors. Licensee MDPI, Basel, Switzerland. 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.
Piedra-Arroni, E., Makni, F., Severac, L., Stigliani, J. L., Pratviel, G., & Bonduelle, C. (2017). Smart poly(imidazoyl-L-lysine) Synthesis and reversible helix-to-coil transition at neutral pH. Polymers, 9(7). https://doi.org/10.3390/polym9070276