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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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6432093 | PMC |
http://dx.doi.org/10.3390/polym9070276 | DOI Listing |
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