Multivalent Elastin-Like Glycopolypeptides: Subtle Chemical Structure Modifications with High Impact on Lectin Binding Affinity

Marie Rosselin (1, 2) , Zoeisha S. Chinoy (1, 2) , Lourdes Mónica Bravo-Anaya (1, 2) , Sébastien Lecommandoux (1, 2) , Elisabeth Garanger (1, 2)

1 LCPO - Laboratoire de Chimie des Polymères Organiques
2 Team 3 LCPO : Polymer Self-Assembly & Life Sciences

A library of synthetic elastin-like glycopolypeptides were synthesized and screened by microscale thermophoresis to identify key structural parameters affecting lectin binding efficacy. While polypeptide backbone size and glycovalency were found to have little influence, the presence of a linker at the anomeric position of galactose and the absence of positive charge on the polypeptide residue holding the sugar unit were found to be critical for the binding to RCA120.

Mots clés: Elastin-like polypeptides (ELPs); saccharides; glycoconjugates; chemoselective modifications; macromolecular click chemistry; lectins

Domaines: Polymères; Biotechnologies

Marie Rosselin, Zoeisha S. Chinoy, Lourdes Mónica Bravo-Anaya, Sébastien Lecommandoux, Elisabeth Garanger. Multivalent Elastin-Like Glycopolypeptides: Subtle Chemical Structure Modifications with High Impact on Lectin Binding Affinity. ACS Macro Letters, 2021, 10 (1), pp.65-70. ⟨10.1021/acsmacrolett.0c00775⟩. ⟨hal-03100778⟩