Functionalized resorcinarenes effectively disrupt the aggregation of αA66-80 crystallin peptide related to cataracts.

ABSTRACT: Cataracts, an eye lens clouding disease, are debilitating and while operable, remain without a cure. αA66-80 crystallin peptide abundant in cataracted eye lenses contributes to aggregation of αA-crystallin protein leading to cataracts. Inspired by the versatility of macrocycles and programmable guest selectivity through discrete functionalizations, we report on three water-soluble ionic resorcinarene receptors (A, B, and C) that disrupt the aggregation of αA66-80 crystallin peptide. A and B each possess four anionic sulfonate groups, while C includes four cationic ammonium groups with four flexible extended benzyl groups. Through multiple non-covalent attractions, these receptors successfully disrupt and reverse the aggregation of αA66-80 crystalli

SUBMITTER: Twum K 

PROVIDER: S-EPMC8672818 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature