Unraveling Determinants of Affinity Enhancement in Dimeric Aptamers for a Dimeric Protein.

ABSTRACT: High-affinity aptamers can be derived de novo by using stringent conditions in SELEX (Systematic Evolution of Ligands by EXponential enrichment) experiments or can be engineered post SELEX via dimerization of selected aptamers. Using electrophoretic mobility shift assays, we studied a series of heterodimeric and homodimeric aptamers, constructed from two DNA aptamers with distinct primary sequences and secondary structures, previously isolated for VEGF-165, a homodimeric protein. We investigated four factors envisaged to impact the affinity of a dimeric aptamer to a dimeric protein: (1) length of the linker between two aptamer domains, (2) linking orientation, (3) binding-site compatibility of two component aptamers in a heterodimeric aptamer, and (4) steric acceptability of the two identi

SUBMITTER: Manochehry S 

PROVIDER: S-EPMC6883073 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature