Exploring Glycan Binding Specificity of Odorranalectin by Alanine Scanning Library.

ABSTRACT: Fluorescently labelled alanine scan analogues of odorranalectin (OL), a cyclic peptide that exhibits lectin like properties, were screened for binding BSA-conjugated monosaccharides using an enzyme-linked lectin assay (ELLA). Results revealed that Lys⁵, Phe⁷, Tyr⁹, Gly¹², Leu¹⁴, and Thr¹⁷ were crucial for binding BSA-L-fucose, BSA-D-galactose and BSA-N-acetyl-D-galactosamine. Notably, Ala substitution of Ser³, Pro⁴, and Val¹³ resulted in higher binding affinities compared to the native OL. The obtained data also indicated that Arg⁸ plays an important role in differentiation of binding for BSA-L-fucose/D-galactose from BSA-N-acetyl-D-galactosamine. The thermodynamics o

SUBMITTER: Singh Y 

PROVIDER: S-EPMC9479679 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature