Work

Exploring Glycan Binding Specificity of Odorranalectin by Alanine Scanning Library

Year: 2022

Type: article

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 of binding of the selected alanine analogues was evaluated by isothermal titration calorimetry. Low to moderate binding affinities were determined for the tetravalent MUC1 glycopeptide and asialofetuin, respectively, and high for the fucose rich polysaccharide, fucoidan. The thermodynamic profile of interactions with asialofetuin exhibits shift to an entropy‐driven mechanism compared to the fucoidan, which displayed an enthalpy‐entropy compensation, typically associated with the carbohydrate‐lectin recognition process.

Source: European Journal of Organic Chemistry

DOI: 10.1002/ejoc.202200302

Authors: YashoNandini Singh, Predrag Cudic, Maré Cudic

Institution: Florida Atlantic University

Language: English

Topic: Glycosylation and Glycoproteins Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Cancer Institute

Award: Mechanistic insight into tumor-associated MUC1 glycopeptides binding to macrophage galactose-type lectin