Characterization of Sialic Acid Affinity of the Binding Domain of Mistletoe Lectin Isoform One.

ABSTRACT: Sialic acid (Sia) is considered as one of the most important biomolecules of life since its derivatives and terminal orientations on cell membranes and macromolecules play a major role in many biological and pathological processes. To date, there is only a limited number of active molecules that can selectively bind to Sia and this limitation has made the study of this glycan challenging. The lectin superfamily is a well-known family of glycan binding proteins, which encompasses many strong glycan binding peptides with diverse glycan affinities. Mistletoe lectin (ML) is considered one of the most active members of lectin family which was initially classified in early studies as a galactose binding lectin; more recent studies have suggested that the peptide can also actively bind to Sia. Ho

SUBMITTER: Mohammed S 

PROVIDER: S-EPMC8348413 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature