A chimeric, multivalent assembly of galectin-1 and galectin-3 with enhanced extracellular activity.

ABSTRACT: Galectins are attractive therapeutic candidates to control aberrant immune system activation because they can alter the phenotype and function of various innate and adaptive immune cells. However, use of exogenous galectin-1 ("G1") and galectin-3 ("G3") as immunomodulators is challenged by their high dosing requirements and dynamic quaternary structures. Here we report a chimeric assembly of G1 and G3 with enhanced extracellular activity ("G1/G3 Zipper"), which was created by recombinant fusion of G1 and G3 via a peptide linker that forms a two-stranded α-helical coiled-coil. G1/G3 Zipper had higher apparent binding affinity for immobilized lactose and a lower concentration threshold for inducing soluble glycoprotein crosslinking than G1, a recombinant fusion of G1 and G3 with a flexible p

SUBMITTER: Fettis MM 

PROVIDER: S-EPMC6553642 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature