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  • Benzimidazole-galactosides bind selectively to the galectin-8 N-terminal domain : structure-based design and optimisation
    Hassan, Mujtaba ...
    We have obtained the X-ray crystal structure of the galectin-8 N-terminal domain (galectin-8N) with a previously reported quinoline-galactoside ligand at a resolution of 1.6Å. Based on this X-ray ... structure, a collection of galactosides derivatised at O3 with triazole, benzimidazole, benzothiazole, and benzoxazole moieties were designed and synthesised. This led to the discovery of a 3-O-(N-methylbenzimidazolylmethyl)-galactoside with a Kd of 1.8%[micro]M for galectin-8N, the most potent selective synthetic galectin-8N ligand to date. Molecular dynamics simulations showed that benzimidazole-galactoside derivatives bind the non-conserved amino acid Gln47, accounting for the higher selectivity for galectin-8N. Galectin-8 is a carbohydrate-binding protein that plays a key role in pathological lymphangiogenesis, modulation of the immune system, and autophagy. Thus, the benzimidazole-derivatised galactosides represent promising compounds for studies of the pathological implications of galectin-8, as well as a starting point for the development of anti-tumour and anti-inflammatory therapeutics targeting galectin-8.
    Vir: European journal of medicinal chemistry. - ISSN 0223-5234 (Vol. 223, 2021, str. 1-13)
    Vrsta gradiva - članek, sestavni del ; neleposlovje za odrasle
    Leto - 2021
    Jezik - angleški
    COBISS.SI-ID - 68254211

    Povezava(-e):

    https://www.sciencedirect.com/science/article/pii/S0223523421005134?via%3Dihub
    Repozitorij Univerze v Ljubljani – RUL
    DOI

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