Identification of new fucosyltransferase-8 inhibitors: An integrated biochemical, biophysical, and computational approach

The α -1,6-fucosyltransferase (FUT8) mediated core fucosylation is responsible for several pathophysiological processes, including prostate cancer progression. FUT8 is a promising therapeutic target owing to its effects on cell migration and its capacity to convert androgen-dependent prostate cancer cells into androgen-independent cells. This study, therefore, investigates potential FUT8 inhibitors as therapeutic options for prostate cancer by targeting FUT8-mediated core fucosylation using in vitro , biophysical, and computational approaches. Eight of the 265 compounds showed significant cytotoxicity against the prostate cancer (PC3) cell line in in vitro screening. These compounds demonstrated dose-dependent reductions in cell viability, with IC 50 values ranging from 2.94 ± 0.04 to 75.82 ± 2.10 µM. These compounds were non-cytotoxic against the normal human fibroblast (BJ) cell line. Biophysical and in silico analyses were conducted on active compounds to obtain atomic-level structural details of interactions between FUT8 and ligands. Among these, compounds 1 , 3 , 6 , and 7 showed significant Saturation Transfer Difference Nuclear Magnetic Resonance (STD-NMR) effects and induced a decrease in the melting temperature (Tm) of FUT8 in the differential scanning fluorimetry (DSF) assay (0.25°C–9°C), indicating ligand-associated destabilization of the protein. Molecular docking and molecular dynamics simulation results showed that compounds 1 , 2 , 3 , 4 , 6 , and 7 stably interacted with the FUT8 binding site. These compounds also exhibited anti-migratory activity in a scratch cell assay, as indicated by scratch closure of only 3.14% to 14.18%, compared with 45.45% to 100% in the control group. Our study identified compounds 1 , 3 , 6 , and 7 as promising leads against the FUT8 enzyme. Further mechanistic and in vivo studies are required to evaluate their mechanisms of action for FUT8-driven prostate cancer progression.

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Publication Details

Journal
PLoS ONE
Published
2026-10-05
DOI
https://doi.org/10.1371/journal.pone.0349302
Primary Topic
Glycosylation and Glycoproteins Research
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article
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article

Identification of new fucosyltransferase-8 inhibitors: An integrated biochemical, biophysical, and computational approach

M. Iqbal Choudhary, Humaira Zafar, Sumaira Javaid, Noor Rahman et al.
PLoS ONE
Glycosylation and Glycoproteins Research
article

Identification of new fucosyltransferase-8 inhibitors: An integrated biochemical, biophysical, and computational approach

M. Iqbal Choudhary, Humaira Zafar, Sumaira Javaid, Noor Rahman, Muhammad Awais, Thirugnanasambandam Rajendran, Atia-tul- Wahab
article en

Abstract

The α -1,6-fucosyltransferase (FUT8) mediated core fucosylation is responsible for several pathophysiological processes, including prostate cancer progression. FUT8 is a promising therapeutic target owing to its effects on cell migration and its capacity to convert androgen-dependent prostate cancer cells into androgen-independent cells. This study, therefore, investigates potential FUT8 inhibitors as therapeutic options for prostate cancer by targeting FUT8-mediated core fucosylation using in vitro , biophysical, and computational approaches. Eight of the 265 compounds showed significant cytotoxicity against the prostate cancer (PC3) cell line in in vitro screening. These compounds demonstrated dose-dependent reductions in cell viability, with IC 50 values ranging from 2.94 ± 0.04 to 75.82 ± 2.10 µM. These compounds were non-cytotoxic against the normal human fibroblast (BJ) cell line. Biophysical and in silico analyses were conducted on active compounds to obtain atomic-level structural details of interactions between FUT8 and ligands. Among these, compounds 1 , 3 , 6 , and 7 showed significant Saturation Transfer Difference Nuclear Magnetic Resonance (STD-NMR) effects and induced a decrease in the melting temperature (Tm) of FUT8 in the differential scanning fluorimetry (DSF) assay (0.25°C–9°C), indicating ligand-associated destabilization of the protein. Molecular docking and molecular dynamics simulation results showed that compounds 1 , 2 , 3 , 4 , 6 , and 7 stably interacted with the FUT8 binding site. These compounds also exhibited anti-migratory activity in a scratch cell assay, as indicated by scratch closure of only 3.14% to 14.18%, compared with 45.45% to 100% in the control group. Our study identified compounds 1 , 3 , 6 , and 7 as promising leads against the FUT8 enzyme. Further mechanistic and in vivo studies are required to evaluate their mechanisms of action for FUT8-driven prostate cancer progression.

PLoS ONEVol. 21(10)
Openalex Percentile: Top 21%
Glycosylation and Glycoproteins Research
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