Unveiling the Small Molecules Binding Site of CD36 Cell Surface Receptor Through Docking and Molecular Dynamics Simulations

This study highlights critical residues and structural features involved in ligand recognition by CD36. The identification of the SMAC and its role in modulating LCFA uptake provides promising insights for the development of therapeutic agents targeting CD36-related pathologies, including cancer, diabetes, and metabolic disorders.

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Publication Details

Journal
Current Medicinal Chemistry
Published
2026-02-26
DOI
https://doi.org/10.2174/0109298673413172251202110617
Primary Topic
Peroxisome Proliferator-Activated Receptors
Type
article
Field-Weighted Citation Impact
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article

Unveiling the Small Molecules Binding Site of CD36 Cell Surface Receptor Through Docking and Molecular Dynamics Simulations

José Correa‐Basurto, David Méndez-Luna, Vicente Sandoval-Herrera, Rosa Salgado-Brito et al.
Current Medicinal Chemistry
Peroxisome Proliferator-Activated Receptors
article

Unveiling the Small Molecules Binding Site of CD36 Cell Surface Receptor Through Docking and Molecular Dynamics Simulations

José Correa‐Basurto, David Méndez-Luna, Vicente Sandoval-Herrera, Rosa Salgado-Brito, José-Rubén García-Sánchez, Sergio-Roberto Zamudio-Hernández, Naomi Montes-Mondragón, Martiniano Bello
article en

Abstract

This study highlights critical residues and structural features involved in ligand recognition by CD36. The identification of the SMAC and its role in modulating LCFA uptake provides promising insights for the development of therapeutic agents targeting CD36-related pathologies, including cancer, diabetes, and metabolic disorders.

Current Medicinal ChemistryVol. 33
Universidad Insurgentes (MX), Instituto Politécnico Nacional (MX)
Good health and well-being
Openalex Percentile: Top 38%
Peroxisome Proliferator-Activated Receptors
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