Fine-tuned structural modifications enable specific drug design against multidrug-resistant pathogens

Marcos Ostolga-Chavarría; Héctor Miranda-Astudillo; Diego González-Halphen

doi:10.1016/j.str.2025.02.001

Fine-tuned structural modifications enable specific drug design against multidrug-resistant pathogens

Structure. 2025 Mar 6;33(3):419-420. doi: 10.1016/j.str.2025.02.001.

Authors

Marcos Ostolga-Chavarría¹, Héctor Miranda-Astudillo², Diego González-Halphen³

Affiliations

¹ Departamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Mexico City, Mexico.
² Departamento de Biología Molecular y Biotecnología, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, Mexico City, Mexico.
³ Departamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Mexico City, Mexico. Electronic address: dhalphen@ifc.unam.mx.

PMID: 40054440
DOI: 10.1016/j.str.2025.02.001

Abstract

In this issue of Structure, Krah et al.¹ present a comprehensive study combining molecular dynamics (MD) simulations, free-energy calculations, and in vivo mutagenesis experiments to investigate how water molecules interact with the F₁F_O-ATP synthase c-ring domain. Their findings highlight the potential of this bacterial enzyme as a drug target.

MeSH terms

Anti-Bacterial Agents* / chemistry
Anti-Bacterial Agents* / pharmacology
Drug Design*
Drug Resistance, Multiple, Bacterial*
Molecular Dynamics Simulation
Proton-Translocating ATPases* / antagonists & inhibitors
Proton-Translocating ATPases* / chemistry
Proton-Translocating ATPases* / metabolism
Water / chemistry

Substances

Anti-Bacterial Agents
Proton-Translocating ATPases
Water