Our research investigates the structure and dynamics of key proteins involved in fatty acid synthesis and aryl polyene biosynthesis, alongside transport proteins related to virulence in multidrug-resistant (MDR) Gram-negative pathogens. By elucidating these mechanisms, we aim to disrupt virulence pathways and develop innovative strategies to overcome antibiotic resistance. We employ techniques such as NMR spectroscopy, molecular dynamics (MD) simulations, and X-ray crystallography. To better understand the virulence of A. baumannii, we focus on its unique membrane—an essential barrier reinforced by lipooligosaccharides (LOS) that provide greater rigidity compared to typical lipopolysaccharides (LPS) in other Gram-negative bacteria. Through structure-based in silico screening, we design potent inhibitors targeting the ketosynthases of A. baumannii, enzymes that initiate the elongation step in the biosynthesis of key virulence factors.
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To combat the MDR challenge, we develop innovative therapeutic antimicrobial peptides that possess broad-spectrum antibacterial and immunomodulatory activities for the treatment of infections and sepsis. Notably, one of our peptide antibiotics has successfully completed Phase I clinical trials for sepsis, marking a significant milestone. We employ techniques such as NMR spectroscopy and molecular dynamics (MD) simulations to elucidate the mechanisms of action of these peptides within bacterial membranes, advancing our understanding and optimization of their antimicrobial efficacy.
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