In silico exploration of phenolics as modulators of penicillin binding protein (PBP) 2× of Streptococcus pneumoniae

• Published in: Scientific reports Vol. 14; no. 1; pp. 8788 - 21
• Main Authors: Aribisala, Jamiu Olaseni, S’thebe, Nosipho Wendy, Sabiu, Saheed
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 16.04.2024; Nature Publishing Group; Nature Portfolio
• Subjects: 631/114; 631/154; Allosteric properties; Amoxicillin; Amoxicillin - pharmacology; Antibacterial; Antibacterial activity; Bacterial Proteins - metabolism; Child; Free energy; Humanities and Social Sciences; Humans; Microbial Sensitivity Tests; Molecular Docking Simulation; Molecular dynamic simulation; multidisciplinary; Multidrug resistance; Penicillin; Penicillin binding protein; Penicillin Resistance - genetics; Penicillin-Binding Proteins - genetics; Penicillin-Binding Proteins - metabolism; Phenolics; Phenols; Science; Science (multidisciplinary); Streptococcus infections; Streptococcus pneumoniae; Streptococcus pneumoniae - genetics; β-Lactam antibiotics; Molecular dynamic simulation; Antibacterial; Phenolics; Penicillin binding protein; Streptococcus pneumoniae

Infections caused by multidrug-resistant Streptococcus pneumoniae remain the leading cause of pneumonia-related deaths in children < 5 years globally, and mutations in penicillin-binding protein (PBP) 2 × have been identified as the major cause of resistance in the organism to beta-lactams. Thus,...