Targeting Pathogenic Bacterial Proteins: An In-silico Study of Oxalic Acid from Curvularia pseudorobusta isolated from Distimake Dissectus (Jacq.) A.R. Simões & Staples.

Abstract

This study investigates the binding interactions of oxalic acid from Curvularia pseudorobusta isolated from       Distimake dissectus (Jacq.) A.R. Simões & Staples., against targeted bacterial proteins and compares these interactions to those of ampicillin which is used as a positive control. We have analysed protein structures from Lactobacillus, E. coli, Pseudomonas, and Bacillus species, viz., 4MKS, 5J9G, 7QLE, 1RX7, 1TLT, 1QJ8, 5OE3, 1EZM, 1IUV, 1NPC, 1AH7, and 1B90.

Oxalic acid exhibited variable binding affinities across different proteins. In Lactobacillus, affinities ranged from +2.59 to -4.54 kcal/mol, with dissociation constants from 9.20 mM to 468.58 µM. In E. coli, affinities ranged from -1.19 to -4.76 kcal/mol, with constants between 134.36 mM and 325.36 µM. For Pseudomonas, affinities varied from -1.13 to -7.67 kcal/mol, with constants ranging from 148.88 mM to 2.38 µM. In Bacillus, affinities ranged from -0.27 to -7.67 kcal/mol, with constants from 9.50 mM to 629.86 mM. Ampicillin showed consistently high binding affinities across all proteins, with values from -1.19 to -9.65 kcal/mol and dissociation constants ranging from 1.68 µM to 84.89 nM. The variability in oxalic acid’s binding affinities highlights its potential as a selective therapeutic agent. These findings provide insights into oxalic acid’s molecular interactions and its comparative efficacy to ampicillin, offering guidance for future drug development and microbial treatment strategies.