Valsartan Binding Affinities for Haemophilus Influenzae PBP3 and Mutants

A research document details in silico drug repurposing findings for the antibiotic-resistant pathogen Haemophilus influenzae. The study, authored by Srujal Kacha, reports molecular docking and simulation results for the FDA-approved drug valsartan against wild-type penicillin-binding protein 3 and two common mutants. The document was last updated on April 28, 2026.

Use Cases

• Evaluating drug candidates for repurposing based on structural similarity to ampicillin, as described in the methods.
• Analyzing binding affinity scores for protein targets, such as the -11.8 kcal/mol value reported for PBP3WT.
• Studying intermolecular interactions and binding stability for PBP3 variants through molecular dynamics simulations, as mentioned in the results.

Strengths

• Specific binding affinity values are provided for three protein targets: -11.8 kcal/mol for PBP3WT, -11.4 kcal/mol for PBP3N526K, and -11.1 kcal/mol for PBP3R517H.
• The research context is clearly defined, linking the work to the WHO's 2024 designation of ampicillin-resistant H. influenzae as a medium-priority pathogen.

Limitations

• The dataset is a 45.4 KB DOCX file, indicating a very small, likely document-based dataset with limited structured data.
• Row count and column-level documentation are unknown, which may limit suitability assessment for computational analysis.
• The description does not specify the source or methodology for the initial drug filtering, only the subsequent in silico evaluations.

Provenance

Source

figshare

Collection Method

In silico molecular docking and dynamics simulations, as described in the document.

Freshness

Last updated 2026-04-28 05:24:22