Designed Peptide Fragments of Chlorotoxin for MMP-2 Binding Analysis

Eli Blaney's 2026 dataset contains computational results from molecular docking and dynamics simulations of chlorotoxin (Ctx) and its C-terminal fragments binding to matrix metalloproteinase-2 (MMP-2). The data includes poses from HPEPDOCK, HADDOCK, and AlphaFold2 platforms and binding energies calculated via MMPBSA from 500 ns simulations. The study investigates potential allosteric inhibition of glioblastoma cellular migration.

Use Cases

• Analyze peptide-protein binding poses based on outputs from three molecular docking platforms
• Compare binding energy calculations based on MMPBSA results from molecular dynamics simulations
• Study potential allosteric binding interactions based on non-catalytic region binding data
• Investigate glioblastoma cellular migration inhibition mechanisms based on peptide fragment interactions

Strengths

• Binding energies calculated via the Molecular Mechanics Poisson-Boltzmann Surface Area (MMPBSA) method
• Poses generated from three distinct molecular docking methodologies (HPEPDOCK, HADDOCK, AlphaFold2)
• Simulation stability assessed via 500 ns molecular dynamics runs with configurational entropy and RMSD analyses

Limitations

• Row count is unknown, which may limit suitability assessment
• Column-level documentation is absent; field semantics must be inferred after download
• The dataset is very small at 5.5 KB, indicating limited scope

Provenance

Source

figshare

Collection Method

Data generated from computational molecular docking and dynamics simulations

Time Range

2026

Freshness

Last updated 2026-04-09 17:26:09; freshness should be verified

Geography

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