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Silveira, S. d. A.

Publications and source records attributed to Silveira, S. d. A..

3 recordsLinked to original sources

predPPI-GReMLIN: prediction of protein-protein interactions through mining of conserved bipartite graphs

Protein-protein interactions (PPIs) play a central role in elucidating cellular mechanisms. However, a substantial gap remains in current prediction models, as they frequently overlook the structural and physicochemical context governing molecular binding, thereby limiting predictive accuracy. To address this limitation, we introduce predPPI-GReMLIN, a graph-based framework that represents protein-protein interfaces as bipartite graphs, integrating atomic-level physicochemical descriptors, spatial distance constraints, and conserved substructure mining to perform PPI prediction. The method employs a graph-search strategy to detect interface interaction patterns and conducts ligand swapping with complexes that share the same patterns as the query, enabling the prediction of novel interaction partners. Evaluations across multiple datasets--including CAMP (protein-peptide), Yeast (binary PPI), and TAGPPI (multi-class PPI)--demonstrate consistently strong predictive performance, achieving precision, recall, accuracy, and F1-scores exceeding 97% on binary classification benchmarks and surpassing state-of-the-art sequence- and structure-based approaches. Furthermore, incorporating solvent-accessible surface area (SASA)-derived features improved multi-class interaction-type classification accuracy to 57.74%. A case study on the SARS-CoV-2 spike-ACE2 complex further validated the approach: docking simulations using ligands predicted by our method reproduced native-like binding energetics comparable to redocking results. Additionally, a comparison between docking using a predPPI-GReMLIN-predicted ligand and docking using ligands selected at random from the PDB yielded a highly significant p-value (p = 5.1 x 10-9), indicating a robust statistical difference in binding performance. Collectively, these findings demonstrate predPPI-GReMLINs ability to capture conserved structural determinants of PPIs, providing a robust and interpretable framework for protein interaction prediction and ligand discovery. The dataset and source code for the experiments are publicly available at https://github.com/morufwork/predPPIGReMLIN.git.

bioinformatics↗

Protein Abundance Prediction Through Machine Learning Methods

Proteins are responsible for most physiological processes, and their abundance provides crucial information for systems biology research. However, absolute protein quantification, as determined by mass spectrometry, still has limitations in capturing the protein pool. Protein abundance is impacted by translation kinetics, which rely on features of codons. In this study, we evaluated the effect of codon usage bias of genes on protein abundance. Notably, we observed differences regarding codon usage patterns between genes coding for highly abundant proteins and genes coding for less abundant proteins. Analysis of synonymous codon usage and evolutionary selection showed a clear split between the two groups. Our machine learning models predicted protein abundances from codon usage metrics with remarkable accuracy, achieving R2 values higher than previously reported in the literature. Upon integration of the predicted protein abundance in enzyme-constrained genome-scale metabolic models, the simulated phenotypes closely matched experimental data, which demonstrates that our predictive models are valuable tools for systems metabolic engineering approaches.

systems biology↗

GAPIN: Grouped and Aligned Protein Interface Networks

SummaryGAPIN is a web-based application for structural interaction network analysis among any type of PDB molecules, regardless of whether their interfaces are between chain-chain or chain-ligand. A special emphasis is given to graph clustering, allowing users to scrutinize target contexts for ligand candidates. We show how GAPIN can be used to unveil underlying hydrophobic patterns on a set of peptidase-inhibitor complexes. In another experiment, we show there is a positive correlation between cluster sizes and the presence of druggable spots, indicating that the clustering may discriminate the higher complexity of these hot subnetworks.\n\nAvailability and implementationGAPIN is freely available as an easy-to-use web interface at https://gapin.unifei.edu.br.\n\nContactbiharck@ufmg.br, carlos.silveira@unifei.edu.br.\n\nSupplementary informationSupplementary data are available online.

bioinformatics↗