ArticleScientific reports2024
Revealing the pH-dependent conformational changes in sol g 2.1 protein and potential ligands binding.
Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Integrated in silico and in vitro assessment of Azadirachta indica leaf extract against multi-drug resistant Citrobacter koseri and Staphylococcus saprophyticus.Scientific reports · 2026Article
- A Safer Alternative Bio-Repellent: Targeting Mosquito Odorant-Binding Proteins with Catnip-Derived Nepetalactones fromInternational journal of molecular sciences · 2026Article
- Article
- Matrix-dependent bioaccessibility of bioactive amines in Milano dry-fermented sausages after in vitro digestion.Current research in food science · 2026Article
- 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025Review
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Authors and funding
6 authors.
Funding
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Abstract
Sol g 2, a major protein found in the venom of the tropical fire ant (Solenopsis geminata), is well-known for its ability to bind various hydrophobic molecules. In this study, we investigate the binding activity of recombinant Sol g 2.1 protein (rSol g 2.1) with potential molecules, including (E)-β-Farnesene, α-Caryophyllene, and 1-Octen-3-ol at different pH levels (pH 7.4 and 5.5) using fluorescence competitive binding assays (FCBA). Our results revealed that Sol g 2.1 protein has higher affinity binding with these ligands at neutral pH. Relevance to molecular docking and molecular dynamics simulations were utilized to provide insights into the stability and conformational dynamics of Sol g 2.1 and its ligand complexes. After simulation, we found that Sol g 2.1 protein has higher affinity binding with these ligands as well as high structural stability at pH 7.4 than at an acidic pH level, indicating by RMSD, RMSF, Rg, SASA, and principal component analysis (PCA). Additionally, the Sol g 2.1 protein complexes at pH 7.4 showed significantly lower binding free energy (∆G
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