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Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
Published on: January 26, 2024
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Bioinformatic Analysis of the Leptin-Ob-R Interface: Structural Modeling, Thermodynamic Profiling, and Stability in
Gabriel I Ortega-López1, Francisco Reyes-Espinosa2, Víctor Eric López-Y-López3
1Laboratorio de Investigación Bioquímica y Biofísica Computacional, ENMH, Instituto Politécnico Nacional, Gustavo A. Madero, Ciudad de México 07320, Mexico.
International Journal of Molecular Sciences
|July 29, 2025
Summary
Leptin-receptor binding is enthalpy-driven and varies across species. Environmental factors like pH and temperature significantly impact this crucial interaction, offering insights into mammalian adaptations.
Area of Science:
- Biochemistry
- Structural Biology
- Bioinformatics
Background:
- Leptin, a hormone from adipocytes, regulates energy balance, immunity, and reproduction via its receptor (Ob-R).
- Understanding the structural stability of the leptin-Ob-R complex across species under physiological conditions is limited.
Purpose of the Study:
- To characterize the structural, stability, and thermodynamic properties of the leptin-CRH2 complex across mammalian species.
- To investigate the influence of environmental factors (pH, ionic strength, temperature) on complex formation.
Main Methods:
- Bioinformatics-driven analysis including structural homology modeling.
- Interface mapping and binding energy estimation.
- Assessment of complex stability under varying pH, ionic strength, and temperature conditions.
Main Results:
- The leptin-Ob-R interaction is primarily enthalpy-driven.
- Complex stability is sensitive to changes in temperature, ionic strength, and pH across analyzed species.
- Predicted binding free energy (ΔG) varied from -10.50 to -16.81 kcal/mol.
Conclusions:
- Subtle sequence variations in leptin and Ob-R influence complex stability and environmental responsiveness.
- This study provides a molecular basis for understanding leptin-Ob-R binding adaptations across species and tissue environments.
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