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Updated: Jul 10, 2026
09:04
A Simple Bioassay for the Evaluation of Vascular Endothelial Growth Factors
Published on: March 15, 2016
On the structure, interactions, and dynamics of bound VEGF
Bruno Araújo Cautiero Horta1, José Jair Vianna Cirino, Ricardo Bicca de Alencastro
1Physical Organic Chemistry Group, Departamento de Química Orgânica, Instituto de Química, Universidade Federal do Rio de Janeiro, Cidade Universitária, CT, Bloco A, Laboratory 609, Rio de Janeiro, RJ 21941-909, Brazil. bruno@iq.ufrj.br
Journal of Molecular Graphics & Modelling
|November 21, 2007
Summary
Vascular endothelial growth factor (VEGF) binding to its receptor or inhibitors causes minimal structural changes. Receptor binding significantly alters VEGF dynamics, unlike inhibitor binding, offering insights into biological processes and drug development.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Vascular Endothelial Growth Factor (VEGF) is crucial for angiogenesis.
- Understanding VEGF's molecular behavior upon binding is key for therapeutic strategies.
Purpose of the Study:
- To investigate the structural and dynamical effects of VEGF binding to its receptor (Flt-1) and a peptide inhibitor (v107).
- To analyze changes in VEGF's interactions, structure, and dynamics.
Main Methods:
- Molecular dynamics simulations of VEGF in complex with Flt-1 receptor, v107 peptide, and a mutant v107.
- Analysis of residue contributions to binding energy.
- Comparison of dynamical variables (thermal fluctuations, correlations) between bound and unbound states.
Main Results:
- VEGF structure remains largely unchanged upon binding.
- Receptor binding induces more significant dynamical perturbations than inhibitor binding.
- VEGF motions become less correlated when bound to the receptor.
Conclusions:
- VEGF's conformational flexibility is altered by binding.
- Binding to Flt-1 receptor impacts VEGF dynamics more than v107 inhibitor binding.
- Findings may inform the design of novel VEGF-targeted therapies.
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