Folding and binding energy of a calmodulin-binding cell antiproliferative peptide
| Autor: | John M. Stewart, Ivan Saika-Voivod, Ahmad M. Almudallal |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Calmodulin
Phenylalanine Amino Acid Motifs Molecular Sequence Data Binding energy Antineoplastic Agents Peptide Peptide binding Plasma protein binding Molecular Dynamics Simulation Ligands Protein Structure Secondary Structure-Activity Relationship User-Computer Interface Materials Chemistry Humans Physical and Theoretical Chemistry Binding site Spectroscopy chemistry.chemical_classification Binding Sites biology Chemistry Computer Graphics and Computer-Aided Design Calmodulin-binding proteins High-Throughput Screening Assays Protein Structure Tertiary Molecular Docking Simulation Biochemistry Docking (molecular) Drug Design biology.protein Biophysics Thermodynamics Calmodulin-Binding Proteins Peptides Hydrophobic and Hydrophilic Interactions Protein Binding |
| Zdroj: | Journal of Molecular Graphics and Modelling. 61:281-289 |
| ISSN: | 1093-3263 |
| DOI: | 10.1016/j.jmgm.2015.08.002 |
| Popis: | We carry out a computational study of a calmodulin-binding peptide shown to be effective in reducing cell proliferation. We find several folded states for two short variants of different length of the peptide and determine the location of the binding site on calmodulin, the binding free energy for the different conformers and structural details that play a role in optimal binding. Binding to a hydrophobic pocket in calmodulin occurs via an anchoring phenylalanine residue of the natively disordered peptide, and is enhanced when a neighbouring hydrophobic residue acts as a co-anchor. The shorter sequence possesses better binding to calmodulin, which is encouraging in terms of the development of non-peptide analogues as therapeutic agents. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect