Abstract | BACKGROUND: OBJECTIVE: This study aims to adopt different strategies for targeting calcium integrin- binding protein 1 by computer- aided drug design methods. Our results showed that the top four selected peptides interact with CIB1 more strongly than the reference peptide and restore normal cell function by engaging CIB1. Our binding affinity analyses explore an innovative approach to planning a new peptide to inhibit triple-negative breast cancer. METHODS: Molecular dynamic simulation of the CIB1-UNC10245092 interaction highlights the potential peptide inhibitors through in-silico mutagenesis and designs novel peptide inhibitors from the reference peptide (UNC10245092) through residue scan methodology. RESULTS: The top four designed peptides (based on binding free energy) were subjected to molecular dynamics simulations using AMBER to evaluate stability. CONCLUSION: Our results indicate that among the top five selected peptides, the mutant 2nd mutants have more potential to inhibit CIB1 than the reference peptide (UNC10245092) and have the potency to prevent or restore the tumor suppressor function of UNC10245092.
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Authors | Muhammad Shahab, Chaoqun Liang, Xiuyuan Duan, Guojun Zheng, Abdul Wadood |
Journal | Current pharmaceutical design
(Curr Pharm Des)
Vol. 29
Issue 8
Pg. 630-638
( 2023)
ISSN: 1873-4286 [Electronic] United Arab Emirates |
PMID | 36998135
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Copyright | Copyright© Bentham Science Publishers; For any queries, please email at [email protected]. |
Chemical References |
- Receptor, ErbB-2
- Receptors, Progesterone
- CIB1 protein, human
- Calcium-Binding Proteins
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Topics |
- Female
- Humans
- Triple Negative Breast Neoplasms
(drug therapy, genetics)
- Breast Neoplasms
(genetics)
- Receptor, ErbB-2
(metabolism)
- Mutagenesis
- Receptors, Progesterone
- Calcium-Binding Proteins
(metabolism)
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