ArticleFrontiers in pharmacology2024
Structure-guided design and cloning of peptide inhibitors targeting CDK9/cyclin T1 protein-protein interaction.
Article in Frontiers in pharmacology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Computational hybrid framework integrating clinical-mutation profiling and physics-based simulations to predict structural tolerance of Bruton tyrosine kinase (BTK) and sustained ARQ 531 binding.Current research in structural biology · 2026Article
- Advances in cyclotide research: bioactivity to cyclotide-based therapeutics.Molecular diversity · 2025Review
- Structure-guided design of a novel, stable, and soluble Cecropin A variant for antimicrobial therapeutic applications.Scientific reports · 2025Article
- Dynamic migration of phenolics in microwaved combined cooked sorghum: Focus on the polyphenols interact with starch/protein.Food chemistry: X · 2025Article
- Stigmurin encapsulated PLA-PEG ameliorates its therapeutic potential, antimicrobial and antiproliferative activities.Discover nano · 2025Article
- Identification of novel saltiness/saltiness enhancing peptides in egg proteins: Molecular docking, action mechanism andFood chemistry: X · 2025Article
- Rethinking MYC inhibition: a multi-dimensional approach to overcome cancer's master regulator.Frontiers in cell and developmental biology · 2025Review
- Exploring New Structures of Kinase Inhibitors and Multitarget Strategies in Alzheimer's Disease Treatment.Protein and peptide letters · 2025Review
- Harnessing Nature's Bounty: The Neuroprotective Potential of Phytoconstituents and Nanotechnology in Neurodegenerative Disease Therapeutics.CNS & neurological disorders drug targets · 2025Review
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Authors and funding
5 authors.
Funding
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Abstract
CDK9 (cyclin-dependent kinase 9) plays a significant role in numerous pathological conditions, such as HIV-1 infection and cancer. The interaction between CDK9 and cyclin T1 is crucial for maintaining the kinase's active state. Therefore, targeting this protein-protein interaction offers a promising strategy for inhibiting CDK9. In this study, we aimed to design and characterize a library of mutant peptides based on the binding region of cyclin T1 to CDK9. Using Osprey software, a total of 7,776 mutant peptides were generated. After conducting a comprehensive analysis, three peptides, namely, mp3 (RAADVEGQRKRRE), mp20 (RAATVEGQRKRRE), and mp29 (RAADVEGQDKRRE), were identified as promising inhibitors that possess the ability to bind to CDK9 with high affinity and exhibit low free binding energy. These peptides exhibited favorable safety profiles and displayed promising dynamic behaviors. Notably, our findings revealed that the mp3 and mp29 peptides interacted with a conserved sequence in CDK9 (residues 60-66). In addition, by designing the structure of potential peptides in the plasmid vector pET28a (+), we have been able to pave the way for facilitating the process of their recombinant production in an
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