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If you need to enhance the affinity of lead peptides or address the issue of peptides not exhibiting sufficient activity towards targets in vivo, CD ComputaBio, with its extensive experience accumulated over many years in the field of peptide lead compound optimization, assists customers in elevating candidate peptides to new heights.
Peptides are organic compounds formed by amino acids linked through peptide bonds after dehydration, with molecular weights between those of small molecules and biological macromolecules. Classic peptide structures often have poor stability against proteases and inadequate bioavailability, making oral administration difficult. Therefore, structural modification and chemical alteration of active peptides are necessary to improve the druggability of peptide compounds and provide theoretical guidance for the development of innovative peptide drugs.
Fig. 1 Representative strategies for peptidomimetic PPI inhibitors design and optimization. (Wang X, et al.; 2021)
CD ComputaBio relies on artificial intelligence and computer simulation technology to provide comprehensive peptide optimization services. From the perspectives of improving the bioactivity, permeability, stability, and druggability of peptide molecules, we offer two modification strategies:
We modify the backbone structure of peptide chains through structural modifications to enhance their stability and functionality. Our strategies include non-natural amino acid modifications, peptidomimetic strategies, retro-inverso strategies, cyclization strategies, and terminal structure modifications.
Peptide Sidechain Modification
We introduce other groups for structural optimization to enhance peptide performance while keeping the peptide backbone unchanged. Our services include advanced fatty acid modifications, PEGylation, protein fusion strategies, and cholesterol modifications to improve the druggability of peptides.
Alchemical relative binding free energy (ΔΔG) calculations have demonstrated high accuracy in predicting ligand binding affinity and have been used as important tools in computer-aided drug discovery and design. We use free energy perturbation (FEP) or thermodynamic integration (TI) methods to predict the relative binding free energy between two different peptides (ligands) for the same receptor, assessing the changes in activity before and after peptide modification.
Fig. 2 Peptide drug optimization using alchemical free energy calculation.
Improving Peptide Activity
Activity is essential for the development of peptides into drugs. Some natural or artificially synthesized peptides exhibit poor bioactivity and require structural modification to enhance their affinity for receptors and improve their activity.
Optimizing Peptide Stability
Most peptide drugs are degraded and inactivated by proteases, leading to very low bioavailability. By modifying and optimizing the structure of peptides, the degradation by proteases can be reduced or avoided, thereby improving their stability.
Enhancing Peptide Solubility
Some peptide drugs used in clinical settings have poor solubility in aqueous solutions because they contain aromatic amino acids like phenylalanine and tyrosine. Introducing alternative groups can enhance the solubility of peptides.
Increasing Peptide Permeability
Peptide drugs must cross the cell membrane to be absorbed and exert pharmacological activity. Structurally modifying peptides to enhance their permeability aids the entry of peptide drugs into cells, allowing them to exert their activity.
CD ComputaBio specializes in the field of peptide optimization services, leveraging cutting-edge computational technology and extensive expertise to offer customized peptide optimization solutions. If you're looking to enhance peptide performance and quality, feel free to contact us to start a collaborative journey.
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CD ComputaBio offers computation-driven peptide design services to research institutions, pharmaceutical, and biotechnology companies.
