Biotinylation at the N- or C-terminus of peptides was found to lead to an increase in bioavailability by up to two orders of magnitude, this modification enables efficient delivery of peptide drugs in mammalian cells and significantly increases the stabilization of peptides (e.g. insulin) oral delivery. CD BioSciences provides comprehensive peptidomimetic biotinylation modification services to help global customers achieve greater research progress in stable drug delivery and drug discovery.
Overview of Biotinylation
Biotinylation is the process of covalently attaching biotin to proteins, nucleic acids or other molecules. Biotinylation is rapid, specific and unlikely to interfere with the natural function of the molecule due to the small size of biotin. Biotin binds to streptavidin and avidin with extremely high affinity, rapid binding rate, and high specificity, and these interactions are used in many areas of biotechnology to isolate biotinylated molecules of interest. The binding of biotin to streptavidin and avidin resists extreme heat, pH, and proteolysis, making it possible to capture biotinylated molecules in a variety of environments. In addition, multiple biotin molecules can bind to the protein of interest, which allows binding of multiple streptavidin, avidin, or neutravidin molecules and increases the sensitivity of detection of the protein of interest.
Fig. 1 Principles of Proximity-Dependent Biotinylation. (Samavarchitehrani, et al., 2020)
Biotinylation of Peptidomimetics
Usually, biotinylated peptides or proteins are mainly used for labeling, purification or detection purposes, especially in immunoassays and protein-protein interaction studies. However, it has been found that administration of peptides or peptidomimetics with simple, nontoxic biotin modifications can facilitate their delivery across cell membranes and facilitate oral uptake. The development of peptidomimetics with biotinylation modifications therefore plays an important role in the development of new therapeutics and their use as drug lead compounds.
Fig. 2 Amino acid sequences and structures of N-terminally biotinylated peptides derived from Asp-hemolysin. (Sato, et al., 2012)
Our Services
CD BioSciences offers comprehensive peptidomimetic biotinylation services. Using our PepDomTM platform, biotin molecules or biotin analogs, which must be reducible, are linked via a suitable bond at the N- or C-terminus. Intracellular delivery of the peptidomimetic is facilitated by these linkages.
- Available Modification Positions
The modification positions we provide can be the C-terminus, N-terminus of the peptide chain and any amino acid side chain end of interest to customers. Their covalent linkages include, but are not limited to, amide bonds, ester bonds, and disulfide bonds.
- Types of Biotins
In the process of biotinylation modification, the biotin used must be in the reduced form.
Types of biotins used for peptidomimetic modification include, but are not limited to: dehydrobiotin, iminobiotin, biotinamine, diaminobiotin, desthiobiotin, halobiotin, long-chain biotin, and biotin-PEG.
Features of Our Services
Advanced Technology Platform
Professional Scientific Staff
Free Consultation and Advice
High-Quality Results Guaranteed
CD BioSciences specializes in providing various services for the development of peptidomimetics, and we are dedicated to the biotinylation of peptidomimetics based on the increased demand for delivery and bioavailability. As long as you are interested in any aspect of peptidomimetic development, please contact us for the best solution.
References
- Samavarchitehrani, P., Samson, R., Gingras, A. Proximity dependent biotinylation: key enzymes and adaptation to proteomics approaches[J]. Molecular & Cellular Proteomics, 2020, 19(5): mcp. R120.001941.
- Sato, A., Kumagai, T., Aoki, J., & Ebina, K. (2012). Synthetic biotinylated peptide compounds derived from Asp-hemolysin: Novel potent inhibitors of platelet-activating factor. European Journal of Pharmacology, 685(1-3), 205–212.
All of our services are intended for preclinical research use only and cannot be used to diagnose, treat or manage patients.
