New Bicyclic RGD Peptides Optimized for Click Chemistry
Figure 1: RGD-3879-PI
Figure 2: RGD-3993-PI
The Arginine-Glycine-Aspartic Acid (RGD) sequence is recognized by many integrins and is a cell attachment sequence for several proteins.1 In cancer tumor imaging, several radiolabeled, cyclic RGD peptides have been found to be useful in integrin αvβ3-targeting. Integrin αvβ3 binding affinity is also increased by using a bicyclic RGD peptide. 2-4
Moreover, Click chemistry is often used in the preparation of radiolabeled RGD peptides. Click chemistry is used to describe a class of efficient and selective reactions that can be used to join molecules together rapidly and in high yield. The addition of an azide (N3), in the presence of Cu(1), allows for the attachment of an alkyne-containing labeling molecule. On the other hand, the introduction of a maleimide (Mal) enables a reaction with thiols (-SH) to form stable bonds at neutral pH.
Peptides International is pleased to introduce two new bicyclic RGD peptides that are optimized for Click chemistry:
If you do not see what you are looking for, we can also prepare a custom peptide to meet your project specifications. Contact us today for a quote.
- C-C. Sun, X-J. Qu, & Z-H. Gao, American Journal of Therapeutics, 23, e198 (2016). Abstract retrieved from https://www.ncbi.nlm.nih.gov/pubmed/24621642
- J. Shi, F. Wang, S. Liu, Biophysics Reports, 2(1), 1 (2016). Retrieved from https://link.springer.com/article/10.1007/s41048-016-0021-8
- S. Liu, Bioconjug Chem., 26(8),1413 (2015). Retrieved from http://pubs.acs.org/doi/abs/10.1021/acs.bioconjchem.5b00327)
- S. Liu, Bioconjug Chem., 20(12),2199 (2010). Retrieved from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2795072/
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