1234692-69-3Relevant academic research and scientific papers
Radiolabeled antagonistic bombesin peptidomimetics for tumor targeting
Valverde, Ibai E.,Huxol, Elena,Mindt, Thomas L.
, p. 275 - 278 (2014/05/06)
The replacement of amide bonds in the backbone of peptides by proteolytically stable 1,2,3-triazole isosteres can provide novel peptidomimetics with promising properties for the development of tumor-targeting radiopeptides. On the basis of our previous work with radiolabeled agonistic bombesin (BBN) derivatives of the sequence [Nle14]BBN(7-14), we substituted selected amide bonds of the structurally closely related antagonistic peptide analog JMV594. With the exception of the C-terminal modification, amide-to-triazole substitutions tolerated by [Nle 14]BBN(7-14) without loss of biological function led to abolished receptor affinity in the case of JMV594. These findings provide an additional piece of evidence for the currently disputed differences in the modes of action of agonistic and antagonistic gastrin-releasing peptide receptor (GRPR)-targeting radiopeptides.
1,2,3-Triazoles as amide bond mimics: Triazole scan yields protease-resistant peptidomimetics for tumor targeting
Valverde, Ibai E.,Bauman, Andreas,Kluba, Christiane A.,Vomstein, Sandra,Walter, Martin A.,Mindt, Thomas L.
supporting information, p. 8957 - 8960 (2013/09/02)
The triazole makes the difference: Replacement of amide bonds in the backbone of peptides by 1,4-disubstituted 1,2,3-triazole isosteres affords peptidomimetics with retained receptor affinity and cell-internalization properties, enhanced proteolytic stability, and improved tumor-targeting capabilities. Copyright
