Complexity of αvβ6-integrin targeting RGD peptide trimers: emergence of non-specific binding by synergistic interaction.

ABSTRACT: Multimerization is an established strategy to design bioactive macromolecules with enhanced avidity, which has been widely employed to increase the target-specific binding and uptake of imaging probes and pharmaceuticals. However, the factors governing the general biodistribution of multimeric probes are less well understood but are nonetheless decisive for their clinical application. We found that regiospecific exchange of phenylalanine by tyrosine (chemically equivalent to addition of single oxygen atoms) can have an unexpected, dramatic impact on the in vivo behavior of gallium-68 labeled αvβ6-integrin binding peptides trimers. For example, introduction of one and two Tyr, equivalent to just 1 and 2 additional oxygens and molecular weight increases of 0.38% and 0.76% for our >4 k

SUBMITTER: Quigley NG 

PROVIDER: S-EPMC10718521 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature