Integrins are transmembrane receptors that mediate bidirectional signaling across the plasma membrane and play a crucial role in tumor progression, metastasis, and cellular communication. In this study, we performed a comparative structural and biophysical analysis of the PTHTRWA-functionalized extracellular vesicles (PTHTRWA-EVs) interacting with α2β1 and α5β1 integrins to investigate the molecular determinants underlying selective recognition. Surface plasmon resonance experiments were used to characterize multivalent bioengineered EVs --- integrin binding under physiological conditions, while molecular dynamics simulations provided residue-level insight into local ligand-receptor interaction patterns and conformational preferences. These results indicate that PTHTRWA binding is associated with local conformational rearrangements consistent with stabilization of an open-like binding geometry at the integrin interface. Together, these complementary approaches highlight the potential of PTHTRWA-functionalized EVs as a platform for targeted drug delivery and cancer diagnostics.
Nowicka et al. (Fri,) studied this question.