RESUMO
The specific binding of RGD cyclic peptide with integrin αvß3 attracts great research interest for tumor-targeting drug delivery. Herein, we designed and synthesized a series of dual-ring RGD-peptide derivatives as a drug carrier for αvß3 targeting. Three novel peptides showed excellent cell adhesion inhibition effect, in which, P3 exhibited 7-fold enhancement in IC50 compared with cyclo(RGDfK). Drug-loaded cytotoxicity experiment and imaging experiment indicated that such dual-cyclic RGD peptides have good tumor targeting effects. This work provides a new strategy for the design of novel RGD peptides.
Assuntos
Integrina alfaVbeta3/metabolismo , Oligopeptídeos/síntese química , Oligopeptídeos/farmacologia , Sequência de Aminoácidos , Antineoplásicos/síntese química , Antineoplásicos/química , Antineoplásicos/farmacologia , Adesão Celular/efeitos dos fármacos , Linhagem Celular Tumoral , Sobrevivência Celular/efeitos dos fármacos , Desenho de Fármacos , Humanos , Oligopeptídeos/química , Conformação ProteicaRESUMO
The functionalization of AuNPs with different biological elements was achieved to investigate their possibility in biomedical applications such as drug delivery, vaccine development, sensing, and imaging. Biofunctionalized AuNPs are pursued for applications such as drug delivery, vaccine development, sensing, and imaging. In this study, AuNPs with diameters of 20 nm were functionalized with lipoic acid, mannose, or the cRGD peptide. By using UV-vis spectroscopy, Fourier transform infrared spectroscopy, dynamic light scattering, transmission electron microscopy, and scanning tunneling microscopy techniques, we showed that AuNPs can be functionalized by these biomolecules in a reliable way to obtain conjugates to explore potential biomedical applications. In particular, we demonstrate that the STM technique can be employed to analyze biofunctionalized AuNPs, and the obtained information can be valuable in the design of biomedical applications.