Fluorescent Phthalocyanine-Encapsulated Bovine Serum Albumin Nanoparticles: Their Deployment as Therapeutic Agents in the NIR Region

Abstract

In recent times, researchers have aimed for new strategies to combat cancer by the implementation of nanotechnologies in biomedical applications. This work focuses on developing protein-based nanoparticles loaded with a newly synthesized NIR emitting and absorbing phthalocyanine dye, with photodynamic and photothermal properties. More precisely, we synthesized highly reproducible bovine serum albumin-based nanoparticles (75% particle yield) through a two-step protocol and successfully encapsulated the NIR active photosensitizer agent, achieving a good loading efficiency of 91%. Making use of molecular docking simulations, we confirm that the NIR photosensitizer is well protected within the nanoparticles, docked in site I of the albumin molecule. Encouraging results were obtained for our nanoparticles towards biomedical use, thanks to their negatively charged surface (−13.6 ± 0.5 mV) and hydrodynamic diameter (25.06 ± 0.62 nm), favorable for benefitting from the enhanced permeability and retention effect; moreover, the MTT viability assay upholds the good biocompatibility of our NIR active nanoparticles. Finally, upon irradiation with an NIR 785 nm laser, the dual phototherapeutic effect of our NIR fluorescent nanoparticles was highlighted by their excellent light-to-heat conversion performance (photothermal conversion efficiency 20%) and good photothermal and size stability, supporting their further implementation as fluorescent therapeutic agents in biomedical applications.

Novel Flurbiprofen Derivatives as Antioxidant and Anti-Inflammatory Agents: Synthesis, In Silico, and In Vitro Biological Evaluation

“…The preparation of the macromolecule as a target followed the standard procedure already reported by our group–removal of the co-crystallized molecules, addition of the polar hydrogen atoms and addition of charges [ 49 ]. Redocking of the co-crystallized ligand could not be performed since its structure is composed of an organic ligand that chelates a copper ion coordinatively linked to the imidazole of His40 of the protein, being impossible to perform the molecular docking using the available software.…”

Enantioselective binding of carvedilol to human serum albumin and alpha‐1‐acid glycoprotein

“…The 3D structure of the apo form of HSA and AGP were taken from RCSB Protein Data Bank (entry codes 1AO6 and 3APU, respectively) and the preparation as targets was made according to the previous reports 29–33 …”

“…26,28,29 The 3D structure of the apo form of HSA and AGP were taken from RCSB Protein Data Bank (entry codes 1AO6 and 3APU, respectively) and the preparation as targets was made according to the previous reports. [29][30][31][32][33] The center coordinates of the search space for the albumin sites were for Site 1 x = 36.4, y = 31.8, and z = 30.5, for Site 2 x = 16.5, y = 29.3, and z = 23.5, and for Site 3 x = 42.0, y = 21.9, and 16.9, respectively, whereas for AGP, center coordinates of the search space were x = 13.6, y = 0.0, and z = 16.2.…”

Antioxidant Activity Evaluation and Assessment of the Binding Affinity to HSA of a New Catechol Hydrazinyl-Thiazole Derivative

“…Synthesis of intermediate compound 3 was performed using an adaptation of previously reported similar protocols and the characterization of the compound corresponds with the expected data [ 8 , 18 , 19 ].…”