Synthetic chlorin derivative self-prevented from aggregation: Behavior in homogeneous medium for PDT applications

Herein the great performance of a synthetic chlorin (Chlo) as photosensitizer (PS) in a homogeneous ethanol/water environment and its interaction with protein model are described. Excellent interaction with the bovine serum albumin (BSA) protein model was achieved and the experimental results revealed that Chlo, designed to have low aggregation level, showed great stability in mixtures up to 65% of water, whereas the formation of small self-aggregates may take place in mixtures with greater proportion of water. In addition, computational calculations have shown that temperature influences the conformational stability of the molecule with consequences in aggregation. Fluorescence and electronic absorption spectroscopies were used to study the interaction between Chlo and BSA under simulative physiological condition at different temperatures.The study of the interaction with a protein model is important in view of the development of new drugs and their pharmacokinetic behavior. The results indicated strong interaction between Chlo and BSA, which is a spontaneous process guided by hydrophobic forces (Delta G <0; Delta H >0; Delta S > 0).These results corroborate with the vision of a good PS lobe applied in Photodynamic Therapy (PDT) and Antimicrobial Photodynamic Therapy (aPDT). (C) 2020 Elsevier B.V. All rights reserved.