Antidepressant drug-protein interactions studied by spectroscopic methods based on fluorescent carbon quantum dots

Abstract

A highly sensitive fluorescent carbon quantum dots (CDs) was designed to measure the interaction of antidepressant drugs and serum albumins (SA). In present investigation the interaction of bovine serum albumin (BSA) and human serum albumin (HSA) with antidepressant drugs viz. amitryptiline hydrochloride (AMT), chlorpromazine hydrochloride (CPZ) and desipramine hydrochloride (DSP) bioconjugated on CDs have been studied by different spectroscopic techniques i.e., Fluorescence, UV-Visible, Dynamic light scattering (DLS) and FT-IR. The CDs were prepared by one-pot method using glucose and PEG-200. The developed CDs showed blue luminescence under irradiation with ultra-violet. The Stern-Volmer quenching constant (K sv ) indicates the presence of static quenching mechanism. The apparent binding constant K a between antidepressant drugs with complex of SA-CDs have been determined. These results illustrated that CPZ shows strong binding with HSA. As further analyzed by FT-IR spectroscopy and DLS technique, the results suggested induced conformational changes on SA, thus confirming the experimental and theoretical results. Thus, a thorough knowledge of the energetics of drug-protein affinities in presence of CDs as attempted in this work is vital in giving way for appropriate drug delivery.

In vitro Interactions of Secnidazole and Its Iron (II), Copper (II) Complexes with Bovine Serum Albumin by Fluorescence Quenching Method

“…This sort of drug-protein interaction can also affect the drug stability and toxicity amid chemotherapeutic process. Since the existence of interaction between drug particles and proteins can give helpful data about the structural characteristics or basic highlights of small molecules and provide new opportunities for the advancement of new drugs, hence studying the interaction of the new drug with protein is important (Reshma et al, 2019). Bovine serum albumin (BSA) is widely used as an in vitro model for studying drugprotein interaction, since its composition is 76% similar to that of human serum albumin (Ran et al, 2007;Khan et al, 2016).…”

Green Synthesis of Highly Fluorescent Carbon Dots from Bovine Serum Albumin for Linezolid Drug Delivery as Potential Wound Healing Biomaterial: Bio-Synergistic Approach, Antibacterial Activity, and In Vitro and Ex Vivo Evaluation

“…Among the precursors recently examined across literature, it can be inferred that proteins are potential precursors to synthesize CDs and are interesting materials due to their enhanced adsorption capacity, low toxicity, superior biodegradability, and exquisite non-immunogenicity [ 12 , 17 ]. The conjugation mechanism of proteins with drug molecules has shed light on various research areas and stipulated new prospects for the development of novel drugs [ 18 ]. Bovine serum albumin (BSA), a model globular protein, is a biocompatible, biodegradable, highly aqueous-soluble, inexpensive, and non-toxic carrier, which conjugates with drugs through non-covalent interactions and presents a 76% sequence homology with the three-dimensional (3D) structure of human serum albumin (HSA) [ 18 , 19 , 20 ].…”

“…The conjugation mechanism of proteins with drug molecules has shed light on various research areas and stipulated new prospects for the development of novel drugs [ 18 ]. Bovine serum albumin (BSA), a model globular protein, is a biocompatible, biodegradable, highly aqueous-soluble, inexpensive, and non-toxic carrier, which conjugates with drugs through non-covalent interactions and presents a 76% sequence homology with the three-dimensional (3D) structure of human serum albumin (HSA) [ 18 , 19 , 20 ]. Furthermore, BSA facilitates the drug to be delivered and transported in the body and be easily given up at the surface of the cell.…”

Interactions of linagliptin, rabeprazole sodium, and their formed complex with bovine serum albumin: Computational docking and fluorescence spectroscopic methods

“…Moreover, many mandatory thermodynamic data or others, structural characteristics, or basic highlights of small molecules can be established from the investigation of interactions between drug particles and protein. Hence insight into these interactions of a new ligand with protein is a significant step for the drug development process 6 . As an in vitro model, bovine serum albumin (BSA) is widely used for studying drug–protein interaction since its molecular composition is almost 76% similar to that of human SA 7 .…”