Journal ArticleDOI
Binding of Tolperisone Hydrochloride with Human Serum Albumin: Effects on the Conformation, Thermodynamics, and Activity of HSA
TLDR
This extensive study provides additional insight of ligand binding and structural changes induced in HSA relevant to the biological activity of HSA in vivo.Abstract:
Tolperisone hydrochloride (TH) has muscle relaxant activity and has been widely used for several years in clinical practice to treat pathologically high skeletal muscle tone (spasticity) and related pains. The current study was designed to explore the binding efficacy of TH with human serum albumin (HSA) using multispectrscopic, calorimetric approach, FRET, esterase-like activity, and a molecular docking method. A reduction in fluorescence emission at 340 nm of HSA was attributed to fluorescence quenching by TH via a static quenching type. Binding constants ( Kb) were evaluated at different temperatures, and obtained Kb values were ∼104 M-1, which demonstrated moderately strong affinity of TH for HSA. A calculated negative Δ G° value indicated spontaneous binding of TH to HSA. Far-UV CD spectroscopy revealed that the α-helix content was increased after TH binding. The binding distance between donor and acceptor was calculated to be 2.11 nm based on Forster's resonance energy transfer theory. ITC results revealed TH interacted with HSA via hydrophobic interactions and hydrogen bonding. The thermal stability of HSA was studied using DSC, and results showed that in the presence of TH the structure of HSA was significantly more thermostable. The esterase-like activity of HSA showed fixed Vmax and increased Km suggesting that TH binds with HSA in a competitive manner. Furthermore, molecular docking results revealed TH binds in the cavity of HSA, that is, subdomain IIA (Sudlow site I), and that it hydrogen bonds with K199 and H242 of HSA. Binding studies of drugs with HSA are potentially useful for elucidating chemico-biological interactions that can be utilized in the drug design, pharmaceutical, pharmacology, and biochemistry fields. This extensive study provides additional insight of ligand binding and structural changes induced in HSA relevant to the biological activity of HSA in vivo.read more
Citations
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Journal ArticleDOI
Structure, enzymatic activities, glycation and therapeutic potential of human serum albumin: A natural cargo
Gulam Rabbani,Sae-Young Ahn +1 more
TL;DR: Human serum albumin is one of the most suitable molecules for future research in drug discovery in pharmaceutical industry because of its numerous features and binding pattern that also governs the metabolism and drug dosage.
Journal ArticleDOI
In Vitro Cytotoxicity and Interaction of Noscapine with Human Serum Albumin: Effect on Structure and Esterase Activity of HSA.
Neha Maurya,Jitendra Kumar Maurya,Upendra Kumar Singh,Ravins Dohare,Zafaryab,Meher Rizvi,Meena Kumari,Rajan Patel +7 more
TL;DR: The mechanism of interaction between the anticancer drug noscapine (NOS) and carrier protein human serum albumin (HSA) is studied by using a variety of spectroscopic techniques and electrochemistry methods to determine the variation in protein functionality after binding with NOS.
Journal ArticleDOI
Hyaluronic acid and albumin based nanoparticles for drug delivery
TL;DR: In this paper, a review of the application of HA and albumin based nanoparticles as drug delivery carriers in tumors, joints, vitreum and skin tissue is systematically discussed with the potential and prospect in combined therapy and theranostics.
Journal ArticleDOI
Novel perspective into the interaction behavior study of the cyanidin with human serum albumin-holo transferrin complex: Spectroscopic, calorimetric and molecular modeling approaches
TL;DR: In this article , the authors examined the inducement of an interaction between two carrier proteins, human serum albumin (HSA) and human holo transferrin (HTF) within the presence of cyanidinin the form of binary and ternary systems, which was conducted by different spectroscopic, isothermal titration calorimetric (ITC), and molecular dynamics simulation techniques.
Journal ArticleDOI
Exploring the interaction of bioactive kaempferol with serum albumin, lysozyme and hemoglobin: A biophysical investigation using multi-spectroscopic, docking and molecular dynamics simulation studies.
Sourav Das,Zaved Hazarika,Sharat Sarmah,Kakali Baruah,Mostofa Ataur Rohman,Debojit Paul,Anupam Nath Jha,Atanu Singha Roy +7 more
TL;DR: The ligand, KMP was able to quench the intrinsic fluorescence of these three proteins efficiently through static quenching mode and alter the micro-environment near the Trp fluorophore of the proteins.
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