Biophysical insight into the binding of triprolidine hydrochloride to human serum albumin: Calorimetric, spectroscopy and molecular docking approaches

2017 ◽  
Vol 233 ◽  
pp. 55-63 ◽  
Author(s):  
Shama Yasmeen ◽  
Riyazuddeen
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Insight Into

Biophysical insight into the interaction of levocabastine with human serum albumin: spectroscopy and molecular docking approach

2020 ◽  
pp. 1-10
Author(s):  
Fahad M. Almutairi ◽  
Mohammad Rehan Ajmal ◽  
Mohammad Khursheed Siddiqi ◽  
Nabeela Majid ◽  
Adel Ibrahim Ahmad Al-Alawy ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Docking Approach ◽  
Insight Into

Biophysical and molecular docking insight into the interaction of cytosine β-D arabinofuranoside with human serum albumin

2015 ◽  
Vol 164 ◽  
pp. 123-130 ◽  
Author(s):  
Parvez Alam ◽  
Sumit Kumar Chaturvedi ◽  
Tamanna Anwar ◽  
Mohammad Khursheed Siddiqi ◽  
Mohd Rehan Ajmal ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Insight Into

Insight into the interaction of benzothiazole tethered triazole analogues with human serum albumin: Spectroscopy and molecular docking approaches

Luminescence ◽  
2019 ◽  
Vol 34 (8) ◽  
pp. 812-822 ◽  
Author(s):  
Priyanka Yadav ◽  
Jitendra Kumar Yadav ◽  
Arvind Kumar Dixit ◽  
Alka Agarwal ◽  
Satish Kumar Awasthi
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Insight Into

scholarly journals Multi-Spectroscopic Characterization of Human Serum Albumin Binding with Cyclobenzaprine Hydrochloride: Insights from Biophysical and In Silico Approaches

2019 ◽  
Vol 20 (3) ◽  
pp. 662 ◽  
Author(s):  
Mohammad Baig ◽  
Safikur Rahman ◽  
Gulam Rabbani ◽  
Mohd Imran ◽  
Khurshid Ahmad ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Docking ◽  
Human Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Human Serum ◽  
Muscle Relaxant ◽  
In Silico ◽  
Dynamics Simulation ◽  
Insight Into

Cyclobenzaprine hydrochloride (CBH) is a well-known muscle relaxant that is widely used to relieve muscle spasms and other pain associated with acute musculoskeletal conditions. In this study, we elucidated the binding characteristics of this muscle relaxant to human serum albumin (HSA). From a pharmaceutical and biochemical viewpoint, insight into the structure, functions, dynamics, and features of HSA-CBH complex holds great importance. The binding of CBH with this major circulatory transport protein was studied using a combination of biophysical approaches such as UV-VIS absorption, fluorescence quenching, and circular dichroism (CD) spectroscopy. Various in silico techniques, molecular docking and molecular dynamics, were also used to gain deeper insight into the binding. A reduction in the fluorescence intensities of HSA-CBH complex with a constant increase in temperature, revealed the static mode of protein fluorescence quenching upon CBH addition, which confirmed the formation of the HSA-CBH ground state complex. The alteration in the UV-VIS and far-UV CD spectrum indicated changes in both secondary and tertiary structures of HSA upon binding of CBH, further proving CBH binding to HSA. The analysis of thermodynamic parameters ∆H° and ∆S° showed that binding of CBH to HSA was dominated by intermolecular hydrophobic forces. The results of the molecular docking and molecular dynamics simulation studies also confirmed the stability of the complex and supported the experimental results.

scholarly journals Allysine and α-Aminoadipic Acid as Markers of the Glyco-Oxidative Damage to Human Serum Albumin under Pathological Glucose Concentrations

Antioxidants ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 474 ◽  
Author(s):  
Carolina Luna ◽  
Alexis Arjona ◽  
Carmen Dueñas ◽  
Mario Estevez
Keyword(s):  
Oxidative Stress ◽  
Plasma Concentration ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Typical Feature ◽  
Advanced Glycation ◽  
Chemical Mechanisms ◽  
Fasting Plasma ◽  
Insight Into

Understanding the molecular basis of the disease is of the utmost scientific interest as it contributes to the development of targeted strategies of prevention, diagnosis, and therapy. Protein carbonylation is a typical feature of glyco-oxidative stress and takes place in health disorders such as diabetes. Allysine as well as its oxidation product, the α-amino adipic acid (α-AA) have been found to be markers of diabetes risk whereas little is known about the chemistry involved in its formation under hyperglycemic conditions. To provide insight into this issue, human serum albumin was incubated in the presence of FeCl3 (25 μM) and increasing glucose concentrations for 32 h at 37 °C. These concentrations were selected to simulate (i) physiological fasting plasma concentration (4 mM), (ii) pathological pre-diabetes fasting plasma concentration (8 mM), and pathological diabetes fasting plasma concentration (12 mM) of glucose. While both allysine and α-AA were found to increase with increasing glucose concentrations, the carboxylic acid was only detected at pathological glucose concentrations and appeared to be a more reliable indicator of glyco-oxidative stress. The underlying chemical mechanisms of lysine glycation as well as of the depletion of tryptophan and formation of fluorescent and colored advanced glycation products are discussed.

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