Multi-Spectroscopic Characterization of Human Serum Albumin Binding with Cyclobenzaprine Hydrochloride: Insights from Biophysical and <i>In Silico</i> Approaches
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 phar...
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doaj-a8c04c1d66f24cdb8e853c06712862b02020-11-25T01:06:05ZengMDPI AGInternational Journal of Molecular Sciences1422-00672019-02-0120366210.3390/ijms20030662ijms20030662Multi-Spectroscopic Characterization of Human Serum Albumin Binding with Cyclobenzaprine Hydrochloride: Insights from Biophysical and <i>In Silico</i> ApproachesMohammad Hassan Baig0Safikur Rahman1Gulam Rabbani2Mohd Imran3Khurshid Ahmad4Inho Choi5Department of Medical Biotechnology, Yeungnam University, 280 Daehak-ro, Gyeongsan, Gyeongbuk 38541, KoreaDepartment of Medical Biotechnology, Yeungnam University, 280 Daehak-ro, Gyeongsan, Gyeongbuk 38541, KoreaDepartment of Medical Biotechnology, Yeungnam University, 280 Daehak-ro, Gyeongsan, Gyeongbuk 38541, KoreaDepartment of Biophysics, All India Institute of Medical Sciences, Ansari nagar, New Delhi 110029, IndiaDepartment of Medical Biotechnology, Yeungnam University, 280 Daehak-ro, Gyeongsan, Gyeongbuk 38541, KoreaDepartment of Medical Biotechnology, Yeungnam University, 280 Daehak-ro, Gyeongsan, Gyeongbuk 38541, KoreaCyclobenzaprine 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 <i>in silico</i> 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.https://www.mdpi.com/1422-0067/20/3/662muscle relaxantcircular dichroismcyclobenzaprine hydrochlorideesterase-like activityhuman serum albuminmolecular dockingmolecular dynamics |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Mohammad Hassan Baig Safikur Rahman Gulam Rabbani Mohd Imran Khurshid Ahmad Inho Choi |
spellingShingle |
Mohammad Hassan Baig Safikur Rahman Gulam Rabbani Mohd Imran Khurshid Ahmad Inho Choi Multi-Spectroscopic Characterization of Human Serum Albumin Binding with Cyclobenzaprine Hydrochloride: Insights from Biophysical and <i>In Silico</i> Approaches International Journal of Molecular Sciences muscle relaxant circular dichroism cyclobenzaprine hydrochloride esterase-like activity human serum albumin molecular docking molecular dynamics |
author_facet |
Mohammad Hassan Baig Safikur Rahman Gulam Rabbani Mohd Imran Khurshid Ahmad Inho Choi |
author_sort |
Mohammad Hassan Baig |
title |
Multi-Spectroscopic Characterization of Human Serum Albumin Binding with Cyclobenzaprine Hydrochloride: Insights from Biophysical and <i>In Silico</i> Approaches |
title_short |
Multi-Spectroscopic Characterization of Human Serum Albumin Binding with Cyclobenzaprine Hydrochloride: Insights from Biophysical and <i>In Silico</i> Approaches |
title_full |
Multi-Spectroscopic Characterization of Human Serum Albumin Binding with Cyclobenzaprine Hydrochloride: Insights from Biophysical and <i>In Silico</i> Approaches |
title_fullStr |
Multi-Spectroscopic Characterization of Human Serum Albumin Binding with Cyclobenzaprine Hydrochloride: Insights from Biophysical and <i>In Silico</i> Approaches |
title_full_unstemmed |
Multi-Spectroscopic Characterization of Human Serum Albumin Binding with Cyclobenzaprine Hydrochloride: Insights from Biophysical and <i>In Silico</i> Approaches |
title_sort |
multi-spectroscopic characterization of human serum albumin binding with cyclobenzaprine hydrochloride: insights from biophysical and <i>in silico</i> approaches |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1422-0067 |
publishDate |
2019-02-01 |
description |
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 <i>in silico</i> 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. |
topic |
muscle relaxant circular dichroism cyclobenzaprine hydrochloride esterase-like activity human serum albumin molecular docking molecular dynamics |
url |
https://www.mdpi.com/1422-0067/20/3/662 |
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