Biophysical investigation of interactions between sorbic acid and human serum albumin through spectroscopic and computational approaches. (13th April 2021)
- Record Type:
- Journal Article
- Title:
- Biophysical investigation of interactions between sorbic acid and human serum albumin through spectroscopic and computational approaches. (13th April 2021)
- Main Title:
- Biophysical investigation of interactions between sorbic acid and human serum albumin through spectroscopic and computational approaches
- Authors:
- Raza, Muslim
Jiang, Yang
Ahmad, Bashir
Rahman, Ata ur
Raza, Saleem
Khan, Ajmal
Tahir, Kamran
Hassan, Said
Khan, Saifullah
Yuan, Qipeng - Abstract:
- Abstract : This work provides an effective strategy to analyze the SA-induced microenvironmental changes in the HSA macromolecule, and also highlights the medicinal importance of SA. Abstract : In this study, we investigate the mechanism underlying the binding of SA with HSA by multiple spectroscopic and computational approaches. The topographic changes in the native HSA and HSA–SA structure and behaviours were explored by atomic force microscopy (AFM). Moreover, other advanced spectroscopic methods such as fluorescence, Fourier transform infrared (FT-IR) and circular dichroism (CD) spectroscopy should be used to investigate and understand the binding mechanism of the HSA–SA complex. The interaction of HSA and SA takes place via a static quenching mechanism as observed from fluorescence spectroscopy. After the interaction between SA and HSA, the complex (HSA–SA) molecular dimensions have been increased as confirmed from the AFM results. Different thermodynamic parameters, such as Δ H (−29.366 kJ mol −1 ) and Δ S (+108.149 J mol −1 K −1 ), were calculated to explore the binding nature of HSA–SA, which is mainly contributed by hydrophobic contacts and hydrogen bonds. The site marker displacement and molecular modelling studies suggested that the SA can bind on the site I of HSA. Slight conformational changes of HSA–SA were observed from the CD and IR spectra. Together, this study will provide insights for the food industry on the safety and biological action of SA in the humanAbstract : This work provides an effective strategy to analyze the SA-induced microenvironmental changes in the HSA macromolecule, and also highlights the medicinal importance of SA. Abstract : In this study, we investigate the mechanism underlying the binding of SA with HSA by multiple spectroscopic and computational approaches. The topographic changes in the native HSA and HSA–SA structure and behaviours were explored by atomic force microscopy (AFM). Moreover, other advanced spectroscopic methods such as fluorescence, Fourier transform infrared (FT-IR) and circular dichroism (CD) spectroscopy should be used to investigate and understand the binding mechanism of the HSA–SA complex. The interaction of HSA and SA takes place via a static quenching mechanism as observed from fluorescence spectroscopy. After the interaction between SA and HSA, the complex (HSA–SA) molecular dimensions have been increased as confirmed from the AFM results. Different thermodynamic parameters, such as Δ H (−29.366 kJ mol −1 ) and Δ S (+108.149 J mol −1 K −1 ), were calculated to explore the binding nature of HSA–SA, which is mainly contributed by hydrophobic contacts and hydrogen bonds. The site marker displacement and molecular modelling studies suggested that the SA can bind on the site I of HSA. Slight conformational changes of HSA–SA were observed from the CD and IR spectra. Together, this study will provide insights for the food industry on the safety and biological action of SA in the human body. … (more)
- Is Part Of:
- New journal of chemistry. Volume 45:Number 17(2021)
- Journal:
- New journal of chemistry
- Issue:
- Volume 45:Number 17(2021)
- Issue Display:
- Volume 45, Issue 17 (2021)
- Year:
- 2021
- Volume:
- 45
- Issue:
- 17
- Issue Sort Value:
- 2021-0045-0017-0000
- Page Start:
- 7682
- Page End:
- 7693
- Publication Date:
- 2021-04-13
- Subjects:
- Chemistry -- Periodicals
Chimie -- Périodiques
540 - Journal URLs:
- http://www.rsc.org/ ↗
http://www.rsc.org/is/journals/current/newjchem/njc.htm ↗ - DOI:
- 10.1039/d0nj06276f ↗
- Languages:
- English
- ISSNs:
- 1144-0546
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6084.319900
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 16790.xml