PMID- 34463217
OWN - NLM
STAT- MEDLINE
DCOM- 20221223
LR  - 20230223
IS  - 1538-0254 (Electronic)
IS  - 0739-1102 (Linking)
VI  - 40
IP  - 22
DP  - 2022
TI  - Elucidation of binding mechanism of stigmasterol with human serum albumin: a 
      biophysical and molecular dynamics simulation approach.
PG  - 12135-12147
LID - 10.1080/07391102.2021.1968498 [doi]
AB  - In the present study, we have analyzed the interaction of a phytochemical, 
      stigmasterol (Stig), with human serum albumin (HSA) under physiological 
      conditions using fluorescence quenching, circular dichroism and molecular 
      modeling methods. Cytotoxic studies with Stig in mouse macrophages (RAW 246.7) 
      and HeLa cell lines showed anti-inflammatory and anti-cancer properties. Further, 
      the intrinsic fluorescence of HSA was quenched by Stig, which was considered a 
      static quenching mechanism. The site-specific marker experiments revealed that 
      Stig binds to the IIIA subdomain of HSA with a binding constant of 
      K(Stig)=1.8 +/- 0.03 x 10(5) M(-1) and free energy of -7.26 +/- 0.031 Kcal/mol. The 
      secondary structure of HSA was partially unfolded after binding of Stig, which 
      indicates an alteration in the microenvironment of the protein binding site. 
      Molecular docking experiments found that Stig binds strongly with HSA at the IIIA 
      domain of the hydrophobic pocket with one hydrogen bond. The rigidity of the 
      protein-Stig complex and free energies were analyzed by molecular dynamic 
      simulation (MDS) for 100 ns, where the HSA-Stig was stabilized after 40 ns. MDS 
      studies revealed that HSA does not significantly change the secondary structure 
      when it binds with Stig, which is in agreement with the circular dichroism data. 
      Overall, the results obtained gave qualitative and quantitative insight into the 
      binding interaction between HSA and Stig, which is essential in understanding the 
      latter as a therapeutic molecule.Communicated by Ramaswamy H. Sarma.
FAU - Yeggoni, Daniel Pushparaju
AU  - Yeggoni DP
AD  - Department of Plant Sciences, School of Life Sciences, University of Hyderabad, 
      Hyderabad, India.
FAU - Dubey, Shreya
AU  - Dubey S
AD  - Department of Plant Sciences, School of Life Sciences, University of Hyderabad, 
      Hyderabad, India.
FAU - Mohammad, Yusuf Zamal
AU  - Mohammad YZ
AD  - Department of Plant Sciences, School of Life Sciences, University of Hyderabad, 
      Hyderabad, India.
FAU - Rachamallu, Aparna
AU  - Rachamallu A
AD  - National Institute of Animal Biotechnology, Hyderabad, India.
FAU - Subramanyam, Rajagopal
AU  - Subramanyam R
AD  - Department of Plant Sciences, School of Life Sciences, University of Hyderabad, 
      Hyderabad, India.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20210831
PL  - England
TA  - J Biomol Struct Dyn
JT  - Journal of biomolecular structure & dynamics
JID - 8404176
RN  - ZIF514RVZR (Serum Albumin, Human)
RN  - 99WUK5D0Y8 (Stigmasterol)
SB  - IM
MH  - Animals
MH  - Mice
MH  - Humans
MH  - *Serum Albumin, Human/chemistry
MH  - *Molecular Dynamics Simulation
MH  - Stigmasterol/pharmacology
MH  - Molecular Docking Simulation
MH  - HeLa Cells
MH  - Spectrometry, Fluorescence
MH  - Thermodynamics
MH  - Protein Binding
MH  - Binding Sites
MH  - Circular Dichroism
OTO - NOTNLM
OT  - Protein-ligand interaction
OT  - conformation
OT  - molecular docking
OT  - molecular dynamic simulations
EDAT- 2021/09/01 06:00
MHDA- 2022/12/24 06:00
CRDT- 2021/08/31 08:47
PHST- 2021/09/01 06:00 [pubmed]
PHST- 2022/12/24 06:00 [medline]
PHST- 2021/08/31 08:47 [entrez]
AID - 10.1080/07391102.2021.1968498 [doi]
PST - ppublish
SO  - J Biomol Struct Dyn. 2022;40(22):12135-12147. doi: 10.1080/07391102.2021.1968498. 
      Epub 2021 Aug 31.