PMID- 37498152
OWN - NLM
STAT- Publisher
LR  - 20230727
IS  - 1538-0254 (Electronic)
IS  - 0739-1102 (Linking)
DP  - 2023 Jul 27
TI  - Binding characteristics and conformational changes in alpha-2-macroglobulin by 
      the dietary flavanone naringenin: biophysical and computational approach.
PG  - 1-16
LID - 10.1080/07391102.2023.2240420 [doi]
AB  - In the present study, we investigated the interaction of alpha-2-macroglobulin 
      (alpha2M) with naringenin using multi-spectroscopic, molecular docking, and molecular 
      simulation approaches to identify the functional changes and structural 
      variations in the alpha2M structure. Our study suggests that naringenin compromised 
      alpha2M anti-proteinase activity. The results of absorption spectroscopy and 
      fluorescence measurement showed that naringenin-alpha2M formed a complex with a 
      binding constant of (k(b)) approximately 10(4), indicative of moderate binding. The value of 
      DeltaG degrees  in the binding indicates the process to be spontaneous and the major force 
      responsible to be hydrophobic interaction. The findings of FRET reveal the 
      binding distance between naringenin and the amino acids of alpha2M was 2.82 nm. The 
      secondary structural analysis of alpha2M with naringenin using multi-spectroscopic 
      methods like synchronous fluorescence, red-edge excitation shift (REES), FTIR, 
      and CD spectra further confirmed the significant conformational alterations in 
      the protein. Molecular docking approach reveals the interactions between 
      naringenin and alpha2M to be hydrogen bonds, van der Waals forces, and pi 
      interactions, which considerably favour and stabilise the binding. Molecular 
      dynamics modelling simulations also supported the steady binding with the least 
      RMSD deviations. Our study suggests that naringenin interacts with alpha2M to alter 
      its confirmation and compromise its activity.Communicated by Ramaswamy H. Sarma.
FAU - Ansari, Sana
AU  - Ansari S
AD  - Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, 
      Aligarh, India.
FAU - Zia, Mohammad Khalid
AU  - Zia MK
AD  - Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, 
      Aligarh, India.
FAU - Ahsan, Haseeb
AU  - Ahsan H
AUID- ORCID: 0000-0002-5313-5959
AD  - Department of Biochemistry, Faculty of Dentistry, Jamia Millia Islamia, New 
      Delhi, India.
FAU - Hashmi, Md Amiruddin
AU  - Hashmi MA
AUID- ORCID: 0000-0002-7230-3962
AD  - Interdisciplinary Biotechnology Unit, Faculty of Life Sciences, Aligarh Muslim 
      University, Aligarh, UP, India.
FAU - Khan, Fahim H
AU  - Khan FH
AUID- ORCID: 0000-0001-9004-7993
AD  - Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, 
      Aligarh, India.
LA  - eng
PT  - Journal Article
DEP - 20230727
PL  - England
TA  - J Biomol Struct Dyn
JT  - Journal of biomolecular structure & dynamics
JID - 8404176
SB  - IM
OTO - NOTNLM
OT  - Naringenin
OT  - alpha-2-macroglobulin
OT  - antiproteinase
OT  - biophysical methods
OT  - molecular docking
OT  - proteinase
EDAT- 2023/07/27 13:10
MHDA- 2023/07/27 13:10
CRDT- 2023/07/27 09:33
PHST- 2023/07/27 13:10 [medline]
PHST- 2023/07/27 13:10 [pubmed]
PHST- 2023/07/27 09:33 [entrez]
AID - 10.1080/07391102.2023.2240420 [doi]
PST - aheadofprint
SO  - J Biomol Struct Dyn. 2023 Jul 27:1-16. doi: 10.1080/07391102.2023.2240420.