PMID- 32615213
OWN - NLM
STAT- MEDLINE
DCOM- 20210409
LR  - 20210409
IS  - 1879-0003 (Electronic)
IS  - 0141-8130 (Linking)
VI  - 163
DP  - 2020 Nov 15
TI  - The reorganization of conformations, stability and aggregation of serum albumin 
      isomers through the interaction of glycopeptide antibiotic teicoplanin: A 
      thermodynamic and spectroscopy study.
PG  - 66-78
LID - S0141-8130(20)33713-2 [pii]
LID - 10.1016/j.ijbiomac.2020.06.258 [doi]
AB  - The drugs-protein binding study is of growing importance for drug-repurposing 
      against amyloidosis. In this work, we study the binding of teicoplanin (TPN), a 
      glycopeptide antibiotic, with bovine serum albumin (BSA) in its neutral (N), 
      physiological (P) and basic (B) forms, which exist at pH 6, pH 7.4 and pH 9, 
      respectively. The binding and thermodynamic parameters of TPN binding were 
      determined by isothermal titration calorimetry (ITC) and fluorescence quench 
      titration methods. Two binding sites were observed for N and P forms, whereas B 
      form showed only one binding site. ITC and molecular docking results indicated 
      that TPN-BSA complex formation is stabilized by hydrogen bonds, salt bridges and 
      hydrophobic interaction. The red-edge excitation shift (REES) study indicated an 
      ordered compact and spatial arrangement of the TPN bound protein molecule. TPN 
      was found to affect the secondary and tertiary structures of B form only. The TPN 
      binding was observed to marginally stabilize BSA isomers. TPN was also found to 
      inhibit BSA aggregation as monitored by Rayleigh light scattering and thioflavin 
      T binding assay. The current in vitro study will open a new path to explore the 
      possible use of TPN as potential drugs to treat amyloidosis.
CI  - Copyright (c) 2020 Elsevier B.V. All rights reserved.
FAU - Muthu, Shivani A
AU  - Muthu SA
AD  - Protein Assembly Laboratory (PAL), JH-Institute of Molecular Medicine, Jamia 
      Hamdard, Hamdard Nagar, New Delhi 110062, India.
FAU - Jadav, Helly Chetan
AU  - Jadav HC
AD  - School of Chemical Sciences, UM-DAE Centre for Excellence in Basic Sciences, 
      University of Mumbai, Vidyanagari Campus, Mumbai 400098, India.
FAU - Srivastava, Sadhavi
AU  - Srivastava S
AD  - School of Chemical Sciences, UM-DAE Centre for Excellence in Basic Sciences, 
      University of Mumbai, Vidyanagari Campus, Mumbai 400098, India; Department of 
      Biotechnology, Central University of South Bihar, Gaya 824236, India.
FAU - Pissurlenkar, Raghuvir R S
AU  - Pissurlenkar RRS
AD  - Department of Pharmaceutical and Medicinal Chemistry, Goa College of Pharmacy, 
      18th June Road, Panaji, Goa 403001, India.
FAU - Ahmad, Basir
AU  - Ahmad B
AD  - Protein Assembly Laboratory (PAL), JH-Institute of Molecular Medicine, Jamia 
      Hamdard, Hamdard Nagar, New Delhi 110062, India. Electronic address: 
      bashirahmad_sch@jamiahamdard.ac.in.
LA  - eng
PT  - Journal Article
DEP - 20200630
PL  - Netherlands
TA  - Int J Biol Macromol
JT  - International journal of biological macromolecules
JID - 7909578
RN  - 0 (Protein Aggregates)
RN  - 0 (Protein Isoforms)
RN  - 27432CM55Q (Serum Albumin, Bovine)
RN  - 61036-62-2 (Teicoplanin)
SB  - IM
MH  - Amyloidosis/drug therapy
MH  - Animals
MH  - Binding Sites
MH  - Calorimetry
MH  - Circular Dichroism
MH  - Hydrogen-Ion Concentration
MH  - Kinetics
MH  - Models, Molecular
MH  - Molecular Docking Simulation
MH  - Protein Aggregates
MH  - Protein Isoforms/genetics/metabolism
MH  - Protein Stability
MH  - Protein Structure, Secondary
MH  - Protein Structure, Tertiary
MH  - Serum Albumin, Bovine/*chemistry/*metabolism
MH  - Spectrometry, Fluorescence/methods
MH  - Teicoplanin/*chemistry/*metabolism
MH  - Temperature
MH  - Thermodynamics
OTO - NOTNLM
OT  - Biophysical chemistry
OT  - Drug repurposing
OT  - Drug-protein interaction
OT  - Isothermal titration calorimetry
OT  - Protein aggregation
COIS- Declaration of competing interest Authors have no competing interests to declare.
EDAT- 2020/07/03 06:00
MHDA- 2021/04/10 06:00
CRDT- 2020/07/03 06:00
PHST- 2020/04/30 00:00 [received]
PHST- 2020/06/10 00:00 [revised]
PHST- 2020/06/26 00:00 [accepted]
PHST- 2020/07/03 06:00 [pubmed]
PHST- 2021/04/10 06:00 [medline]
PHST- 2020/07/03 06:00 [entrez]
AID - S0141-8130(20)33713-2 [pii]
AID - 10.1016/j.ijbiomac.2020.06.258 [doi]
PST - ppublish
SO  - Int J Biol Macromol. 2020 Nov 15;163:66-78. doi: 10.1016/j.ijbiomac.2020.06.258. 
      Epub 2020 Jun 30.