Investigation on the interaction between triclosan and bovine serum albumin by spectroscopic methods.

Tytuł:: Investigation on the interaction between triclosan and bovine serum albumin by spectroscopic methods.
Autorzy:: Gu J; Department of Chemistry, College of Sciences, Northeastern University, Shenyang, P.R. China.; College of Chemistry and Chemical Engineering, Bohai University, Jinzhou, P.R. China.
Zheng S; College of Chemistry and Chemical Engineering, Bohai University, Jinzhou, P.R. China.
Zhao H; College of Chemistry and Chemical Engineering, Bohai University, Jinzhou, P.R. China.
Sun T; Department of Chemistry, College of Sciences, Northeastern University, Shenyang, P.R. China.
Źródło:: Journal of environmental science and health. Part. B, Pesticides, food contaminants, and agricultural wastes [J Environ Sci Health B] 2020; Vol. 55 (1), pp. 52-59. Date of Electronic Publication: 2019 Aug 27.
Typ publikacji:: Journal Article; Video-Audio Media
Język:: English
Imprint Name(s):: Publication: 2005- : Abingdon, Oxford : Taylor & Francis
Original Publication: New York, Dekker.
MeSH Terms:: Serum Albumin, Bovine/*chemistry
Triclosan/*chemistry
Animals ; Anti-Infective Agents, Local/chemistry ; Binding Sites ; Cattle ; Circular Dichroism ; Hydrogen Bonding ; Molecular Docking Simulation ; Protein Conformation ; Serum Albumin, Bovine/metabolism ; Spectrometry, Fluorescence ; Spectrophotometry, Ultraviolet ; Thermodynamics ; Triclosan/metabolism
Contributed Indexing:: Keywords: Triclosan; bovine serum albumin; molecular docking; spectroscopic techniques
Substance Nomenclature:: 0 (Anti-Infective Agents, Local)
27432CM55Q (Serum Albumin, Bovine)
4NM5039Y5X (Triclosan)
Entry Date(s):: Date Created: 20190828 Date Completed: 20200413 Latest Revision: 20200413
Update Code:: 20240104
DOI:: 10.1080/03601234.2019.1656499
PMID:: 31453744
: Czasopismo naukowe

Pełny tekst

Multi-spectroscopic and molecular docking methods were used to study the interaction between triclosan (TCS) and bovine serum albumin (BSA). The results indicated that the fluorescence quenching of BSA by TCS was due to the formation of TCS-BSA complex through static quenching. This result was also demonstrated by time-resolved fluorescence experiment. The binding constants and number of binding sites between TCS and BSA were 1.30 × 10 5 M -1 and 1.17 at 298 K, respectively. The thermodynamic parameters were studied in detail which suggested that hydrophobic forces and hydrogen bond played major roles in the TCS-BSA interaction. Moreover, the site marker competitive experiments and docking studies revealed that TCS could bind BSA into site I in subdomain IIA. All the results of UV-vis spectrophotometry, circular dichroism spectroscopy and synchronous fluorescence spectroscopy showed that interaction between TCS and BSA induced conformation changes of BSA.

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