Cargando…

Interaction of gallic acid with trypsin analyzed by spectroscopy

The interactions between trypsin and gallic acid (GA) were investigated by means of fluorescence spectroscopy, UV-vis absorption spectroscopy, resonance light scattering (RLS) spectroscopy, synchronous fluorescence spectroscopy, and enzymatic inhibition assay. It was found that GA can cause the fluo...

Descripción completa

Detalles Bibliográficos
Autores principales: Song, Hao, Chen, Chaoyin, Zhao, Shenglan, Ge, Feng, Liu, Diqiu, Shi, Dandan, Zhang, Tiancai
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taiwan Food and Drug Administration 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9351775/
https://www.ncbi.nlm.nih.gov/pubmed/28911378
http://dx.doi.org/10.1016/j.jfda.2014.09.001
_version_ 1784762504420786176
author Song, Hao
Chen, Chaoyin
Zhao, Shenglan
Ge, Feng
Liu, Diqiu
Shi, Dandan
Zhang, Tiancai
author_facet Song, Hao
Chen, Chaoyin
Zhao, Shenglan
Ge, Feng
Liu, Diqiu
Shi, Dandan
Zhang, Tiancai
author_sort Song, Hao
collection PubMed
description The interactions between trypsin and gallic acid (GA) were investigated by means of fluorescence spectroscopy, UV-vis absorption spectroscopy, resonance light scattering (RLS) spectroscopy, synchronous fluorescence spectroscopy, and enzymatic inhibition assay. It was found that GA can cause the fluorescence quenching of trypsin during the process of formation of GA-trypsin complex, resulting in inhibition of trypsin activity (IC(50) = 3.9 × 10(−6) mol/L). The fluorescence spectroscopic data showed that the quenching efficiency can reach about 80%. The binding constants were 1.9371 × 10(4) L/mol, 1.8192 × 10(4) L/mol, and 1.7465 × 10(4) L/mol at three temperatures, respectively. The thermodynamic parameters revealed that hydrogen bonds, van der Waals, hydrophobic, and electrostatic interactions were involved in the binding process of GA to trypsin. Molecular modeling studies illustrated a specific display of binding information and explained most of the experiment phenomena. The microenvironments of tryptophan and tyrosine residue in trypsin were changed by the GA. Results indicated that GA was a strong quencher and inhibitor of trypsin.
format Online
Article
Text
id pubmed-9351775
institution National Center for Biotechnology Information
language English
publishDate 2014
publisher Taiwan Food and Drug Administration
record_format MEDLINE/PubMed
spelling pubmed-93517752022-08-09 Interaction of gallic acid with trypsin analyzed by spectroscopy Song, Hao Chen, Chaoyin Zhao, Shenglan Ge, Feng Liu, Diqiu Shi, Dandan Zhang, Tiancai J Food Drug Anal Original Article The interactions between trypsin and gallic acid (GA) were investigated by means of fluorescence spectroscopy, UV-vis absorption spectroscopy, resonance light scattering (RLS) spectroscopy, synchronous fluorescence spectroscopy, and enzymatic inhibition assay. It was found that GA can cause the fluorescence quenching of trypsin during the process of formation of GA-trypsin complex, resulting in inhibition of trypsin activity (IC(50) = 3.9 × 10(−6) mol/L). The fluorescence spectroscopic data showed that the quenching efficiency can reach about 80%. The binding constants were 1.9371 × 10(4) L/mol, 1.8192 × 10(4) L/mol, and 1.7465 × 10(4) L/mol at three temperatures, respectively. The thermodynamic parameters revealed that hydrogen bonds, van der Waals, hydrophobic, and electrostatic interactions were involved in the binding process of GA to trypsin. Molecular modeling studies illustrated a specific display of binding information and explained most of the experiment phenomena. The microenvironments of tryptophan and tyrosine residue in trypsin were changed by the GA. Results indicated that GA was a strong quencher and inhibitor of trypsin. Taiwan Food and Drug Administration 2014-12-04 /pmc/articles/PMC9351775/ /pubmed/28911378 http://dx.doi.org/10.1016/j.jfda.2014.09.001 Text en © 2015 Taiwan Food and Drug Administration https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC-BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) ).
spellingShingle Original Article
Song, Hao
Chen, Chaoyin
Zhao, Shenglan
Ge, Feng
Liu, Diqiu
Shi, Dandan
Zhang, Tiancai
Interaction of gallic acid with trypsin analyzed by spectroscopy
title Interaction of gallic acid with trypsin analyzed by spectroscopy
title_full Interaction of gallic acid with trypsin analyzed by spectroscopy
title_fullStr Interaction of gallic acid with trypsin analyzed by spectroscopy
title_full_unstemmed Interaction of gallic acid with trypsin analyzed by spectroscopy
title_short Interaction of gallic acid with trypsin analyzed by spectroscopy
title_sort interaction of gallic acid with trypsin analyzed by spectroscopy
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9351775/
https://www.ncbi.nlm.nih.gov/pubmed/28911378
http://dx.doi.org/10.1016/j.jfda.2014.09.001
work_keys_str_mv AT songhao interactionofgallicacidwithtrypsinanalyzedbyspectroscopy
AT chenchaoyin interactionofgallicacidwithtrypsinanalyzedbyspectroscopy
AT zhaoshenglan interactionofgallicacidwithtrypsinanalyzedbyspectroscopy
AT gefeng interactionofgallicacidwithtrypsinanalyzedbyspectroscopy
AT liudiqiu interactionofgallicacidwithtrypsinanalyzedbyspectroscopy
AT shidandan interactionofgallicacidwithtrypsinanalyzedbyspectroscopy
AT zhangtiancai interactionofgallicacidwithtrypsinanalyzedbyspectroscopy