Exploring the fluorescence quenching interaction of amino acids and protein with natural organic matter by a multi-spectroscopic method

The main objective of this research was to explore the fluorescence quenching mechanism of a humic substance (Suwannee River natural organic matter (SWNOM)) to amino acids (tryptophan, tyrosine) and protein (bovine serum albumin, (BSA)) by multi-spectroscopic methods. The locations of the peaks of t...

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Autores principales:	Kornravee Saipetch, Rajendra Khanal, Masaki Yamazaki, Qing-Long Fu, Chihiro Yoshimura, Xin Kai Jin
Formato:	article
Lenguaje:	EN
Publicado:	IWA Publishing 2021
Materias:	bovine serum albumin fluorescence quenching fluorescence titration parafac tryptophan tyrosine Water supply for domestic and industrial purposes TD201-500 River, lake, and water-supply engineering (General) TC401-506
Acceso en línea:	https://doaj.org/article/bb8053c8c3534aeba44fea921ec13237
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spelling	oai:doaj.org-article:bb8053c8c3534aeba44fea921ec132372021-11-23T18:55:42ZExploring the fluorescence quenching interaction of amino acids and protein with natural organic matter by a multi-spectroscopic method1606-97491607-079810.2166/ws.2021.103https://doaj.org/article/bb8053c8c3534aeba44fea921ec132372021-11-01T00:00:00Zhttp://ws.iwaponline.com/content/21/7/3402https://doaj.org/toc/1606-9749https://doaj.org/toc/1607-0798The main objective of this research was to explore the fluorescence quenching mechanism of a humic substance (Suwannee River natural organic matter (SWNOM)) to amino acids (tryptophan, tyrosine) and protein (bovine serum albumin, (BSA)) by multi-spectroscopic methods. The locations of the peaks of tryptophan, tyrosine, and BSA from Parallel Factor Analysis were at Ex/Em 280/356 nm, 275/302 nm, and 280/344 nm, respectively. For SWNOM, two peaks appeared at Ex/Em of 240/448 nm, and 350/450 nm. Static quenching was the dominant quenching mechanism between BSA and SWNOM, whereas no quenching was observed between tryptophan or tyrosine and SWNOM. Fourier-transform infrared spectroscopy and thermodynamic calculation demonstrated that hydrogen bonding and van der Waals force are the potential binding forces of the BSA-SWNOM complex, as a result of rearrangement in the secondary polypeptide carbonyl hydrogen bonding network of BSA. This rearrangement led to the conformational change in BSA that induced quenching of BSA fluorescence by SWNOM. HIGHLIGHTS No quenching of tyrosine and tryptophan by Suwannee River natural organic matter (SWNOM).; Quenching of bovine serum albumin (BSA) by SWNOM occurs only when BSA is in the tertiary structure.; FTIR amide I peak of BSA was shifted on the addition of SWNOM.; Non-covalent bonding forms and quenching is static between BSA and SWNOM.;Kornravee SaipetchRajendra KhanalMasaki YamazakiQing-Long FuChihiro YoshimuraXin Kai JinIWA Publishingarticlebovine serum albuminfluorescence quenchingfluorescence titrationparafactryptophantyrosineWater supply for domestic and industrial purposesTD201-500River, lake, and water-supply engineering (General)TC401-506ENWater Supply, Vol 21, Iss 7, Pp 3402-3415 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	bovine serum albumin fluorescence quenching fluorescence titration parafac tryptophan tyrosine Water supply for domestic and industrial purposes TD201-500 River, lake, and water-supply engineering (General) TC401-506
spellingShingle	bovine serum albumin fluorescence quenching fluorescence titration parafac tryptophan tyrosine Water supply for domestic and industrial purposes TD201-500 River, lake, and water-supply engineering (General) TC401-506 Kornravee Saipetch Rajendra Khanal Masaki Yamazaki Qing-Long Fu Chihiro Yoshimura Xin Kai Jin Exploring the fluorescence quenching interaction of amino acids and protein with natural organic matter by a multi-spectroscopic method
description	The main objective of this research was to explore the fluorescence quenching mechanism of a humic substance (Suwannee River natural organic matter (SWNOM)) to amino acids (tryptophan, tyrosine) and protein (bovine serum albumin, (BSA)) by multi-spectroscopic methods. The locations of the peaks of tryptophan, tyrosine, and BSA from Parallel Factor Analysis were at Ex/Em 280/356 nm, 275/302 nm, and 280/344 nm, respectively. For SWNOM, two peaks appeared at Ex/Em of 240/448 nm, and 350/450 nm. Static quenching was the dominant quenching mechanism between BSA and SWNOM, whereas no quenching was observed between tryptophan or tyrosine and SWNOM. Fourier-transform infrared spectroscopy and thermodynamic calculation demonstrated that hydrogen bonding and van der Waals force are the potential binding forces of the BSA-SWNOM complex, as a result of rearrangement in the secondary polypeptide carbonyl hydrogen bonding network of BSA. This rearrangement led to the conformational change in BSA that induced quenching of BSA fluorescence by SWNOM. HIGHLIGHTS No quenching of tyrosine and tryptophan by Suwannee River natural organic matter (SWNOM).; Quenching of bovine serum albumin (BSA) by SWNOM occurs only when BSA is in the tertiary structure.; FTIR amide I peak of BSA was shifted on the addition of SWNOM.; Non-covalent bonding forms and quenching is static between BSA and SWNOM.;
format	article
author	Kornravee Saipetch Rajendra Khanal Masaki Yamazaki Qing-Long Fu Chihiro Yoshimura Xin Kai Jin
author_facet	Kornravee Saipetch Rajendra Khanal Masaki Yamazaki Qing-Long Fu Chihiro Yoshimura Xin Kai Jin
author_sort	Kornravee Saipetch
title	Exploring the fluorescence quenching interaction of amino acids and protein with natural organic matter by a multi-spectroscopic method
title_short	Exploring the fluorescence quenching interaction of amino acids and protein with natural organic matter by a multi-spectroscopic method
title_full	Exploring the fluorescence quenching interaction of amino acids and protein with natural organic matter by a multi-spectroscopic method
title_fullStr	Exploring the fluorescence quenching interaction of amino acids and protein with natural organic matter by a multi-spectroscopic method
title_full_unstemmed	Exploring the fluorescence quenching interaction of amino acids and protein with natural organic matter by a multi-spectroscopic method
title_sort	exploring the fluorescence quenching interaction of amino acids and protein with natural organic matter by a multi-spectroscopic method
publisher	IWA Publishing
publishDate	2021
url	https://doaj.org/article/bb8053c8c3534aeba44fea921ec13237
work_keys_str_mv	AT kornraveesaipetch exploringthefluorescencequenchinginteractionofaminoacidsandproteinwithnaturalorganicmatterbyamultispectroscopicmethod AT rajendrakhanal exploringthefluorescencequenchinginteractionofaminoacidsandproteinwithnaturalorganicmatterbyamultispectroscopicmethod AT masakiyamazaki exploringthefluorescencequenchinginteractionofaminoacidsandproteinwithnaturalorganicmatterbyamultispectroscopicmethod AT qinglongfu exploringthefluorescencequenchinginteractionofaminoacidsandproteinwithnaturalorganicmatterbyamultispectroscopicmethod AT chihiroyoshimura exploringthefluorescencequenchinginteractionofaminoacidsandproteinwithnaturalorganicmatterbyamultispectroscopicmethod AT xinkaijin exploringthefluorescencequenchinginteractionofaminoacidsandproteinwithnaturalorganicmatterbyamultispectroscopicmethod
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Exploring the fluorescence quenching interaction of amino acids and protein with natural organic matter by a multi-spectroscopic method

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