Bimolecular interaction of zwitterionic surfactant with hen egg white lysozyme (HEWL): A biophysical study

The interaction between Hen Egg White Lysozyme (HEWL) and 3-[(3-cholamidopropyl) dimethyl-ammonio]-1-propanesulphonate (CHAPS) was examined using biophysical techniques (spectrofluorometric, circular dichroism, and dynamic light scattering) at pH 9.0. The results obtained from multi-techniques showe...

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Autores principales:	Javed Masood Khan, Ajamaluddin Malik, Mohammad Z. Ahmed
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2022
Materias:	CHAPS Hen egg white lysozyme Zwitterionic surfactant pH and conformation Science (General) Q1-390
Acceso en línea:	https://doaj.org/article/89474100eeb5431fb9cbddd1442f4952
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spelling	oai:doaj.org-article:89474100eeb5431fb9cbddd1442f49522021-11-10T04:21:05ZBimolecular interaction of zwitterionic surfactant with hen egg white lysozyme (HEWL): A biophysical study1018-364710.1016/j.jksus.2021.101674https://doaj.org/article/89474100eeb5431fb9cbddd1442f49522022-01-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S1018364721003360https://doaj.org/toc/1018-3647The interaction between Hen Egg White Lysozyme (HEWL) and 3-[(3-cholamidopropyl) dimethyl-ammonio]-1-propanesulphonate (CHAPS) was examined using biophysical techniques (spectrofluorometric, circular dichroism, and dynamic light scattering) at pH 9.0. The results obtained from multi-techniques showed that CHAPS interact with the HEWL strongly and affects protein conformations. The far-UV CD results suggest that lower as well as higher (1.0–15.0 mM) concentrations of CHAPS are inducing α-helical structure in HEWL. The near-UV CD and fluorescence data indicated that the tertiary structure of HEWL is alter in the presence of CHAPS. The ANS dye binding suggest that the exposure of HEWL tertiary structure is dependent on CHAPS concentration. As the concentrations of CHAPS is increasing the exposure of HEWL tertiary structure is also increasing and maximum exposure was found at 15.0 mM of CHAPS concentrations. The hydrodynamic radii of HEWL is also increase in the presence of sub-micellar and micellar concentrations of CHAPS because the tertiary structure of HEWL is disrupted. Overall, the results suggest that CHAPS is inducing secondary structure and disrupting tertiary structure of HEWL. This study provides detailed interaction of CHAPS with HEWL at the molecular level.Javed Masood KhanAjamaluddin MalikMohammad Z. AhmedElsevierarticleCHAPSHen egg white lysozymeZwitterionic surfactantpH and conformationScience (General)Q1-390ENJournal of King Saud University: Science, Vol 34, Iss 1, Pp 101674- (2022)
institution	DOAJ
collection	DOAJ
language	EN
topic	CHAPS Hen egg white lysozyme Zwitterionic surfactant pH and conformation Science (General) Q1-390
spellingShingle	CHAPS Hen egg white lysozyme Zwitterionic surfactant pH and conformation Science (General) Q1-390 Javed Masood Khan Ajamaluddin Malik Mohammad Z. Ahmed Bimolecular interaction of zwitterionic surfactant with hen egg white lysozyme (HEWL): A biophysical study
description	The interaction between Hen Egg White Lysozyme (HEWL) and 3-[(3-cholamidopropyl) dimethyl-ammonio]-1-propanesulphonate (CHAPS) was examined using biophysical techniques (spectrofluorometric, circular dichroism, and dynamic light scattering) at pH 9.0. The results obtained from multi-techniques showed that CHAPS interact with the HEWL strongly and affects protein conformations. The far-UV CD results suggest that lower as well as higher (1.0–15.0 mM) concentrations of CHAPS are inducing α-helical structure in HEWL. The near-UV CD and fluorescence data indicated that the tertiary structure of HEWL is alter in the presence of CHAPS. The ANS dye binding suggest that the exposure of HEWL tertiary structure is dependent on CHAPS concentration. As the concentrations of CHAPS is increasing the exposure of HEWL tertiary structure is also increasing and maximum exposure was found at 15.0 mM of CHAPS concentrations. The hydrodynamic radii of HEWL is also increase in the presence of sub-micellar and micellar concentrations of CHAPS because the tertiary structure of HEWL is disrupted. Overall, the results suggest that CHAPS is inducing secondary structure and disrupting tertiary structure of HEWL. This study provides detailed interaction of CHAPS with HEWL at the molecular level.
format	article
author	Javed Masood Khan Ajamaluddin Malik Mohammad Z. Ahmed
author_facet	Javed Masood Khan Ajamaluddin Malik Mohammad Z. Ahmed
author_sort	Javed Masood Khan
title	Bimolecular interaction of zwitterionic surfactant with hen egg white lysozyme (HEWL): A biophysical study
title_short	Bimolecular interaction of zwitterionic surfactant with hen egg white lysozyme (HEWL): A biophysical study
title_full	Bimolecular interaction of zwitterionic surfactant with hen egg white lysozyme (HEWL): A biophysical study
title_fullStr	Bimolecular interaction of zwitterionic surfactant with hen egg white lysozyme (HEWL): A biophysical study
title_full_unstemmed	Bimolecular interaction of zwitterionic surfactant with hen egg white lysozyme (HEWL): A biophysical study
title_sort	bimolecular interaction of zwitterionic surfactant with hen egg white lysozyme (hewl): a biophysical study
publisher	Elsevier
publishDate	2022
url	https://doaj.org/article/89474100eeb5431fb9cbddd1442f4952
work_keys_str_mv	AT javedmasoodkhan bimolecularinteractionofzwitterionicsurfactantwithheneggwhitelysozymehewlabiophysicalstudy AT ajamaluddinmalik bimolecularinteractionofzwitterionicsurfactantwithheneggwhitelysozymehewlabiophysicalstudy AT mohammadzahmed bimolecularinteractionofzwitterionicsurfactantwithheneggwhitelysozymehewlabiophysicalstudy
_version_	1718440671651561472

Bimolecular interaction of zwitterionic surfactant with hen egg white lysozyme (HEWL): A biophysical study

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