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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| Format: | Article |
| Language: | English |
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Elsevier
2022-01-01
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| Series: | Journal of King Saud University: Science |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S1018364721003360 |
| _version_ | 1819093528147394560 |
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| author | Javed Masood Khan Ajamaluddin Malik Mohammad Z. Ahmed |
| author_facet | Javed Masood Khan Ajamaluddin Malik Mohammad Z. Ahmed |
| author_sort | Javed Masood Khan |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-21T23:12:56Z |
| format | Article |
| id | doaj.art-89474100eeb5431fb9cbddd1442f4952 |
| institution | Directory Open Access Journal |
| issn | 1018-3647 |
| language | English |
| last_indexed | 2024-12-21T23:12:56Z |
| publishDate | 2022-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of King Saud University: Science |
| spelling | doaj.art-89474100eeb5431fb9cbddd1442f49522022-12-21T18:47:00ZengElsevierJournal of King Saud University: Science1018-36472022-01-01341101674Bimolecular interaction of zwitterionic surfactant with hen egg white lysozyme (HEWL): A biophysical studyJaved Masood Khan0Ajamaluddin Malik1Mohammad Z. Ahmed2Department of Food Science and Nutrition, Faculty of Food and Agricultural Sciences, King Saud University, 2460, Riyadh 11451, Saudi Arabia; Corresponding authors.Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi ArabiaDepartment of Pharmacognosy, College of Pharmacy, King Saud University, Riyadh, Saudi ArabiaThe 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.http://www.sciencedirect.com/science/article/pii/S1018364721003360CHAPSHen egg white lysozymeZwitterionic surfactantpH and conformation |
| spellingShingle | Javed Masood Khan Ajamaluddin Malik Mohammad Z. Ahmed Bimolecular interaction of zwitterionic surfactant with hen egg white lysozyme (HEWL): A biophysical study Journal of King Saud University: Science CHAPS Hen egg white lysozyme Zwitterionic surfactant pH and conformation |
| title | 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_short | 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 |
| topic | CHAPS Hen egg white lysozyme Zwitterionic surfactant pH and conformation |
| url | http://www.sciencedirect.com/science/article/pii/S1018364721003360 |
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