Pollutant-induced modulation in conformation and β-lactamase activity of human serum albumin.

Structural changes in human serum albumin (HSA) induced by the pollutants 1-naphthol, 2-naphthol and 8-quinolinol were analyzed by circular dichroism, fluorescence spectroscopy and dynamic light scattering. The alteration in protein conformational stability was determined by helical content inductio...

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Autores principales:	Ejaz Ahmad, Gulam Rabbani, Nida Zaidi, Basir Ahmad, Rizwan Hasan Khan
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/3193bb8cb78d4ee0ab144d9aefe4b9ee
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spelling	oai:doaj.org-article:3193bb8cb78d4ee0ab144d9aefe4b9ee2021-11-18T07:16:05ZPollutant-induced modulation in conformation and β-lactamase activity of human serum albumin.1932-620310.1371/journal.pone.0038372https://doaj.org/article/3193bb8cb78d4ee0ab144d9aefe4b9ee2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22685563/?tool=EBIhttps://doaj.org/toc/1932-6203Structural changes in human serum albumin (HSA) induced by the pollutants 1-naphthol, 2-naphthol and 8-quinolinol were analyzed by circular dichroism, fluorescence spectroscopy and dynamic light scattering. The alteration in protein conformational stability was determined by helical content induction (from 55 to 75%) upon protein-pollutant interactions. Domain plasticity is responsible for the temperature-mediated unfolding of HSA. These findings were compared to HSA-hydrolase activity. We found that though HSA is a monomeric protein, it shows heterotropic allostericity for β-lactamase activity in the presence of pollutants, which act as K- and V-type non-essential activators. Pollutants cause conformational changes and catalytic modifications of the protein (increase in β-lactamase activity from 100 to 200%). HSA-pollutant interactions mediate other protein-ligand interactions, such as HSA-nitrocefin. Therefore, this protein can exist in different conformations with different catalytic properties depending on activator binding. This is the first report to demonstrate the catalytic allostericity of HSA through a mechanistic approach. We also show a correlation with non-microbial drug resistance as HSA is capable of self-hydrolysis of β-lactam drugs, which is further potentiated by pollutants due to conformational changes in HSA.Ejaz AhmadGulam RabbaniNida ZaidiBasir AhmadRizwan Hasan KhanPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 6, p e38372 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ejaz Ahmad Gulam Rabbani Nida Zaidi Basir Ahmad Rizwan Hasan Khan Pollutant-induced modulation in conformation and β-lactamase activity of human serum albumin.
description	Structural changes in human serum albumin (HSA) induced by the pollutants 1-naphthol, 2-naphthol and 8-quinolinol were analyzed by circular dichroism, fluorescence spectroscopy and dynamic light scattering. The alteration in protein conformational stability was determined by helical content induction (from 55 to 75%) upon protein-pollutant interactions. Domain plasticity is responsible for the temperature-mediated unfolding of HSA. These findings were compared to HSA-hydrolase activity. We found that though HSA is a monomeric protein, it shows heterotropic allostericity for β-lactamase activity in the presence of pollutants, which act as K- and V-type non-essential activators. Pollutants cause conformational changes and catalytic modifications of the protein (increase in β-lactamase activity from 100 to 200%). HSA-pollutant interactions mediate other protein-ligand interactions, such as HSA-nitrocefin. Therefore, this protein can exist in different conformations with different catalytic properties depending on activator binding. This is the first report to demonstrate the catalytic allostericity of HSA through a mechanistic approach. We also show a correlation with non-microbial drug resistance as HSA is capable of self-hydrolysis of β-lactam drugs, which is further potentiated by pollutants due to conformational changes in HSA.
format	article
author	Ejaz Ahmad Gulam Rabbani Nida Zaidi Basir Ahmad Rizwan Hasan Khan
author_facet	Ejaz Ahmad Gulam Rabbani Nida Zaidi Basir Ahmad Rizwan Hasan Khan
author_sort	Ejaz Ahmad
title	Pollutant-induced modulation in conformation and β-lactamase activity of human serum albumin.
title_short	Pollutant-induced modulation in conformation and β-lactamase activity of human serum albumin.
title_full	Pollutant-induced modulation in conformation and β-lactamase activity of human serum albumin.
title_fullStr	Pollutant-induced modulation in conformation and β-lactamase activity of human serum albumin.
title_full_unstemmed	Pollutant-induced modulation in conformation and β-lactamase activity of human serum albumin.
title_sort	pollutant-induced modulation in conformation and β-lactamase activity of human serum albumin.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/3193bb8cb78d4ee0ab144d9aefe4b9ee
work_keys_str_mv	AT ejazahmad pollutantinducedmodulationinconformationandblactamaseactivityofhumanserumalbumin AT gulamrabbani pollutantinducedmodulationinconformationandblactamaseactivityofhumanserumalbumin AT nidazaidi pollutantinducedmodulationinconformationandblactamaseactivityofhumanserumalbumin AT basirahmad pollutantinducedmodulationinconformationandblactamaseactivityofhumanserumalbumin AT rizwanhasankhan pollutantinducedmodulationinconformationandblactamaseactivityofhumanserumalbumin
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Pollutant-induced modulation in conformation and β-lactamase activity of human serum albumin.

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