ArticlePloS one2012
Pollutant-induced modulation in conformation and β-lactamase activity of human serum albumin.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 94 citations in OpenAlex.
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- Interactions of ferulic acid and ferulic acid methyl ester with endogenous proteins: Determination using the multi-methods.Heliyon · 2024Article
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- Kanamycin-Mediated Conformational Dynamics ofFrontiers in molecular biosciences · 2021Article
- Insights from a combination of theoretical and experimental methods for probing the biomolecular interactions between human serum albumin and clomiphene.RSC advances · 2018Article
- Structural characteristics of thermostable immunogenic outer membrane protein from Salmonella enterica serovar Typhi.Applied microbiology and biotechnology · 2014Article
- Toxicity of CdTe QDs with different sizes targeted to HSA investigated by two electrochemical methods.Molecular biology reports · 2013Article
- gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins.International journal of nanomedicine · 2013Article
- Reciprocal allosteric modulation of carbon monoxide and warfarin binding to ferrous human serum heme-albumin.PloS one · 2013Article
- Investigation of the interaction of naringin palmitate with bovine serum albumin: spectroscopic analysis and molecular docking.PloS one · 2013Article
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- Effect of pullulan nanoparticle surface charges on HSA complexation and drug release behavior of HSA-bound nanoparticles.PloS one · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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