Structures of bovine, equine and leporine serum albumin

Bujacz, A.

doi:10.1107/s0907444912027047

Cited by 696 publications

(591 citation statements)

References 62 publications

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“…One (dry, crystalline) BSA molecule has a volume of about 154 nm 3 (Bujacz, 2012). In a flat orientation (4.4 nm layer height and a projecting area of 35 nm 2 molecule −1 ) 3.64 × 10 14 molecules (40.5 µg; 0.32 µg cm −2 ) of BSA are needed to form one complete monolayer in the flow tube (i.d.…”

Section: Impact Of Coating Thicknessmentioning

confidence: 99%

Light-induced protein nitration and degradation with HONO emission

et al. 2017

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Abstract. Proteins can be nitrated by air pollutants (NO 2 ), enhancing their allergenic potential. This work provides insight into protein nitration and subsequent decomposition in the presence of solar radiation. We also investigated lightinduced formation of nitrous acid (HONO) from protein surfaces that were nitrated either online with instantaneous gas-phase exposure to NO 2 or offline by an efficient nitration agent (tetranitromethane, TNM). Bovine serum albumin (BSA) and ovalbumin (OVA) were used as model substances for proteins. Nitration degrees of about 1 % were derived applying NO 2 concentrations of 100 ppb under VIS/UV illuminated conditions, while simultaneous decomposition of (nitrated) proteins was also found during long-term (20 h) irradiation exposure. Measurements of gas exchange on TNMnitrated proteins revealed that HONO can be formed and released even without contribution of instantaneous heterogeneous NO 2 conversion. NO 2 exposure was found to increase HONO emissions substantially. In particular, a strong dependence of HONO emissions on light intensity, relative humidity, NO 2 concentrations and the applied coating thickness was found. The 20 h long-term studies revealed sustained HONO formation, even when concentrations of the intact (nitrated) proteins were too low to be detected after the gas exchange measurements. A reaction mechanism for the NO 2 conversion based on the Langmuir-Hinshelwood kinetics is proposed.

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Section: Impact Of Coating Thicknessmentioning

confidence: 99%

Light-induced protein nitration and degradation with HONO emission

et al. 2017

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“…1). 23 As the pH lowers toward more acidic conditions, the BSA molecule extends its structure, becoming more linear. 15,16 The extended (E) form of BSA exists below pH 4.0.…”

Section: Introductionmentioning

confidence: 99%

Adsorption of bovine serum albumin on silicon dioxide nanoparticles: Impact of pH on nanoparticle–protein interactions

et al. 2017

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Bovine serum albumin (BSA) adsorbed on amorphous silicon dioxide (SiO2) nanoparticles was studied as a function of pH across the range of 2 to 8. Aggregation, surface charge, surface coverage, and protein structure were investigated over this entire pH range. SiO2 nanoparticle aggregation is found to depend upon pH and differs in the presence of adsorbed BSA. For SiO2 nanoparticles truncated with hydroxyl groups, the largest aggregates were observed at pH 3, close to the isoelectric point of SiO2 nanoparticles, whereas for SiO2 nanoparticles with adsorbed BSA, the aggregate size was the greatest at pH 3.7, close to the isoelectric point of the BSA-SiO2 complex. Surface coverage of BSA was also the greatest at the isoelectric point of the BSA-SiO2 complex with a value of ca. 3 ± 1 × 1011 molecules cm−2. Furthermore, the secondary protein structure was modified when compared to the solution phase at all pH values, but the most significant differences were seen at pH 7.4 and below. It is concluded that protein–nanoparticle interactions vary with solution pH, which may have implications for nanoparticles in different biological fluids (e.g., blood, stomach, and lungs).

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“…These four residues are conserved in albumins from mammals. A copious amount of X-ray crystallographic studies have been carried out on HSA [44][45][46][47][48][49][50][51][52][53], with structural information on other serum albumins having become available recently [54,55]. Inspection of these structures reveals that the MBS is consistently only present in fatty acid-free preparations [33] (Figure 1c).…”

Section: +mentioning

confidence: 99%

Fatty Acid-Mediated Inhibition of Metal Binding to the Multi-Metal Site on Serum Albumin: Implications for Cardiovascular Disease

Blindauer

Khazaipoul²,

Yu³

et al. 2016

CTMC

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(2016) Fatty acid-mediated inhibition of metal binding to the multi-metal site on serum albumin : implications for cardiovascular disease. Current Trends in Medicinal Chemistry, 16. Permanent WRAP URL:http://wrap.warwick.ac.uk/78963 Copyright and reuse:The Warwick Research Archive Portal (WRAP) makes this work by researchers of the University of Warwick available open access under the following conditions. Copyright © and all moral rights to the version of the paper presented here belong to the individual author(s) and/or other copyright owners. To the extent reasonable and practicable the material made available in WRAP has been checked for eligibility before being made available.Copies of full items can be used for personal research or study, educational, or not-for-profit purposes without prior permission or charge. Provided that the authors, title and full bibliographic details are credited, a hyperlink and/or URL is given for the original metadata page and the content is not changed in any way.Publisher's statement: © Bentham Science Publishers. http://dx.doi.org/10.2174/1568026616666160216155927 A note on versions:The version presented here may differ from the published version or, version of record, if you wish to cite this item you are advised to consult the publisher's version. Please see the 'permanent WRAP URL' above for details on accessing the published version and note that access may require a subscription. Abstract: Human serum albumin (HSA) is the major protein in blood plasma and is responsible for circulatory transport of a range of small molecules including fatty acids, metal ions and drugs. We previously identified the major plasma Zn 2+ transport site on HSA and revealed that fatty-acid binding (at a distinct site called the FA2 site) and Zn 2+ binding are interdependent via an allosteric mechanism. Since binding affinities of long-chain fatty acids exceed those of plasma Zn 2+ , this means that under certain circumstances the binding of fatty acid molecules to HSA is likely to diminish HSA Zn 2+ -binding, and hence affects the control of circulatory and cellular Zn 2+ dynamics. This relationship between circulatory fatty acid and Zn 2+ dynamics is likely to have important physiological and pathological implications, especially since it has been recognised that Zn 2+ acts as a signalling agent in many cell types. Fatty acid levels in the blood are dynamic, but most importantly, chronic elevation of plasma fatty acid levels is associated with some metabolic disorders and disease states -including myocardial infarction and other cardiovascular diseases. In this article, we briefly review the metalbinding properties of albumin and highlight the importance of their interplay with fatty acid binding. We also consider the impact of this dynamic link upon levels and speciation of plasma Zn 2+ , its effect upon cellular Zn 2+ homeostasis and its relevance to cardiovascular and circulatory processes in health and disease.

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Structures of bovine, equine and leporine serum albumin

Cited by 696 publications

References 62 publications

Light-induced protein nitration and degradation with HONO emission

Light-induced protein nitration and degradation with HONO emission

Adsorption of bovine serum albumin on silicon dioxide nanoparticles: Impact of pH on nanoparticle–protein interactions

Fatty Acid-Mediated Inhibition of Metal Binding to the Multi-Metal Site on Serum Albumin: Implications for Cardiovascular Disease

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