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231226s2023 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.3c00249
|2 doi
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|a pubmed24n1184.xml
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|a (DE-627)NLM355321769
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|a (NLM)37027519
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|a DE-627
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|c DE-627
|e rakwb
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|a eng
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|a Enders, Abigail A
|e verfasserin
|4 aut
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|a New Insights into Cation- and Temperature-Driven Protein Adsorption to the Air-Water Interface through Infrared Reflection Studies of Bovine Serum Albumin
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|c 2023
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|a Date Completed 19.04.2023
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|a Date Revised 10.05.2023
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a The chemistry and structure of the air-ocean interface modulate biogeochemical processes between the ocean and atmosphere and therefore impact sea spray aerosol properties, cloud and ice nucleation, and climate. Protein macromolecules are enriched in the sea surface microlayer and have complex adsorption properties due to the unique molecular balance of hydrophobicity and hydrophilicity. Additionally, interfacial adsorption properties of proteins are of interest as important inputs for ocean climate modeling. Bovine serum albumin is used here as a model protein to investigate the dynamic surface behavior of proteins under several variable conditions including solution ionic strength, temperature, and the presence of a stearic acid (C17COOH) monolayer at the air-water interface. Key vibrational modes of bovine serum albumin are examined via infrared reflectance-absorbance spectroscopy, a specular reflection method that ratios out the solution phase and highlights the aqueous surface to determine, at a molecular level, the surface structural changes and factors affecting adsorption to the solution surface. Amide band reflection absorption intensities reveal the extent of protein adsorption under each set of conditions. Studies reveal the nuanced behavior of protein adsorption impacted by ocean-relevant sodium concentrations. Moreover, protein adsorption is most strongly affected by the synergistic effects of divalent cations and increased temperature
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|a Journal Article
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a Serum Albumin, Bovine
|2 NLM
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|a 27432CM55Q
|2 NLM
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|a Water
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|a 059QF0KO0R
|2 NLM
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|a Cations
|2 NLM
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|a Clark, Jessica B
|e verfasserin
|4 aut
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|a Elliott, Scott M
|e verfasserin
|4 aut
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|a Allen, Heather C
|e verfasserin
|4 aut
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 39(2023), 15 vom: 18. Apr., Seite 5505-5513
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|x 1520-5827
|7 nnns
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|g volume:39
|g year:2023
|g number:15
|g day:18
|g month:04
|g pages:5505-5513
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|u http://dx.doi.org/10.1021/acs.langmuir.3c00249
|3 Volltext
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