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Effects of Detergent Micelles on Lipid Binding to Proteins in Electrospray Ionization Mass Spectrometry
Univ Oxford, Phys & Theoret Chem Lab, Dept Chem, South Parks Rd, Oxford OX1 3QZ, Oxon, England.;Karolinska Inst, Department Microbiol Tumour & Cell Biol, SE-17165 Stockholm, Sweden.;Sci Life Lab, SE-17165 Stockholm, Sweden..
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Biochemistry. (Marklund grupp)
Univ Oxford, Phys & Theoret Chem Lab, Dept Chem, South Parks Rd, Oxford OX1 3QZ, Oxon, England..
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Biochemistry. (Marklund grupp)ORCID iD: 0000-0002-9804-5009
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2017 (English)In: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 89, no 14, p. 7425-7430Article in journal (Refereed) Published
Abstract [en]

A wide variety of biological processes rely upon interactions between proteins and lipids, ranging from molecular transport to the organization of the cell membrane. It was recently established that electrospray ionization mass spectrometry (ESI-MS) is capable of capturing transient interactions between membrane proteins and their lipid environment, and a detailed understanding of the underlying processes is therefore of high importance. Here, we apply ESIMS to investigate the factors that govern complex formation in solution and gas phases by comparing nonselective lipid binding with soluble and membrane proteins. We find that exogenously added lipids did not bind to soluble proteins, suggesting that lipids have a low propensity to form electrospray ionization adducts. The presence of detergents at increasing micelle concentrations, on the other hand, resulted in moderate lipid binding to soluble proteins. A direct ESI-MS comparison of lipid binding to the soluble protein serum albumin and to the integral membrane protein NapA shows that soluble proteins acquire fewer lipid adducts. Our results suggest that protein lipid complexes form via contacts between proteins and mixed lipid/detergent micelles. For soluble proteins, these complexes arise from nonspecific contacts between the protein and detergent/lipid micelles in the electrospray droplet. For membrane proteins, lipids are incorporated into the surrounding micelle in solution, and complex formation occurs independently of the ESI process. We conclude that the lipids in the resulting complexes interact predominantly with sites located in the transmembrane segments, resulting in nativelike complexes that can be interrogated by MS.

Place, publisher, year, edition, pages
2017. Vol. 89, no 14, p. 7425-7430
National Category
Analytical Chemistry
Identifiers
URN: urn:nbn:se:uu:diva-332417DOI: 10.1021/acs.analchem.7b00922ISI: 000406085300021OAI: oai:DiVA.org:uu-332417DiVA, id: diva2:1154479
Funder
Swedish Research CouncilWellcome trust, 104633/Z/14/ZAvailable from: 2017-11-02 Created: 2017-11-02 Last updated: 2018-02-23

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Costeira-Paulo, JoanaMarklund, Erik

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