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Lipodisks integrated with weak affinity chromatography enable fragment screening of integral membrane proteins
Linnaeus University, Department of Chemistry and Biomedical Sciences, SE-39182 Kalmar, Sweden.
Linnaeus University, Department of Chemistry and Biomedical Sciences, SE-39182 Kalmar, Sweden.
Uppsala universitet, Teknisk-naturvetenskapliga vetenskapsområdet, Kemiska sektionen, Institutionen för kemi - BMC, Analytisk kemi.
Uppsala universitet, Teknisk-naturvetenskapliga vetenskapsområdet, Kemiska sektionen, Institutionen för kemi - BMC, Analytisk kemi.
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2016 (Engelska)Ingår i: The Analyst, ISSN 0003-2654, E-ISSN 1364-5528, Vol. 141, nr 3, s. 981-988Artikel i tidskrift (Refereegranskat) Published
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Abstract [en]

Membrane proteins constitute the largest class of drug targets but they present many challenges in drug discovery. Importantly, the discovery of potential drug candidates is hampered by the limited availability of efficient methods for screening drug-protein interactions. In this work we present a novel strategy for rapid identification of molecules capable of binding to a selected membrane protein. An integral membrane protein (human aquaporin-1) was incorporated into planar lipid bilayer disks (lipodisks), which were subsequently covalently coupled to porous derivatized silica and packed into HPLC columns. The obtained affinity columns were used in a typical protocol for fragment screening by weak affinity chromatography (WAC), in which one hit was identified out of a 200 compound collection. The lipodisk-based strategy, which ensures a stable and native-like lipid environment for the protein, is expected to work also with other membrane proteins and screening procedures.

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2016. Vol. 141, nr 3, s. 981-988
Nationell ämneskategori
Analytisk kemi
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URN: urn:nbn:se:uu:diva-269874DOI: 10.1039/C5AN02105GISI: 000368942600028PubMedID: 26673836OAI: oai:DiVA.org:uu-269874DiVA, id: diva2:885328
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VetenskapsrådetTillgänglig från: 2015-12-18 Skapad: 2015-12-18 Senast uppdaterad: 2017-12-01Bibliografiskt granskad

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