Probing the membrane interface-interacting proteome using photoactivatable lipid cross-linkers.

Journal article

To analyze proteins interacting at the membrane interface, a phospholipid analogue was used with a photoactivatable headgroup (ASA-DLPE, N-(4-azidosalicylamidyl)-1,2-dilauroyl-sn-glycero-3-phosphoethanolamine) for selective cross-linking. The peripheral membrane protein cytochrome c from the inner mitochondrial membrane was rendered carbonate wash-resistant by cross-linking to ASA-DLPE in a model membrane system, validating our approach. Cross-link products of cytochrome c and its precursor a...

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Authors: Gubbens, J; Vader, P; Damen, J; O'Flaherty, M; Slijper, M

• Journal: Journal of proteome research
• Volume: 6
• Issue: 5
• Pages: 1951-1962
• Publication date: 2007-05-01
• DOI: 10.1021/pr060561a
• EISSN: 1535-3907
• ISSN: 1535-3893
• Language: English
• Keywords: Molecular Structure; Ultraviolet Rays; Cytochromes c; Cell Membrane; Chromatography, Liquid; Mitochondria; Cross-Linking Reagents; Phospholipids; Saccharomyces cerevisiae; Proteome; Tandem Mass Spectrometry; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Animals; Saccharomyces cerevisiae Proteins