Photochemical labeling of membrane-associated and channel-forming domains of proteins directed by energy transfer

• Published in: FEBS Letters Vol. 346; no. 1; pp. 127 - 131
• Main Authors: Peng, Ling, Alcaraz, Marie-Lyne, Klotz, Philippe, Kotzyba-Hibert, Florence, Goeldner, Maurice
• Format: Book Review Journal Article
• Language: English
• Published: England Elsevier B.V 06.06.1994
• Subjects: Affinity Labels; Cell Membrane - metabolism; Energy Transfer; Hydrophobic labeling; Ion Channels - chemistry; Ion Channels - metabolism; Membrane Proteins - chemistry; Membrane Proteins - metabolism; Phospholipids - metabolism; Photoactivatable permeant; Photoactivatable phospholipid; Photochemistry; Photolabeling; Tryptophan - metabolism; Hydrophobic labeling; Photolabeling; Photoactivatable permeant; Energy transfer; Photoactivatable phospholipid
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(94)00392-0

Singlet—singlet energy transfer reactions from excited tryptophan residues to photoactivatable probes possessing a suitable chromophore, generate reactive species in the vicinity of the protein, leading to its covalent labeling. This delayed labeling process can be used to map the membrane-surrounded regions of proteins with improved efficiency when it is applied with appropriate photoactivatable phospholipids. The same principle could also be applied to the labeling of channel-forming transmembrane domains of ion channels, provided that suitable photoactivatable permeant ions were available. Both applications will be discussed with regard to their potential and feasibility.