title: Photochemical labeling of membrane-associated and channel-forming domains of proteins directed by energy transfer.
abstract: 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.
authors.affiliation: Laboratoire de Chimie Bio-organique, URA 1386 CNRS, Faculté de Pharmacie, Université Louis Pasteur Strasbourg, Illkirch, France.
authors.forename: L
authors.initials: L
authors.lastname: Peng
authors.forename: M L
authors.initials: ML
authors.lastname: Alcaraz
authors.forename: P
authors.initials: P
authors.lastname: Klotz
authors.forename: F
authors.initials: F
authors.lastname: Kotzyba-Hibert
authors.forename: M
authors.initials: M
authors.lastname: Goeldner
mesh_terms: D000345:Affinity Labels; D002462:Cell Membrane / Q000378:metabolism; D004735:Energy Transfer; D007473:Ion Channels / Q000737:chemistry / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism; D010777:Photochemistry; D014364:Tryptophan / Q000378:metabolism
chemical_list: D000345:Affinity Labels; D007473:Ion Channels; D008565:Membrane Proteins; D010743:Phospholipids; D014364:Tryptophan