Photochemical labeling of membrane-associated and channel-forming domains of proteins directed by energy transfer.
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.
Peng
L
L
Laboratoire de Chimie Bio-organique, URA 1386 CNRS, Faculté de Pharmacie, Université Louis Pasteur Strasbourg, Illkirch, France.
Alcaraz
M L
ML
Klotz
P
P
Kotzyba-Hibert
F
F
Goeldner
M
M
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
D000345:Affinity Labels; D007473:Ion Channels; D008565:Membrane Proteins; D010743:Phospholipids; D014364:Tryptophan