Photo-leucine

Structural formula
	Illustration of L -Photo-Leucine
General
Surname	Photo-leucine
other names	2-amino-4,4-azipentanoic acid; 3- (3-methyl-3-diazirinyl) alanine;
Molecular formula	C 5 H 9 N 3 O 2
Brief description	white to yellow-brown powder
External identifiers / databases
PubChem	24998139
ChemSpider	32980228
Wikidata	Q18353234
properties
Molar mass	143.14 g mol −1
Physical state	firmly
solubility	soluble in water: 10 g l −1 (25 ° C)
safety instructions
GHS labeling of hazardous substances	no GHS pictograms
	no GHS pictograms
H and P phrases	H: no H-phrases
	P: no P-phrases
	As far as possible and customary, SI units are used. Unless otherwise noted, the data given apply to standard conditions .

Photo-leucine is a synthetic derivative of the amino acid leucine . It carries a diazirine group which, compared to leucine, replaces a methyl group . It is used in biochemistry for photoaffinity labeling . For this purpose, the isomerically pure L -photo-leucine corresponding to naturally occurring L -leucine is usually used.

properties

When exposed to UV radiation , the diazirine group forms carbenes that react unspecifically with molecules in the immediate vicinity. This enables protein-protein interactions to be determined, since the reaction of the diazirine group with a binding protein results in a covalent crosslinking of these two molecules. The crosslinking of the two proteins can then be used for purification and detection , since at least one of the binding partners is known and so z. B. is purified with affinity chromatography or immunoprecipitation and detected with immunostaining . The advantages of photo-leucine are the small size of the reactive group, which tends to disrupt less protein-protein interactions, and the controllability of the cross-linking period. One disadvantage is the unselective reaction with an atom in the neighboring molecule, which can lead to a loss of the biological activity of the bound molecule. Since leucine occurs more frequently in β-sheets and β-loops , proteins that bind to them can be specifically identified.

Individual evidence

↑ ^a ^b ^c ^d data sheet L-Photo-Leucine at lifetechnologies.com, accessed on April 19, 2015.
^ M. Suchanek, A. Radzikowska, C. Thiele: Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells. In: Nature methods . Volume 2, Number 4, April 2005, pp. 261-267, doi : 10.1038 / nmeth752 , PMID 15782218 .
↑ AL MacKinnon, JL Garrison, RS Hegde, J. Taunton: Photo-leucine incorporation reveals the target of a cyclodepsipeptide inhibitor of cotranslational translocation. In: Journal of the American Chemical Society . Volume 129, number 47, November 2007, pp. 14560-14561, doi : 10.1021 / ja076250y , PMID 17983236 , PMC 2574519 (free full text).
↑ C. Iacobucci, S. Reale, F. De Angelis: Photoactivable amino acid bioisosteres and mass spectrometry: snapshots of in vivo 3D protein structures. In: ChemBioChem . Volume 14, number 2, January 2013, pp. 181-183, doi : 10.1002 / cbic.201200742 , PMID 23280986 .

[LifeTech-1] ta sheet L-Photo-Leucine at lifetechnologies.com, accessed on April 19, 2015.

[2] M. Suchanek, A. Radzikowska, C. Thiele: Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells. In: Nature methods . Volume 2, Number 4, April 2005, pp. 261-267, doi : 10.1038 / nmeth752 , PMID 15782218 .

[3] AL MacKinnon, JL Garrison, RS Hegde, J. Taunton: Photo-leucine incorporation reveals the target of a cyclodepsipeptide inhibitor of cotranslational translocation. In: Journal of the American Chemical Society . Volume 129, number 47, November 2007, pp. 14560-14561, doi : 10.1021 / ja076250y , PMID 17983236 , PMC 2574519 (free full text).

[4] C. Iacobucci, S. Reale, F. De Angelis: Photoactivable amino acid bioisosteres and mass spectrometry: snapshots of in vivo 3D protein structures. In: ChemBioChem . Volume 14, number 2, January 2013, pp. 181-183, doi : 10.1002 / cbic.201200742 , PMID 23280986 .