907278
H-L-Photo-leucine HCl
≥98%
Synonyme(s) :
(S)-2-Amino-3-(3-methyl-3H-diazirin-3-yl)propanoic acid hydrochloride, (S)-2-Amino-3-(3H-diazirin-3-yl)butanoic acid hydrochloride, Diazirine amino acid, Photo-Leu, Photo-crosslinking amino acid, Photoprobe building block
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About This Item
Formule empirique (notation de Hill):
C5H10ClN3O2
Poids moléculaire :
179.60
Code UNSPSC :
12352209
Produits recommandés
Pureté
≥98%
Forme
solid
Capacité de réaction
reaction type: solution phase peptide synthesis
Disponibilité
available only in USA
Application(s)
peptide synthesis
Température de stockage
−20°C
Application
H-L-Photo-leucine HCl is a diazirine-containing leucine amino acid and multifunctional photo-crosslinker. Its incorporation into peptides or small-molecule probes and tools allows for photoaffinity labeling of cellular targets and protein-protein interactions upon UV light (∼360 nm) irradiation to form a covalent bond. This and other multifunctional probe building blocks will continue to accelerate drug discovery research for probing cellular mechanisms, target ID/validation, and understanding traditionally undruggable targets. An Fmoc-protected version is also available as 907391.
Autres remarques
Development, optimization, and structural characterization of an efficient peptide-based photoaffinity cross-linking reaction
for generation of homogeneous conjugates from wild-type antibodies
Mechanistic studies of a small-molecule modulator of SMN2 splicing
Protein-Polymer Conjugation via Ligand Affinity and Photoactivation of Glutathione S-Transferase
Direct Interaction between an Allosteric Agonist Pepducin and the Chemokine Receptor CXCR4
Photo-leucine and photo-methionine allow identification of protein-?protein interactions in living cells
Fishing for Drug Targets: A Focus on Diazirine Photoaffinity Probe Synthesis
Photo-affinity labeling (PAL) in chemical proteomics: a handy tool to investigate protein-protein interactions (PPIs)
for generation of homogeneous conjugates from wild-type antibodies
Mechanistic studies of a small-molecule modulator of SMN2 splicing
Protein-Polymer Conjugation via Ligand Affinity and Photoactivation of Glutathione S-Transferase
Direct Interaction between an Allosteric Agonist Pepducin and the Chemokine Receptor CXCR4
Photo-leucine and photo-methionine allow identification of protein-?protein interactions in living cells
Fishing for Drug Targets: A Focus on Diazirine Photoaffinity Probe Synthesis
Photo-affinity labeling (PAL) in chemical proteomics: a handy tool to investigate protein-protein interactions (PPIs)
Produit(s) apparenté(s)
Réf. du produit
Description
Tarif
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Self-react. C
Code de la classe de stockage
5.2 - Organic peroxides and self-reacting hazardous materials
Classe de danger pour l'eau (WGK)
WGK 3
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Bojie Zhang et al.
Journal of the American Society for Mass Spectrometry, 27(3), 552-555 (2015-12-19)
Protein footprinting combined with mass spectrometry provides a method to study protein structures and interactions. To improve further current protein footprinting methods, we adapted the fast photochemical oxidation of proteins (FPOP) platform to utilize carbenes as the footprinting reagent. A
Christopher J Shaffer et al.
Journal of the American Society for Mass Spectrometry, 27(7), 1176-1185 (2016-04-10)
We report a combined experimental and computational study aimed at elucidating the structure of N-terminal fragment ions of the c type produced by electron transfer dissociation of photo-leucine (L*) peptide ions GL*GGKX. The c 4 ion from GL*GGK is found
Lavanya K Iyer et al.
Molecular pharmaceutics, 10(12), 4629-4639 (2013-10-16)
Local side-chain interactions in lyophilized protein formulations were mapped using solid-state photolytic labeling-mass spectrometry (ssPL-MS). Photoactive amino acid analogues (PAAs) were used as probes and either added to the lyophilized matrix or incorporated within the amino acid sequence of a
Chanelle C Jumper et al.
Analytical chemistry, 84(10), 4411-4418 (2012-04-07)
Carbene chemistry has been used recently in structural mass spectrometry as a labeling method for mapping protein surfaces. The current study presents a method for quantitating label distribution at the amino acid level and explores the nature and basis for
Andrew L MacKinnon et al.
Journal of the American Chemical Society, 129(47), 14560-14561 (2007-11-07)
Photoaffinity labeling is a powerful tool to identify protein targets of biologically active small molecules, yet is often limited by the size, chemical properties, and availability of photoreactive groups. We report an improved synthesis of photo-leucine, a diazirine-based photoreactive analogue
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