907278
H-L-Photo-leucine HCl
≥98%
别名:
(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
经验公式（希尔记法）:
C5H10ClN3O2
分子量:
179.60
UNSPSC代码:
12352209
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方案
≥98%
表单
solid
反应适用性
reaction type: solution phase peptide synthesis
存货情况
available only in USA
应用
peptide synthesis
储存温度
−20°C
应用
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.
其他说明
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)
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价格
警示用语：
Danger
危险声明
危险分类
Self-react. C
储存分类代码
5.2 - Organic peroxides and self-reacting hazardous materials
WGK
WGK 3
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(4), 633-645 (2016-01-29)
Noncovalent complexes of hydrophobic peptides GLLLG and GLLLK with photoleucine (L*) tagged peptides G(L* n L m )K (n = 1,3, m = 2,0) were generated as singly charged ions in the gas phase and probed by photodissociation at 355
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
En-Wei Lin et al.
Bioconjugate chemistry, 25(10), 1902-1909 (2014-10-16)
A photoactivated, site-selective conjugation of poly(ethylene glycol) (PEG) to the glutathione (GSH) binding pocket of glutathione S-transferase (GST) is described. To achieve this, a GSH analogue (GSH-BP) was designed and chemically synthesized with three functionalities: (1) the binding affinity of
Knut Kölbel et al.
Angewandte Chemie (International ed. in English), 51(50), 12602-12605 (2012-10-31)
Photochemical cross-linking was applied to trap intramolecular interactions in peptides. The incorporation of diazirine-labeled amino acid analogues in combination with high-resolution mass spectrometry made it possible to catch reverse-turn conformations within peptides, exactly map their self-interacting surfaces, and discriminate between
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