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Merck
CN
所有图片(1)

文件

907278

Sigma-Aldrich

H-L-Photo-leucine HCl

≥98%

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所有图片(1)
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
经验公式（希尔记法）:
C5H10ClN3O2
分子量:
179.60
UNSPSC代码:
12352200

检测方案

≥98%

形式

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)

象形图

Flame
GHS02

警示用语：

Danger

危险声明

H242

危险分类

Self-react. C

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(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
Jay M Janz et al.
Journal of the American Chemical Society, 133(40), 15878-15881 (2011-09-13)
Cell surface heptahelical G protein-coupled receptors (GPCRs) mediate critical cellular signaling pathways and are important pharmaceutical drug targets. (1) In addition to traditional small-molecule approaches, lipopeptide-based GPCR-derived pepducins have emerged as a new class of pharmaceutical agents. (2, 3)
Nicholas Vance et al.
Bioconjugate chemistry, 30(1), 148-160 (2018-12-20)
Site-specific conjugation of small molecules to antibodies represents an attractive goal for the development of more homogeneous targeted therapies and diagnostics. Most site-specific conjugation strategies require modification or removal of antibody glycans or interchain disulfide bonds or engineering of an
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