3350-19-4

Basic information

• Product Name: BOC-LEU-ONP
• Synonyms: N-TERT-BUTOXYCARBONYL-L-LEUCINE-P-NITROPHENYL ESTER;BOC-L-LEUCINE P-NITROPHENYL ESTER;BOC-L-LEUCINE 4-NITROPHENYL ESTER;BOC-LEUCINE-ONP;BOC-LEU-ONP;p-nitrophenyl N-(tert-butoxycarbonyl)-L-leucinate;(S)-2-(tert-Butoxycarbonylamino)-4-methylvaleric acid 4-nitrophenyl ester;N-[(1,1-Dimethylethoxy)carbonyl]-L-leucine 4-nitrophenyl ester
• CAS NO: 3350-19-4
• Molecular Formula: C₁₇H₂₄N₂O₆
• Molecular Weight: 352.38
• EINECS: 222-107-3
• Product Categories: Amino Acid Derivatives;Amino Acids
• Mol File: 3350-19-4.mol

Chemical Properties

• Boiling Point: 487.8 °C at 760 mmHg
• Flash Point: 248.8 °C
• Appearance: /
• Density: 1.172 g/cm³
• Vapor Pressure: 1.15E-09mmHg at 25°C
• Refractive Index: 1.518
• Storage Temp.: 2-8°C
• CAS DataBase Reference: BOC-LEU-ONP(CAS DataBase Reference)
• NIST Chemistry Reference: BOC-LEU-ONP(3350-19-4)
• EPA Substance Registry System: BOC-LEU-ONP(3350-19-4)

Safety Data

• WGK Germany: 3
• F: 8
• Hazardous Substances Data: 3350-19-4(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Research and Development:
BOC-LEU-ONP is used as a building block in the synthesis of peptides and peptidomimetics for the development of new drugs. Its role in solid-phase peptide synthesis allows for the creation of peptide chains with specific sequences, which are essential for the discovery and optimization of bioactive compounds.
Used in Peptide Chemistry:
BOC-LEU-ONP is utilized as a key intermediate in peptide chemistry, enabling the synthesis of complex peptide structures with potential therapeutic applications. Its presence in the synthesis process ensures the correct formation of peptide bonds and the desired peptide sequence, contributing to the advancement of peptide-based therapeutics.

InChI:InChI=1/C17H24N2O6/c1-11(2)10-14(18-16(21)25-17(3,4)5)15(20)24-13-8-6-12(7-9-13)19(22)23/h6-9,11,14H,10H2,1-5H3,(H,18,21)/t14-/m0/s1

Upstream product

• 100-02-7 4-nitro-phenol 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 

Downstream Products

• 83595-89-5 Boc-Leu-Gly-Asn-Gln-Trp(Mtb)-Ala-Val-Gly-His-Leu-Met-NH₂ 
• 82176-10-1 N-tert-butoxycarbonyl-L-leucyl-O-benzyl-L-tyrosyl-L-leucyl-L-valine methyl ester 
• 171618-06-7 BOC-Leu-His-Lys(Z)-Leu-Gln-Thr-OMe 
• 100-02-7 4-nitro-phenol 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 70533-96-9 N-tert-butoxycarbonyl-(L)-leucinamide 
• 17663-34-2 L-leucine p-nitrophenyl ester 
• 1177408-26-2 C₂₈H₃₇N₃O₆ 
• 125718-90-3 (S)-2-((S)-2-tert-Butoxycarbonylamino-4-methyl-pentanoylamino)-4-methylsulfanyl-butyric acid; compound with dicyclohexyl-amine 
• 33900-17-3 Boc-Leu-NHCh 
• 2280-68-4 N-tert-butoxycarbonyl-L-leucyl-L-methioninamide 
• 687-51-4 H-L-Leu-NH₂ 
• 75691-76-8 HCl, H-Leu-ONp 
• 1019330-86-9 C₂₉H₄₁N₂O₇P 

Relevant articles and documents

SULFOXONIUM YLIDE DERIVATIVES AS PROBES FOR CYSTEINE PROTEASE

The present invention relates to compounds of formula I bearing a sulfoxonium ylide moiety as warhead, or salts thereof. Such compounds can be used as activity-based probes for cysteine proteases such as cathepsin X, in methods of detecting cysteine protease activity and in related diagnostic or therapeutic methods.

The urea-dipeptides show stronger H-bonding propensity to nucleate β-sheetlike assembly than natural sequence

In this article, we report the distinct solution behavior of a set of urea-dipeptides to that of natural sequence. The urea-dipeptides adopt β-folding conformations and form into β-sheetlike assembly in chloroform. Most surprisedly, the urea-dipeptides tend to form interpeptide H-bonding interactions even at a concentration of as low as 0.1 mM, while the natural sequence shows H-bonding propensity at a concentration of about 7 mM, indicating that the urea-dipeptides show much stronger H-bonding propensity to nucleate formation of β-sheetlike assembly than the natural sequence. CD spectra reveal that the investigated urea-dipeptides have two negative CD bands, respectively, around 217 nm and 224 nm, supporting the β-folding conformations and in turn formation of β-sheetlike assembly. The β-sheetlike assembly is also confirmed by the XRD reflections, which give two typical d-spacings of 12.7 and 4.8 A?, respectively, corresponding to stacking periodicity of the β-sheets and the spacing between peptide backbones running orthogonal to the β-sheet axis.

A simple synthesis of imide-dipeptides

We report a simple approach to synthesize a new class of imide-dipeptides. This approach is mild, and the starting materials are the easily accessible amino acid derivatives. The imide-dipeptides were synthesized from the coupling of an amide and a 4-nitrophenyl activating ester of an amino acid. The acidic proton of the first amide was removed by 1 equivalent of n-butyl lithium to afford the corresponding amide anion which then reacted with the activating ester to give the desired imide derivatives. Georg Thieme Verlag Stuttgart.

Oxo-ester mediated native chemical ligation: Concept and applications

A direct oxo-ester peptide ligation method has been developed. Through the use of an activated C-terminal para nitrophenyl ester (1), it is possible to achieve direct cysteine ligations (1 + 2 → 4). Peptide substrates incorporating bulky C-terminal amino acids (1) can be accommodated with high reaction efficiency. Copyright

ACTIVATION OF A CARBOXY GROUP BY DIALKYL PYROCARBONATES. SYNTHESIS OF SYMMETRICAL ANHYDRIDES AND ARYL ESTERS OF N-PROTECTED AMINO ACIDS USING DI-tert-BUTYL PYROCARBONATE AS CONDENSING REAGENT

It has been shown that di-tert-butyl pyrocarbonate can be used as a condensing reagent in the production of anhydrides and some aryl esters of carboxylic acids.The synthesis of anhydrides and of phenyl, p-nitrophenyl, β-naphtyl, and quinolin-8-yl esters of N-protected amino acids is described.