2212-75-1

Basic information

• Product Name: N-alpha-Cbz-L-lysine
• Synonyms: N-CBZ-L-LYSINE;N-CBZ-L-LYSINE-OH;N2-(CARBOBENZYLOXY)-L-LYSINE;N-ALPHA-BENZYLOXYCARBONYL-L-LYSINE;N-BENZYLOXYCARBONYL-L-LYSINE;N-ALPHA-CBZ-L-LYS;N(ALPHA)-CBZ-L-LYSINE;N-ALPHA-CARBOBENZOXY-L-LYSINE
• CAS NO: 2212-75-1
• Molecular Formula: C₁₄H₂₀N₂O₄
• Molecular Weight: 280.32
• EINECS: 218-662-6
• Product Categories: Lysine [Lys, K];Z-Amino Acids and Derivatives;Amino Acids;Amino Acids (N-Protected);Biochemistry;Cbz-Amino Acids;Z-Amino acid series
• Mol File: 2212-75-1.mol

Chemical Properties

• Melting Point: 226-231 °C (dec.)(lit.)
• Boiling Point: 497 °C at 760 mmHg
• Flash Point: 254.4 °C
• Appearance: /
• Density: 1.206 g/cm³
• Refractive Index: 1,512
• Storage Temp.: −20°C
• Solubility: Methanol (Slightly), Water (Slightly)
• PKA: 3.90±0.21(Predicted)
• BRN: 2153826
• CAS DataBase Reference: N-alpha-Cbz-L-lysine(CAS DataBase Reference)
• NIST Chemistry Reference: N-alpha-Cbz-L-lysine(2212-75-1)
• EPA Substance Registry System: N-alpha-Cbz-L-lysine(2212-75-1)

Safety Data

• Hazard Codes: Xn
• Statements: 20/21/22-36/37/38
• Safety Statements: 22-24/25-36-26
• WGK Germany: 3
• TSCA: Yes
• Hazardous Substances Data: 2212-75-1(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
N-alpha-Cbz-L-lysine is used as an intermediate in the synthesis of hydroxamic acids and mycobacterium inhibitors. These compounds have significant applications in the development of new drugs for the treatment of various diseases, including tuberculosis and other bacterial infections.
Used in Chemical Synthesis:
N-alpha-Cbz-L-lysine is used as an educt for the convenient preparation of L-α-aminoadipic acid, which is an important building block for the synthesis of various bioactive compounds and pharmaceuticals.
Used in Research and Development:
Due to its unique chemical properties, N-alpha-Cbz-L-lysine is also used in research and development for the study of protein structure, function, and interactions. It can be employed as a starting material for the synthesis of novel peptides, peptidomimetics, and other bioactive molecules with potential applications in medicine and biotechnology.

InChI:InChI=1/C14H20N2O4/c15-9-5-4-8-12(13(17)18)16-14(19)20-10-11-6-2-1-3-7-11/h1-3,6-7,12H,4-5,8-10,15H2,(H,16,19)(H,17,18)/t12-/m0/s1

Upstream product

• 14511-39-8 2(S)-2-amino-6-(benzylideneamino)hexanoic acid 
• 501-53-1 benzyl chloroformate 
• 69861-90-1 Nα-benzyloxycarbonyl-L-lysine thiobenzyl ester 
• 657-27-2 L-Lysine hydrochloride 
• 56-87-1 L-lysine 
• 1413890-77-3 N_ε-(allyloxycarbonyl-L-isoleucyl)-N_α-benzyloxycarbonyl-L-lysine 
• 2418-95-3 (S)-2-amino-6-(tert-butoxycarbonylamino)hexanoic acid 
• 47594-83-2 α-Benzyloxycarbonyl-ε-troc-L-lysine 
• 2389-60-8 Z-Lys(Boc)-OH 
• 4272-71-3 N^α-benzyloxycarbonyl-L-lysine p-nitrophenyl ester 

Downstream Products

• 2389-60-8 Z-Lys(Boc)-OH 
• 78221-47-3 (S)-2-Benzyloxycarbonylamino-6-(2,2,2-trichloro-ethoxycarbonylamino)-hexanoic acid; compound with tert-butylamine 
• 119147-50-1 N^α-Benzyloxycarbonyl-N^ε-<4,6-bis(octadecyloxy)-1,3,5-triazin-2-yl>-L-lysin 
• 1871-67-6 (E)-oct-2-enoic acid 
• 75-07-0 acetaldehyde 
• 112157-39-8 Nα-(Benzyloxycarbonyl)-L-lysine tert-butyl ester 
• 170797-46-3 Boc-Tyr(Bzl)-D-Met-Gly-Phe-Pro-Z-Lys 
• 6033-32-5 (S)-2-amino-6-hydroxyhexanoic acid 
• 246516-49-4 Z-Lys[3-carbamidopropyl O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-(1->4)-O-2-acetamido-3,6-di-O-acetyl-2-deoxy-β-D-glucopyranoside]-OH 
• 105751-18-6 N_α-carbobenzyloxy-N_ε-9-fluorenylmethoxycarbonyl-L-lysine 

Relevant articles and documents

SIDE REACTIONS AND CADMIUM CATALYSED REMOVAL OF THE TRICHLOROETHOXYCARBONYL (TROC) PROTECTING GROUP.

The Troc protecting group has been found to be unstable to the hydrogenolytic conditions used for removal of the benzyloxycarbonyl group; an improved method of removal employing cadmium dust in 50percent AcOH/DMF is described.

A kind of amino acid tanshinone phenolic derivative and its preparation method

The invention relates to amino acid tanshinone phenolic ester derivatives and a preparation method thereof. The derivatives are obtained by reducing tanshinone compounds and performing esterified modification on the reduced tanshinone compounds and an amino acid into prodrugs, wherein the tanshinone compounds are phenanthrenequinone compounds which exist in salvia miltiorrhiza and have an o-quinone structure; the esterified amino acid is alpha-amino acid. The amino acid tanshinone phenolic ester derivatives are compounds having a structure of a general formula (I) or medicinal salts thereof, wherein R1 and R2 represent H or acyl alpha-amino acid and a salt thereof, and R1 and R2 are not H at the same time. The amino acid tanshinone phenolic ester derivatives have the beneficial effects that firstly, the new tanshinone derivatives are provided and the new substances have potential treatment effect on some serious diseases such as tumors, and secondly, amino acid tanshinone phenolic ester derivatives have excellent water solubility and thus can be prepared into injections conveniently in addition to various oral preparations, and therefore, the amino acid tanshinone phenolic ester derivatives are capable of quickly taking effect in disease treatment. As important prodrugs, the amino acid tanshinone phenolic ester derivatives have important application value.

CHEMICAL CROSSLINKERS AND COMPOSITIONS THEREOF

Chemical crosslinkers and methods of their synthesis are disclosed.

Orthogonally protected artificial amino acid as tripod ligand for automated peptide synthesis and labeling with [99mTc(OH2) 3(CO)3]+

1,2-Diamino-propionic acid (Dap) is a very strong chelator for the [ 99mTc(CO)3]+ core, yielding small and hydrophilic complexes. We prepared the lysine based Dap derivative l-Lys(Dap) in which the ε-NH2 group was replaced by the tripod through conjugation to its α-carbon. The synthetic strategy produced an orthogonally protected bifunctional chelator (BFC). The -NH2 group of the α-amino acid portion is Fmoc- and the -NH2 of Dap are Boc-protected. Fmoc-l-Lys(Dap(Boc)) was either conjugated to the N- and C-terminus of bombesin BBN(7-14) or integrated into the sequence using solid-phase peptide synthesis (SPPS). We also replaced the native lysine in a cyclic RGD peptide with l-Lys(Dap). For all peptides, quantitative labeling with the [99mTc(CO)3]+ core at a 10 μM concentration in PBS buffer (pH = 7.4) was achieved. For comparison, the rhenium homologues were prepared from [Re(OH2)3(CO) 3]+ and Lys(Dap)-BBN(7-14) or cyclo-(RGDyK(Dap)), respectively. Determination of integrin receptor binding showed low to medium nanomolar affinities for various receptor subtypes. The IC50 of cyclo-(RGDyK(Dap[Re(CO)3])) for αvβ3 is 7.1 nM as compared to 3.1 nM for nonligated RGD derivative. Biodistribution studies in M21 melanoma bearing nude mice showed reasonable α vβ3-integrin specific tumor uptake. Altogether, orthogonally protected l-Lys(Dap) represents a highly versatile building block for integration in any peptide sequence. Lys(Dap)-precursors allow high-yield 99mTc-labeling with [99mTc(OH2) 3(CO)3]+, forming small and hydrophilic complexes, which in turn leads to peptide radiopharmaceuticals with excellent in vivo characteristics.

Tandem catalysis for the preparation of cylindrical polypeptide brushes

Here, we report a method for synthesis of cylindrical copolypeptide brushes via N-carboxyanhydride (NCA) polymerization utilizing a new tandem catalysis approach that allows preparation of brushes with controlled segment lengths in a straightforward, one-pot procedure requiring no intermediate isolation or purification steps. To obtain high-density brush copolypeptides, we used a "grafting from" approach where alloc-α-aminoamide groups were installed onto the side chains of NCAs to serve as masked initiators. These groups were inert during cobalt-initiated NCA polymerization and gave allyloxycarbonyl-α-aminoamide-substituted polypeptide main chains. The alloc-α-aminoamide groups were then activated in situ using nickel to generate initiators for growth of side-chain brush segments. This use of stepwise tandem cobalt and nickel catalysis was found to be an efficient method for preparation of high-chain-density, cylindrical copolypeptide brushes, where both the main chains and side chains can be prepared with controlled segment lengths.

THIAZOLIDINE DERIVATIVE AND MEDICINAL USE THEREOF

A thiazolidine derivative represented by the formula (I) wherein each symbol is as defined in the specification, and a pharmaceutically acceptable salt thereof exhibit a potent DPP-IV inhibitory activity, and can be provided as an agent for the prophylaxis or treatment of diabetes, an agent for the prophylaxis or treatment of obesity and the like.

Stereocontrolled synthesis of onchidins

(Chemical Equation Presented) The first total synthesis of a molecule possessing the stereochemistry proposed for onchidin is described. The structure synthesized appears to be different from that of the marine natural product.

Fairly marked enantioselectivity for the hydrolysis of amino acid esters by chemically modified enzymes

The hydrolysis (deacylation) of enantiomeric substrates by the chemically modified enzymes decanoyl-α-chymotrypsin and decanoyl-trypsin was studied. Reaction activity for decanoyl-α-chymotrypsin was lower than that for the native enzyme, although intriguingly the enantioselectivity was markedly enhanced as compared with the native enzyme. In particular, the apparently complete enantioselective catalysis was attained for the hydrolytic cleavage of p-nitrophenyl N-dodecanoyl- D(L)-phenylalaninates. The enhancement of enantioselectivity, however, was not observed for decanoyl-trypsin. These results suggest that the chemically modified α-chymotrypsin by addition of hydrophobic groups has promoted enantioselectivity for the hydrolysis of hydrophobic esters.

Synthesis of L-indospicine

Preparation of L-indospicine in eight steps by a reaction sequence starting with L-lysine.

Fibrinolytic and antithrombotic protease from Spirodela polyrhiza.

A fibrinolytic protease was purified from a Chinese herb (Spirodela polyrhiza). The protease has a molecular mass of 145 kDa and 70 kDa in gel filtration and SDS-polyacrlamide gel electrophoresis (PAGE), respectively, implying it is a dimer. Its optimum p