21027-01-0

Basic information

• Product Name: Z-ALA-PRO-OH
• Synonyms: CBZ-L-ALA-PRO;Z-ALA-PRO-OH;Z-L-ALANYL-L-PROLINE;N-cbz-ala-pro;NSC 333444;N-Benzyloxycarbonyl-L-alanyl-L-proline;Cbz-Ala-Pro-OH
• CAS NO: 21027-01-0
• Molecular Formula: C₁₆H₂₀N₂O₅
• Molecular Weight: 320.34
• Mol File: 21027-01-0.mol

Chemical Properties

• Boiling Point: 576.4°Cat760mmHg
• Flash Point: 302.4°C
• Appearance: /
• Density: 1.301g/cm³
• Vapor Pressure: 3.99E-14mmHg at 25°C
• Refractive Index: 1.572
• Storage Temp.: -15°C
• CAS DataBase Reference: Z-ALA-PRO-OH(CAS DataBase Reference)
• NIST Chemistry Reference: Z-ALA-PRO-OH(21027-01-0)
• EPA Substance Registry System: Z-ALA-PRO-OH(21027-01-0)

Safety Data

• Hazardous Substances Data: 21027-01-0(Hazardous Substances Data)

Usage

Uses

Used in Organic Synthesis:
Z-ALA-PRO-OH is used as a building block for the synthesis of longer peptides and proteins. The Z-protecting group allows for more precise control over the assembly of the desired peptide sequence by preventing unwanted side reactions.
Used in Peptide Chemistry:
In peptide chemistry, Z-ALA-PRO-OH is utilized as a key component in the creation of complex peptide structures. The Z-protecting group ensures that the amino group remains unreactive until the desired point in the synthesis process, facilitating the formation of specific peptide bonds.
Used in Pharmaceutical Development:
Z-ALA-PRO-OH may be employed as a starting material or intermediate in the development of new pharmaceuticals and bioactive compounds, given its role in peptide synthesis and the potential for creating novel therapeutic agents.
Used in Bioactive Compound Development:
Z-ALA-PRO-OH's potential applications extend to the development of bioactive compounds, where its structural properties and the Z-protecting group can be leveraged to create molecules with specific biological activities.

InChI:InChI=1/C16H20N2O5/c1-11(14(19)18-9-5-8-13(18)15(20)21)17-16(22)23-10-12-6-3-2-4-7-12/h2-4,6-7,11,13H,5,8-10H2,1H3,(H,17,22)(H,20,21)

Upstream product

• 27544-35-0 Cbz-L-Ala-L-Pro-O^tBu 
• 1168-87-2 benzyloxycarbonylalanine p-nitrophenyl ester 
• 147-85-3 L-proline 
• 3401-36-3 (N-benzyloxycarbonyl)-L-alanine N-hydroxysuccinimide ester 
• 1142-20-7 N-Cbz-Ala 
• 226543-68-6 Z-Ala-Pro-NHNHPh 
• 820239-42-7 benzyl N-[(1S)-2-(1H-1,2,3-benzotriazol-1-yl)-1-methyl-2-oxoethyl]carbamate 
• 15761-39-4 1-(tert-butoxycarbonyl)-L-proline 
• 28861-55-4 Z-Ala-NHNHPh 
• 71989-31-6 Fmoc-Pro-OH 
• 153240-03-0 H-Pro-NHNHPh 
• 474316-85-3 (S)-tert-butyl 2-(2-phenylhydrazinecarbonyl)pyrrolidine-1-carboxylate 
• 474316-88-6 Fmoc-Pro-NHNHPh 
• 33305-75-8 L-proline ethyl ester monohydrochloride 

Downstream Products

• 22610-33-9 (2S,2'S)-N-(N-Benzyloxycarbonylalanyl)proline methyl ester 
• 120791-83-5 N-(Benzyloxycarbonyl)-L-alanyl-L-prolyl-O-(2-acetamido-3,4,6-tri-O-acetyl-2-desoxy-α-D-galactopyranosyl)-L-threonin-tert-butylester 
• 27446-57-7 benzyl N-(1S)-2-[(2S)-2-(aminocarbonyl)tetrahydro-1H-pyrrol-1-yl]-1-methyl-2-oxoethylcarbamate 
• 66383-09-3 Benzyloxycarbonylalanyl-proline Ethylamide 
• 75893-19-5 Z-Ala-Pro-NHNH₂ 
• 75893-20-8 Z-Ala-Pro-Pro-Pro-OH 
• 73535-26-9 Z-Ala-Pro-Pro-Pro-NHNHBoc 
• 108074-21-1 Z-Ala-Pro-Phe 
• 5565-29-7 L-alanyl-L-proline t-butylester 
• 29375-30-2 (S)-alanyl-(S)-proline tert-butyl ester 
• 66382-56-7 N-benzyloxycarbonyl-L-alanyl-L-proline 4-nitroanilide 
• 66412-10-0 N-benzyloxycarbonyl-L-alanyl-L-proline anilide 
• 1140836-14-1 (2S,3R)-tert-butyl 3-(benzyloxy)-2-((S)-1-((S)-2-(benzyloxycarbonylamino)propanoyl)-N-methylpyrrolidine-2-carboxamido)butanoate 
• 1173817-68-9 benzyl N-(1S)-2-[(2S)-2-(1H-1,2,3-benzotriazol-1-ylcarbonyl)tetrahydro-1H-pyrrol-1-yl]-1-methyl-2-oxoethylcarbamate 

Relevant articles and documents

3-Azaspiro[5,5]undecan-2,4-dioxo-3-yl diphenyl phosphate (ASUD-diphenyl phosphate), a new reagent for the synthesis of the N-protected amino acid-ASUD ester

A new reagent, 3-azaspiro[5,5]undecan-2,4-dioxo-3-yl diphenyl phosphate (ASUD-diphenyl phosphate) is described for the synthesis of N-protected amino acid-ASUD esters which are active esters useful in the synthesis of peptides. This compound was synthesized by reacting N-hydroxy-3-azaspiro[5,5]undecane-2,4-dione (HO-ASUD) with diphenyl chlorophosphate in the presence of a base at room temperature and was obtained in high yields. The ASUD-diphenyl phosphate reagent reacts with N-protected amino acids under mild conditions to give the corresponding ASUD active esters, while preserving the enantiomeric purity of the amino acid. The new reagent is a stable crystalline compound and eliminates the need for DCC, a potent skin allergen, used previously for the synthesis of N-protected amino acid-ASUD ester.

A new benzotriazole-mediated stereoflexible gateway to hetero-2,5- diketopiperazines

Open chain Cbz-L-aa1-L-Pro-Bt (Bt=benzotriazole) sequences were converted into either the corresponding trans- or cis-fused 2,5- diketopiperazines (DKPs) depending on the reaction conditions. Thermodynamic tandem cyclization/epimerization afforded selectively the corresponding trans-DKPs (69-75%). Complementarily, tandem deprotection/cyclization led to the cis-DKPs (65-72%). A representative set of proline-containing cis- and trans-DKPs has been prepared. A mechanistic investigation, based on chiral HPLC, kinetics, and computational studies enabled a rationalization of the results. Stereoflexible route to DKPs: A convenient, versatile, and flexible benzotriazole-mediated methodology for the synthesis of proline-containing hetero-2,5-diketopiperazines (DKPs) is reported. Depending on the reaction conditions, either cis- or trans-configured DKPs were obtained starting from the same inexpensive l,l-dipeptidoyl benzotriazole key intermediate (see scheme). Kinetics, chiral HPLC, and computational studies forged a background for mechanistic rationalization. Copyright

Convenient synthesis of C-terminal di- and tri-peptide amides from N-protected dipeptidoylbenzotriazoles

N-Protected dipeptidoylbenzotriazoles react with aqueous ammonia to give dipeptide primary amides (77-98%) and with N-unprotected α-amino amides to afford tripeptide primary amides (82-86%).

Solution-phase peptide synthesis; Synthesis of 'North-Western' and 'South Eastern' fragments of the antifungal cyclodepsipeptide petriellin A

The solution-phase synthesis of two highly modified peptides, a hexamer and a heptamer, that constitute the two halves of the antifungal cyclic depsipeptide, Petriellin A, is reported. CSIRO 2008.

Efficient peptide coupling involving sterically hindered amino acids

(Chemical Equation Presented) Hindered amino acids have been introduced into peptide chains by coupling N-(Cbz- and Fmoc-α-aminoacyl) benzotriazoles with amino acids, wherein at least one of the components was sterically hindered, to provide compounds 3a-e, (3c +3 c′), 5a-d, (5a + 5a′), 6a-c, (6b + 6b′), 8a-c, 9a-e, 10a-d, and (10a + 10a′) in isolated yields of 41-95% with complete retention of chirality as evidenced by NMR and HPLC analysis. The benzotriazole activation methodology is a new route for the synthesis of sterically hindered peptides. (Note: compound numbers written within brackets represent diastereomeric mixtures or racemates; compound numbers without brackets represent enantiomers.)

Phenylhydrazide as an enzyme-labile protecting group in peptide synthesis

The enzymatic cleavage of amino acid phenylhydrazides with the enzyme tyrosinase (EC 1.14.18.1) offers a new, mild, and selective method for C-terminal deprotection of peptides. The advantages of the described methodology are the very mild oxidative removal of the protecting group at room temperature and pH 7, a high chemo- and regioselectivity, and the availability of the biocatalyst. Even in oxygen-saturated solution, the oxidation of sensitive methionine residues was not observed. These features make the methodology suitable for the synthesis of sensitive peptide conjugates. Mechanistic data suggest that the hydrolysis of the oxidized adducts proceeds by a free-radical mechanism.

The phenyl hydrazide as an enzyme-labile protecting group - Oxidative cleavage with mushroom tyrosinase

Amino acid and peptide phenyl hydrazides are selectively cleaved by oxidation to acyl diazenes with mushroom tyrosinase and their subsequent hydrolysis.

A Chemical Model for the Activation of Pyruvate-Formate-Lyase

A chemical model is described for the activation of the carbon-centred radical-based enzyme, pyruvate-formate-lyase.The feasibility of a 5'-deoxyadensyl radical abstracting a hydrigen atom from C-2 of a peptideglycine residue has been demonstrated in an intramolecular process.