3338-39-4

Basic information

• Product Name: (R)-2-((R)-2-Benzyloxycarbonylamino-3-phenyl-propionylamino)-propionic acid
• CAS NO: 3338-39-4
• Molecular Weight: 370.405
• Mol File: 3338-39-4.mol
• Article Data: 19

Chemical Properties

• CAS DataBase Reference: (R)-2-((R)-2-Benzyloxycarbonylamino-3-phenyl-propionylamino)-propionic acid(CAS DataBase Reference)
• NIST Chemistry Reference: (R)-2-((R)-2-Benzyloxycarbonylamino-3-phenyl-propionylamino)-propionic acid(3338-39-4)
• EPA Substance Registry System: (R)-2-((R)-2-Benzyloxycarbonylamino-3-phenyl-propionylamino)-propionic acid(3338-39-4)

Safety Data

• Hazardous Substances Data: 3338-39-4(Hazardous Substances Data)

Upstream product

• 28944-94-7 (S)-methyl 2-((S)-2-(((benzyloxy)carbonyl)amino)-3-phenylpropanamido)propanoate 
• 35909-92-3 N-carbobenzoxy-L-phenylalanine methyl ester 
• 16480-55-0 sodium L-alaninate 
• 56-41-7 L-alanin 
• 2688-13-3 Z-L-Phe-O-N=C(CH₃)-C₆H₄-m-NO₂ 
• 1161-13-3 N-Cbz-L-Phe 
• 3397-32-8 N-(benzyloxycarbonyl)-phenylalanine-N-hydroxysuccinimide ester 
• 72015-61-3 (Z)-2-benzyloxycarbonylaminocinnamic acid 
• 117999-32-3 Z-ΔPhe-(S)-Ala-OH 
• 117999-35-6 Z-ΔPhe-(R)-Ala-OH 
• 67-56-1 methanol 
• 65118-54-9 N-(benzyloxycarbonyl)phenylalanyl-alanine amide 
• 41518-17-6 Z-Phe-O-COO-isoBu 
• 2578-84-9 N-benzyloxycarbonyl-L-phenylalanine p-nitrophenyl ester 

Downstream Products

• 98695-15-9 Z-Ala-Phe-Ser(OBzl)(OMe) 
• 74075-19-7 Cbz-Phe-Ala-Pro-Obzl 
• 115186-22-6 Z-L-phenylalanyl-L-alanyl bromomethyl ketone 
• 1161-13-3 N-Cbz-L-Phe 
• 28709-70-8 N-benzyloxycarbonyl-L-phenylalanine ethyl ester 
• 60644-13-5 Z-Phe-Ala-OEt 
• 872369-31-8 (3S,4S)-3-{(R)-2-[(S)-2-((S)-2-Benzyloxycarbonylamino-3-phenyl-propionylamino)-propionylamino]-4-methyl-pentanoyloxy}-4-methyl-octanoic acid 4-nitro-benzyl ester 
• 213771-64-3 C₂₀H₂₃N₃O₄ 
• 65118-54-9 N-(benzyloxycarbonyl)phenylalanyl-alanine amide 

Relevant articles and documents

Optimization and anti-cancer properties of fluoromethylketones as covalent inhibitors for ubiquitin C-terminal hydrolase L1

The deubiquitinating enzyme (DUB) UCHL1 is implicated in various disease states including neurodegenerative disease and cancer. However, there is a lack of quality probe molecules to gain a better understanding on UCHL1 biology. To this end a study was carried out to fully characterize and optimize the irreversible covalent UCHL1 inhibitor VAEFMK. Structure-activity relationship studies identified modifications to improve activity versus the target and a full cellular characterization was carried out for the first time with this scaffold. The studies produced a new inhibitor, 34, with an IC50 value of 7.7 μM against UCHL1 and no observable activity versus the closest related DUB UCHL3. The molecule was also capable of selectively inhibiting UCHL1 in cells and did not demonstrate any discernible off-target toxicity. Finally, the molecule was used for initial probe studies to assess the role of UCHL1 role in proliferation of myeloma cells and migration behavior in small cell lung cancer cells making 34 a new tool to be used in the biological evaluation of UCHL1.

α-N-Protected dipeptide acids: A simple and efficient synthesis via the easily accessible mixed anhydride method using free amino acids in DMSO and tetrabutylammonium hydroxide

The importance of dipeptides both in medicinal and pharmacological fields is well documented and many efforts have been made to find simple and efficient methods for their synthesis. For this reason, we have investigated the synthesis of α-N-protected dipeptide acids by reacting the easily accessible mixed anhydride of α-N-protected amino acids with free amino acids under different reaction conditions. The combination of TBA-OH and DMSO has been found to be the best to overcome the low solubility of amino acids in organic solvents. Under these experimental conditions, the homogeneous phase condensation reaction occurs rapidly and without detectable epimerization. The present method is also applicable to side-chain unprotected Tyr, Trp, Glu, and Asp but not Lys. This latter residue is able to engage two molecules of mixed anhydride giving the corresponding isotripeptide. Moreover, the applicability of this protocol for the synthesis of tri- and tetrapeptides has been tested. This approach reduces the need for protecting groups, is cost effective, scalable, and yields dipeptide acids that can be used as building blocks in the synthesis of larger peptides.

Modulation of the inhibitor properties of dipeptidyl (acyloxy)methyl ketones toward the CaaX proteases

Dipeptidyl (acyloxy)methyl ketones (AOMKs) have been identified as mechanism-based inhibitors of certain cysteine proteases. These compounds are also inhibitors of the integral membrane proteins Rce1p and Ste24p, which are proteases that independently mediate a cleavage step associated with the maturation of certain isoprenylated proteins. The enzymatic mechanism of Rce1p is ill-defined, whereas Ste24p is a zinc metalloprotease. Rce1p is required for the proper processing of the oncoprotein Ras and is viewed as a potential target for cancer therapy. In this study, we synthesized a small library of dipeptidyl AOMKs to investigate the structural elements that contribute to the inhibitor properties of this class of molecules toward Rce1p and Ste24p. The compounds were evaluated using a fluorescence-based in vitro proteolysis assay. The most potent dipeptidyl AOMKs contained an arginine residue and the identity of the benzoate group strongly influenced potency. A 'warhead' free AOMK inhibited Rce1p and Ste24p. The data suggest that the dipeptidyl AOMKs are not mechanism-based inhibitors of Rce1p and Ste24p and corroborate the hypothesis that Rce1p is not a cysteine protease.