41961-03-9

Basic information

• Product Name: Cbz-Gly-L-Thr-OMe
• Synonyms: Cbz-Gly-L-Thr-OMe
• CAS NO: 41961-03-9
• Molecular Weight: 324.334
• Mol File: 41961-03-9.mol

Chemical Properties

• CAS DataBase Reference: Cbz-Gly-L-Thr-OMe(CAS DataBase Reference)
• NIST Chemistry Reference: Cbz-Gly-L-Thr-OMe(41961-03-9)
• EPA Substance Registry System: Cbz-Gly-L-Thr-OMe(41961-03-9)

Safety Data

• Hazardous Substances Data: 41961-03-9(Hazardous Substances Data)

Upstream product

• 3373-59-9 L-threonine methyl ester 
• 1138-80-3 N-(Benzyloxycarbonyl)glycine 
• 39994-75-7 L-threonine methyl ester hydrochloride 

Downstream Products

• 871915-43-4 Cbz-Gly-Thr(Ψ^Me,MePro)-OMe 
• 871915-47-8 Cbz-Phe-Phe-Gly-Thr(Ψ^Me,MePro)-Phe-Phe-Gly-OH 
• 871915-40-1 Cbz-Phe-Phe-Gly-Thr(Ψ^Me,MePro)-Phe-Phe-Gly-OMe 
• 871915-37-6 H2N-Phe-Phe-Gly-Thr(Ψ^Me,MePro)-Phe-Phe-Gly-OH 
• 871915-42-3 H₂N-Phe-Phe-Gly-Thr-Phe-Phe-Gly-OH 
• 871915-41-2 cyclo-[Phe-Phe-Gly-Thr(Ψ^Me,MePro)-Phe-Phe-Gly] 
• 871915-45-6 Cbz-Phe-Gly-Thr(Ψ^Me,MePro)-Phe-Phe-Gly-OMe 
• 871915-46-7 H2N-Phe-Gly-Thr(Ψ^Me,MePro)-Phe-Phe-Gly-OMe 
• 871915-39-8 Cbz-Gly-Thr(Ψ^Me,MePro)-Phe-Phe-Gly-OMe 
• 871915-44-5 H2N-Gly-Thr(Ψ^Me,MePro)-Phe-Phe-Gly-OMe 
• 871915-38-7 Cbz-Gly-Thr(Ψ^Me,MePro)-OH 
• 949-90-6 N-(carbobenzyloxy)glycinamide 

Relevant articles and documents

Total Synthesis of the Proposed Microcyclamides MZ602 and MZ568

The first convergent total synthesis for the proposed structures of microcyclamides MZ602 (1) and MZ568 (2) has been accomplished in 11 linear steps with 12.5 and 16.8% overall yield, respectively. Key features of the syntheses include a one-pot cascade r

N,O-isopropylidenated threonines as tools for peptide cyclization: Application to the synthesis of mahafacyclin B

(Chemical Equation Presented) The influence of a single N,O-isopropylidenated threonine turn-inducer on the cyclization of a linear heptapeptide precursor to mahafacyclin B has been investigated. Incorporation of an N,O-isopropylidenated threonine more th

Bromelain catalyzed synthesis of peptides in organic solvent

For the first time, immobilized bromelain was shown to maintain high catalytic activity in organic solvent and to form peptide bonds. It requires only 7 hours to obtain Cbz-Gly-L-Leu-OMe in 85% yield. The precursor of aspartame (Cbz-L-Asp-L-Phe-OMe) and other dipeptides were also synthesized by this method.

Protein backbone modification by novel C(α)-C side-chain scission

α-Ketoamide (-NH-CO-CO-) units in intact peptides are generated from Ser/Thr residues via Ru(VIII)-catalyzed C(α)-C side-chain scission. Facets associated with this novel α-carbon modification have been probed with 75 peptides chosen to represent every possible peptide environment. The reactions were carried out at room temperature with in situ generated Ru(VIII) in biphasic (CH3CN/CCl4/pH 3 phosphate buffer, 1:1:2 v/v) medium. Whereas Ser/Thr residues placed at the C-terminal end in peptides undergo N-C bond scission leading to des-Ser/Thr peptide amides - thus acting as Gly equivalents in simulating the α-amidating action of pituitary enzymes - those located at the N-terminal or nonterminal or even at the C-terminal position (protected as amide) were found to undergo oxidative C-C bond scission (involving C(α) and C side-chain bond), resulting in the generation of α-ketoamide (-NH-CO-CO-) units in the intact peptide backbone. The difference in the products arising from C(α)-C side-chain scission of Ser/Thr esters and amides is rationalized on the basis of a common mechanism involving either oxaloesters [PeP-NH-CO-COX; X = OMe] or oxalamides [X = NH2 or NH-Pep] arising from the oxidation of initially formed carbinolamide intermediates [Pep-NH-CH(OH)-COX], wherein, while the former are shown to undergo hydrolysis to terminal amides [Pep-NH2], the oxalamides are found to be stable to hydrolysis. Ancillary noteworthy findings are those of peptide bond scission when contiguous Ser-Ser/Thr-Thr residues are present and the oxidative cleavage at C-terminal Tyr/Trp sites generating des amides. The oxidative methodology presented here is mild, simple, and practical and proceeds with chiral retention. The insensitivity of a large number of amino acid residues, such as Gly, Ala, Leu, Asn, Gln, Asp, Glu, Pro, Arg, Phe, Lys, Val, and Aib, and N-protecting groups, such as Boc, Z, and Bz, toward Ru(VIII) under the experimental conditions should make this methodology practical and useful. Sulfur-containing amino acids Cys and Met get oxidized to sulfones in the products.