22610-33-9

Upstream product

• 125814-23-5 Z-L-Ala-NCA 
• 126408-55-7 1-allyl 2-methyl (S)-pyrrolidine-1,2-dicarboxylate 
• 2133-40-6 L-proline methyl ester monohydrochloride 
• 25172-67-2 Z-Ala-O-COO-isoBu 
• 501-53-1 benzyl chloroformate 
• 139373-72-1 (S)-1-{2-[(Z)-Hydroxyimino]-propionyl}-pyrrolidine-2-carboxylic acid methyl ester 
• 26607-52-3 Cbz-Ala-OH*DCHA 
• 6233-97-2 Z-Ala-OPcp 
• 2577-48-2 methyl (2S)-pyrrolidine carboxylate 
• 1168-87-2 benzyloxycarbonylalanine p-nitrophenyl ester 
• 186581-53-3 diazomethane 
• 21027-01-0 N-benzyloxycarbonyl-L-alanyl-L-proline 
• 1142-20-7 N-Cbz-Ala 
• 147-85-3 L-proline 

Downstream Products

• 73535-26-9 Z-Ala-Pro-Pro-Pro-NHNHBoc 
• 75893-20-8 Z-Ala-Pro-Pro-Pro-OH 
• 36357-32-1 (3S,8aS)-3-methylhexahydropyrrolo[1,2-a]pyrazine-1,4-dione 
• 27446-57-7 benzyl N-(1S)-2-[(2S)-2-(aminocarbonyl)tetrahydro-1H-pyrrol-1-yl]-1-methyl-2-oxoethylcarbamate 
• 36238-64-9 (3R,8aS)-3-Methyl-1,2,3,4,6,7,8,8a-octahydropyrrolo<1,2-a>pyrazine-1,4-dione 
• 75893-19-5 Z-Ala-Pro-NHNH₂ 

Relevant academic research and scientific papers

Tandem deprotection-coupling of N(α)-Alloc-amino acids by use of ternary systems Pd cat./PhSiH3/carboxy-activated amino acid

N(α)-allyloxycarbonyl derivatives of amino acids undergo smooth coupling with various carboxy-activated partners when treated with phenylsilane (PhSiH3) in the presence of catalytic amounts of tetrakis- (triphenylphosphine) palladium.

Ynamides as Racemization-Free Coupling Reagents for Amide and Peptide Synthesis

A highly efficient, two-step, one-pot synthetic strategy for amides and peptides was developed by employing ynamides as novel coupling reagents under extremely mild reaction conditions. The ynamides not only are effective for simple amide and dipeptide synthesis but can also be used for peptide segment condensation. Importantly, no racemization was detected during the activation of chiral carboxylic acids. Excellent amidation selectivity toward amino groups in the presence of -OH, -SH, -CONH2, ArNH2, and the NH of indole was observed, making the protection of these functional groups unnecessary in amide and peptide synthesis.

Further evidence for 2-alkyl-2-carboxyazetidines as γ-turn inducers

(Chemical Equation Presented) Reverse turns, a common motif in proteins and peptides, have attracted attention due to their relevance in a wide variety of biological processes. In an attempt to artificially imitate and stabilize these turns in short pepti

A flow reactor process for the synthesis of peptides utilizing immobilized reagents, scavengers and catch and release protocols

A general flow process for the multi-step assembly of peptides has been developed and this procedure has been used to successfully construct a series of Boc, Cbz and Fmoc N-protected dipeptides in excellent yields and purities, including an extension of t

Structures, sensory activity, and dose/response functions of 2,5-diketopiperazines in roasted cocoa nibs (Theobroma cacao)

The taste compounds inducing the blood-like, metallic bitter taste sensation reported recently for a dichloromethane extract prepared from roasted cocoa nibs were identified as a series of 25 diketopiperazines by means of HPLC degustation, LC-MS/MS, and i

Synthesis of fused 1,2,5-triazepine-1,5-diones and some N2- and N3-substituted derivatives: Potential conformational mimetics for cis-peptidyl prolinamides

The synthesis of a new fused 1,2,5-triazepine-1,5-dione heterocycle, which is expected to mimic structural features of cis-peptldyl prolinamides, is described. The required parent heterocycle, corresponding to cis-glycy-(2S)-prolinamide, has been prepared in good yield by the cyclisation of N-(2-bromoacetylprolyl)-hydrazine which is itself generated in situ from the bromoacetyl proline methyl ester. Analogues corresponding to cis-(2R)-alanyl- and cis-(2S)-alanyl-(2S)-prolinamide have been similarly prepared from the appropriate N-(2-bromopropionyl)proline methyl esters and hydrazine hydrate where the cyclisation step, involving the displacement of bromide, has been shown to occur with inversion of configuration at C-2 of the propionyl moiety. Acylation at the N-3 position of the triazepine is equivalent to N-terminal acylation of the residue preceding the proline residue in cis-aminoacyl prolinamides. This has been achieved without incident using standard peptide coupling procedures. Extension at the 'C-terminal' has been achieved by preparing elaborated hydrazine precursors which are reacted with suitably activated esters of N-α-halogenoacylprolines, prior to cyclisation, to give the required fused triazepine dione. Thus it is possible to prepare constrained cis-peptidyl prolyl peptide mimetics of defined stereochemistry based upon this new triazepine dione in which all of the non-proline residues can be varied.

A Novel Method for Preparation of Optically Active Dipeptide. Chemo- and Stereoselective Reduction of 2-Hydroxyimino Amides with Samarium Diiodide

Various α,β-unsaturated amides derived from α-amino acids are converted to the corresponding 2-hydroxyimino amides of α-amino acids by the reaction with butyl nitrite and silane, which are directly reduced with samarium diiodide to the optically active di

KINETICS OF THE ALKALINE HYDROLYSIS OF SEVERAL N-BENZYLOXYCARBONYLDIPEPTIDE METHYL AND ETHYL ESTERS

The reaction rates of the alkaline hydrolysis of synthesized N-protected dipeptide methyl and ethyl esters were studied systematically.From the kinetic data the energies of activation, the pre-exponential factors and the reference values at 40 deg C were calculated.The rate of hydrolysis shows to be strongly dependent on the C-terminal amino acid in the sequence Gly >> Ala/Met/Phe > Leu >> Val/Pro.Surprisingly the N-terminal amino acid also exerts an effect, but in a different sequence.N-Terminal Phe in particular shows a relative accelerating effect.Remarkable is the significantly faster ester hydrolysis of glycine containing dipeptide ethyl esters in ethanol/water compared to the corresponding methyl esters in methanol/water.

RATES OF PEPTIDE FORMATION INVOLVING IMINO ACID RESIDUES

The determination of the rates for peptide coupling in tetrahydrofuran between Z-Aaa-OPcp (Aaa = Ala, (NMe)Ala, Pro, Thz, Pip and (S)Pip) and H-Bbb-OMe (Bbb = (NMe)Ala, Pro, Thz, Pip and (S)Pip) allowed us to evaluate the relative reactivities between these members, either as active components or as amino components.The reactivity of Pro (either as the active species or the amino component) equals that of (NMe)Ala.The reactivity of Pip and (S)Pip as imino components is low while the activation energy is raised by an amount that roughly equals the energy increment needed for bringing the carboxylate grouping from the equatorial to the axial position The reactivities of these six-membered residues are also appreciably low when being the active components during peptide coupling.The presence of a ring-sulfur atom at γ-position of nitrogen additionally decreases the rate for peptidation, especially if (S)Pip is the imino component.