32303-82-5

Usage

Uses

Used in Pharmaceutical Industry:
Z-ALA-HIS-OME is used as a research intermediate for the synthesis of other histidine-containing peptides. It plays a crucial role in the development of novel therapeutic agents, particularly those targeting various diseases and conditions. The presence of histidine in the peptide sequence allows for the formation of metal complexes, which can be utilized in the design of metallodrugs or as chelating agents for metal ions.
Used in Peptide Synthesis:
Z-ALA-HIS-OME is used as a building block in the synthesis of larger peptides and proteins. The Z protecting group on the alanine residue helps prevent unwanted side reactions during peptide synthesis, ensuring the formation of the desired peptide sequence. Once the desired peptide is synthesized, the Z group can be removed under mild acidic conditions, allowing for further modification or functionalization of the peptide.
Used in Biochemical Research:
Z-ALA-HIS-OME is used as a substrate or inhibitor in various biochemical assays and enzymatic reactions. The presence of histidine in the peptide sequence allows for the study of enzymes that specifically recognize and process histidine-containing peptides. Additionally, the compound can be used to investigate the role of histidine in protein folding, stability, and function.

Upstream product

• 1168-87-2 benzyloxycarbonylalanine p-nitrophenyl ester 
• 4467-54-3 l-histidine methyl ester dihydrochloride 
• 501-53-1 benzyl chloroformate 
• 1142-20-7 N-benzyloxycarbonyl-L-alanine 
• 7389-87-9 L-histidine methyl ester dihydrochloride 
• 4132-86-9 N-benzyloxycarbonylalanine 
• 1142-20-7 N-Cbz-Ala 

Downstream Products

• 79458-92-7 N-(Benzyloxycarbonyl-L-ananyl)-L-histidine 
• 54300-25-3 cyclo-Ala-His 

Relevant academic research and scientific papers

Design, synthesis, and application of enantioselective coupling reagent with a traceless chiral auxiliary

(Chemical Equation Presented) Stable chiral N-triazinylbrucinium tetrafluoroborate enantioselectively activates racemic carboxylic acids yielding enantiomerically enriched amides, esters, and dipeptides with er from 8:92 to 0.5:99.5. Due to the departure

Thermodynamic and (1)H NMR Study of Proton Complex Formation of Histidine-containing Cyclodipeptides in Aqueous Solution

A thermodynamic and (1)H NMR study of proton complex formation in aqueous solution of some L-histidine-containing cyclic L-dipeptides has been carried out.The enthalpic and entropic changes associated with protonation of the cyclodipeptides, obtained by potentiometric and calorimetric measurements, together with the (1)H NMR data and NOESY experiments, enable the role played by non-covalent interactions in proton complex formation to be assessed.In addition, a comparison with c(Gly-His) permits the influence of side-chain residues on the conformation of protonated species to be observed.

Mechanism of Enantioselective Ester Cleavage by Histidine-Containing Dipeptides at a Micellar Interface

Chiral p-nitrophenyl esters derived from the amino acid phenylalanine are cleaved by histidine-containing dipeptides at a micellar interface.High enantioselectivities (up to kL/kD = 30.4 at 0 deg C) are observed.Both the substrates and the catalysts contain an alternating sequence of hydrophobic and hydrophilic groups.Due to the need for hydration of the hydrophilic groups, the hydrophobic groups cannot dissolve completely into the micellar hydrocarbon phase.The kinetic data suggest that the micellar interface is capable of discriminating between transition states that have different hydrophilic and hydrophobic properties.One of the diastereomeric transition states is characterized by a hydrogen bond between the amide CO group of the ester and an NH group of the histidine-containing dipeptide.Upon formation of this hydrogen bond these polar CO and NH groups lose their hydrophilicity which allows the transfer of the adjacent apolar groups to the micellar hydrocarbon phase.The other diastereomeric transition state cannot form this hydrogen bond and the hydrophobic groups remain hydrated.Consequently, the latter transition state is of higher energy.The kinetic data reveal that it is important to prevent steric hinderance between the reactants in order to allow the unhindered formation of the hydrogen bond.