32303-82-5 Usage
Description
Z-ALA-HIS-OME, also known as N-(benzyloxycarbonyl)-L-alanine histidine methyl ester, is a synthetic peptide compound that consists of three amino acids: alanine, histidine, and methionine. It is characterized by the presence of a benzyloxycarbonyl (Z) protecting group on the alanine residue and a methyl ester (OME) group on the methionine residue. Z-ALA-HIS-OME is a valuable research intermediate in the field of peptide chemistry.
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.
Check Digit Verification of cas no
The CAS Registry Mumber 32303-82-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 3,2,3,0 and 3 respectively; the second part has 2 digits, 8 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 32303-82:
(7*3)+(6*2)+(5*3)+(4*0)+(3*3)+(2*8)+(1*2)=75
75 % 10 = 5
So 32303-82-5 is a valid CAS Registry Number.
32303-82-5Relevant articles and documents
Design, synthesis, and application of enantioselective coupling reagent with a traceless chiral auxiliary
Kolesinska, Beata,Kaminski, Zbigniew J.
supporting information; experimental part, p. 765 - 768 (2009/09/06)
(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
Mechanism of Enantioselective Ester Cleavage by Histidine-Containing Dipeptides at a Micellar Interface
Cleij, Marco C.,Drenth, Wiendelt,Nolte, Roeland J. M.
, p. 3883 - 3891 (2007/10/02)
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.
