Z-Ala-His-OMe (BAT-006560)
* For research use only

Z-Ala-His-OMe is a useful research intermediate for the synthesis of other histidine-containing peptides.

Category
Catalog Peptides
Catalog number
BAT-006560
CAS number
32303-82-5
Molecular Formula
C18H22N4O5
Molecular Weight
374.40
Z-Ala-His-OMe
Synonyms
(S)-methyl 2-((S)-2-(benzyloxycarbonylamino)propanamido)-3-(1H-imidazol-4-yl)propanoate; Z Ala His OMe
Appearance
White product
Purity
≥ 99% (TLC)
Storage
Store at 2-8 °C
InChI
InChI=1S/C18H22N4O5/c1-12(21-18(25)27-10-13-6-4-3-5-7-13)16(23)22-15(17(24)26-2)8-14-9-19-11-20-14/h3-7,9,11-12,15H,8,10H2,1-2H3,(H,19,20)(H,21,25)(H,22,23)/t12-,15-/m0/s1
InChI Key
FPMLCYUEXWDCDX-WFASDCNBSA-N
Canonical SMILES
CC(C(=O)NC(CC1=CN=CN1)C(=O)OC)NC(=O)OCC2=CC=CC=C2
1.Kinetic studies on the mechanism of pepsin action.
Silver MS, Stoddard M. Biochemistry. 1975 Feb 11;14(3):614-21.
The linear noncompetitive inhibition of the pepsin-catalyzed hydrolysis of Ac-Phe-Phe-Gly at pH 2.1 by L-Ac-Phe, L-Ac-Phe-NH2, and L-Ac-Phe-OEt has been claimed to substantiate the ordered release of products specified by the amino-enzyme mechanism for pepsin action. According to this interpretation, the binding of inhibitor to free enzyme and the amino-enzyme intermediate (Scheme I) generates the observed inhibition pattern. The proposition is valid only if a simple alternative explanation for the kinetic data, Scheme II, can be disproved. Scheme II attributes the inhibition pattern to the binding of inhibitor to free enzyme and the enzyme-substrate (Michaelis) complex. The experiments reported here have enabled us to distinguish between the two mechanisms. The pepsin-catalyzed hydrolyses of Ac-Phe-Trp, Z-H'IS-Phe-Trp, Z-Gly-His-Phe-Trp, and Z-Ala-His-Phe-Trp at pH 1.8 occur exclusively at the Phe-Trp bond and must yield the same amino-enzyme, E-Trp, if it is implicated.
2.The effect of histidyl residues on the complexation of bis(imidazolyl) containing tripeptides with copper(II) ion.
Várnagy K1, Sóvágó I, Süli-Vargha H, Sanna D, Micera G. J Inorg Biochem. 2000 Jul 15;81(1-2):35-41.
Copper(II) complexes of tripeptide derivatives of bis(imidazol-2-yl) group have been studied by potentiometric, UV-visible and EPR spectroscopic methods. The peptide molecules correspond to the amino acid sequence of collagen containing histidyl residues in different locations and were connected to the bis(imidazol-2-yl) group either on the C-termini (BOC-Pro-Leu-His-BIMA, BOC-His-Leu-Gly-BIMA) or on the N-termini (BIP-His-Ala-Gly-OEt, BIP-Ile-Ala-His-OMe). It was concluded that the imidazole nitrogen donor atoms of the bis(imidazol-2-yl) moiety are the primary metal binding sites, but the histidyl imidazole nitrogens in the side chains have also some effect on the stability and the coordination mode of the complexes. All ligands can coordinate tridentately to copper(II) ion forming a six-membered chelate and a macrochelate in the [CuL]2+ complexes, which results in a slight distortion in the coordination geometry of [CuL2]2+ complexes. The deprotonation and coordination of amide nitrogens, however, were not observed in any cases.
3.Antagonists of bombesin/gastrin releasing peptide based on [D-Ala24]GRP(20-26)-heptapeptide. Modifications leading to potent analogues with prolonged duration of action.
Best JR1, Cotton R, Dutta AS, Fleming B, Garner A, Gormley JJ, Hayward CF, McLachlan PF, Scholes PB. Drug Des Deliv. 1990 Oct;6(4):255-71.
Analogues of gastrin releasing peptide (GRP) and bombesin based on His-Trp-Ala-Val-D-Ala-His-Leu, the 20-26 heptapeptide sequence of [D-Ala24]GRP, have been synthesized and tested in vitro for their ability to inhibit GRP (18-27)-induced mitogenesis in Swiss 3T3 cells. Compounds identified as potent antagonists in this test system were also tested in vivo for their ability to inhibit bombesin-induced amylase secretion in rats. The Trp-Ala-Val sequence was found to be a very important feature of the antagonist activity; most substitutions in this region led either to much less potent or inactive analogues. In contrast, amino acid replacements in other parts of the molecule were more tolerated and sometimes led to marked increases in the in vitro and in vivo activity. The most potent analogues were obtained by replacing Leu26 by MeLeu and His25 by Lys(X) where X = Z, PhCO, PhCH2CO or Ph(CH2)2CO. Thus 4-pyridylcarbonyl-His-Trp-Ala-Val-D-Ala-Lys(CO-CH2-CH2-Ph)-Leu- NHMe (86) and 4-pyridylcarbonyl-His-Trp-Ala-Val-D-Ala-Lys(Z)-MeLeu-OMe (87) had IC50 values of less than 20 micrograms/kg s.
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Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2

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Tip: Chemical formula is case sensitive. C22H30N4O c22h30n40
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