Z-L-alanine amide
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Z-L-alanine amide

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Category
Other Unnatural Amino Acids
Catalog number
BAT-004275
CAS number
13139-27-0
Molecular Formula
C11H14N2O3
Molecular Weight
222.25
Z-L-alanine amide
IUPAC Name
benzyl N-[(2S)-1-amino-1-oxopropan-2-yl]carbamate
Synonyms
Z-L-Ala-NH2
Appearance
White to off-white powder
Purity
≥ 98% (HPLC)
Melting Point
131-136 °C
Storage
Store at 2-8°C
InChI
InChI=1S/C11H14N2O3/c1-8(10(12)14)13-11(15)16-7-9-5-3-2-4-6-9/h2-6,8H,7H2,1H3,(H2,12,14)(H,13,15)/t8-/m0/s1
InChI Key
CTZZSWNVVFTJRN-QMMMGPOBSA-N
Canonical SMILES
CC(C(=O)N)NC(=O)OCC1=CC=CC=C1

Z-L-alanine amide, a significant compound in the bioscience industry, boasts diverse critical applications. Below are presented the key applications of Z-L-alanine amide, articulated with a high degree of perplexity and burstiness:

Peptide Synthesis: Found commonly as a building block in peptide synthesis, Z-L-alanine amide offers stability and protection against enzymatic breakdown—a vital aspect in crafting peptides for pharmaceutical uses. Researchers integrate Z-L-alanine amide into peptide chains to enhance their pharmacokinetic attributes, thereby advancing the realm of drug development.

Enzyme Substrate: Within enzymology, Z-L-alanine amide serves as a substrate for exploring aminopeptidase and amidase activities. Through monitoring the enzymatic response with Z-L-alanine amide, scientists delve into enzyme kinetics and selectivity, fostering insights that could pave the way for developing enzyme inhibitors as potential therapeutic solutions.

Chiral Auxiliary: Functioning as a chiral auxiliary in asymmetric synthesis, Z-L-alanine amide aids in establishing chiral centers with exceptional enantiomeric purity—an essential requirement for producing optically active drugs. This application proves invaluable in synthesizing intricate organic compounds where stereochemistry plays a fundamental role.

Biochemical Research: In the realm of biochemical assays and experiments, Z-L-alanine amide emerges as a valuable tool. Acting as a probe, it enables the investigation of preferences and binding characteristics of specific proteins and enzymes, shedding light on protein functionalities and interactions crucial for drug discovery and development efforts.

1. Chirality in microcystins
T Krishnamurthy J Am Soc Mass Spectrom. 1994 Aug;5(8):724-30. doi: 10.1016/1044-0305(94)80004-9.
A new method has been developed to identify the isomers of amino acids by derivatization of the corresponding standards with 1-fluoro-2,4-dinitrophenyl-5-L-alanine amide (Marfey's reagent or FDAA) and analysis of the diastereomeric derivatives by a liquid chromatography-thermospray mass spectrometry technique. Quantification of the FDAA derivatives that originate from standards was possible by using L-phenylalanine as the internal standard. The procedure was applied to determine the chiralities of the amino acids present in some previously uncharacterized blue-green algal peptides (microcystins).
2. The intrinsic helix-forming tendency of L-alanine
J Vila, R L Williams, J A Grant, J Wójcik, H A Scheraga Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7821-5. doi: 10.1073/pnas.89.16.7821.
Conformational energy calculations have been carried out for three hexadecapeptides in water--namely, a copolymer with the sequence acetyl-AAAAKAAAA-KAAAAKA-amide, 3K(I), in both the charged and neutral forms; a neutral peptide with the sequence acetyl-AAQAAAAQAAAAQAAY-amide, AQY; and a 16-residue L-alanine homopolymer with acetyl and amide terminal groups. The conformational energy was a sum of the empirical conformational energy program for peptides (ECEPP/2) potential energy plus continuum hydration free energy. An empirical (JRF) parameter set was used for the hydration free energy, together with an electrostatic contribution to the solvent effect from charged lysines. The computed relatively high helix content of the most probable conformation of charged 3K(I) and the intermediate helix content of AQY agree reasonably well with experimental values. The computed very low helix content of the alanine homopolymer agrees with experiments on block copolymers and on host-guest random copolymers. The calculations suggest that the high helix content computed for 3K(I) is due to the sum of internal and hydration free energies of the lysine residues rather than to a high intrinsic helix-forming tendency of alanine. The principal component lowering the computed helix contents of AQY and the alanine copolymer relative to 3K(I) is hydration.
3. Double axial chirality promoted asymmetric [2,3] Stevens rearrangement of N-cinnamyl L-alanine amide-derived ammonium ylides
Eiji Tayama, Noriko Naganuma, Hajime Iwamoto, Eietsu Hasegawa Chem Commun (Camb). 2014 Jul 4;50(52):6860-2. doi: 10.1039/c4cc02536a.
The base-induced asymmetric [2,3] Stevens rearrangement of N-cinnamyl tetraalkylammonium ylides derived from L-alanine amides proceeds via a double axially chiral intermediate to afford the corresponding α-substituted alanine derivatives with high enantio- and diastereoselectivities.
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