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Application Area

β-Cyclohexyl-L-alanine

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category

L-Amino Acids

Catalog number

BAT-005819

CAS number

27527-05-5

Molecular Formula

C9H17NO2

Molecular Weight

171.20

IUPAC Name

(2S)-2-amino-3-cyclohexylpropanoic acid

Synonyms

L-Cha-OH; 3-Cyclohexyl-L-alanine; (S)-2-Amino-3-cyclohexylpropionic acid

Appearance

Off-white to white powder

Purity

≥ 99% (Chiral purity, HPLC)

Density

1.075g/cm3

Melting Point

322°C

Boiling Point

307.1°C at 760mmHg

Storage

Store at 2-8°C

InChI

InChI=1S/C9H17NO2/c10-8(9(11)12)6-7-4-2-1-3-5-7/h7-8H,1-6,10H2,(H,11,12)/t8-/m0/s1

InChI Key

ORQXBVXKBGUSBA-QMMMGPOBSA-N

Canonical SMILES

C1CCC(CC1)CC(C(=O)O)N

β-Cyclohexyl-L-alanine, a non-proteinogenic amino acid with diverse applications in bioscience, is a versatile tool in various domains. Here are the key applications of β-Cyclohexyl-L-alanine presented with high perplexity and burstiness:

Drug Development: Embedded in the landscape of pharmaceutical innovation, β-Cyclohexyl-L-alanine plays a pivotal role in the formulation and synthesis of cutting-edge therapeutic compounds. Its distinctive molecular structure can optimize the pharmacokinetic profiles of peptides and proteins. By integrating β-Cyclohexyl-L-alanine into drug prototypes, researchers can elevate their stability, efficacy, and bioavailability, forging new avenues for enhanced medical treatments.

Protein Engineering: In the intricate realm of protein manipulation, β-Cyclohexyl-L-alanine emerges as a key catalyst for engineering proteins with heightened functionalities or novel characteristics. Through strategic substitution of this amino acid at specific loci within protein sequences, scientists can probe the impact on protein folding dynamics, stability, and enzymatic activity. This strategic approach is imperative for crafting biologics with enhanced therapeutic attributes, propelling the frontier of medical biotechnology.

Enzyme Inhibition Studies: Serving as a cornerstone for unraveling the intricacies of enzyme inhibition mechanisms, β-Cyclohexyl-L-alanine stands as an invaluable asset in biochemistry research. Functioning as a mimetic substrate, it aids in deciphering the intricate interplays between enzymes and inhibitory agents, shedding light on crucial interactions. Such profound insights are indispensable for the formulation of enzyme-targeted medications and the elucidation of metabolic regulations, sculpting the future landscape of pharmaceutical interventions.

Peptide Synthesis: Nestled at the core of peptide design and synthesis, β-Cyclohexyl-L-alanine emerges as a fundamental building block with transformative implications. Its integration modulates the conformational characteristics and biological functionalities of peptides, ushering in new vistas for peptide-based therapeutics and biomaterial development. This innovative approach not only expands horizons for medical applications but also heralds a new era of peptide-driven solutions for diverse healthcare challenges.

1. Conformation analysis of aspartame-based sweeteners by NMR spectroscopy, molecular dynamics simulations, and X-ray diffraction studies

Antonia De Capua, Murray Goodman, Yusuke Amino, Michele Saviano, Ettore Benedetti Chembiochem. 2006 Feb;7(2):377-87. doi: 10.1002/cbic.200500332.

We report here the synthesis and the conformation analysis by 1H NMR spectroscopy and computer simulations of six potent sweet molecules, N-[3-(3-hydroxy-4-methoxyphenyl)-3-methylbutyl]-alpha-L-aspartyl-S-tert-butyl-L-cysteine 1-methylester (1; 70 000 times more potent than sucrose), N-[3-(3-hydroxy-4-methoxyphenyl)-3-methylbutyl]-alpha-L-aspartyl-beta-cyclohexyl-L-alanine 1-methylester (2; 50 000 times more potent than sucrose), N-[3-(3-hydroxy-4-methoxyphenyl)-3-methylbutyl]-alpha-L-aspartyl-4-cyan-L-phenylalanine 1-methylester (3; 2 000 times more potent than sucrose), N-[3,3-dimethylbutyl]-alpha-L-aspartyl-(1R,2S,4S)-1-methyl-2-hydroxy-4-phenylhexylamide (4; 5500 times more potent than sucrose), N-[3-(3-hydroxy-4-methoxyphenyl)propyl]-alpha-L-aspartyl-(1R,2S,4S)-1-methyl-2-hydroxy-4-phenylhexylamide (5; 15 000 times more potent than sucrose), and N-[3-(3-hydroxy-4-methoxyphenyl)-3-methylbutyl]-alpha-L-aspartyl-(1R,2S,4S)-1-methyl-2-hydroxy-4-phenylhexylamide (6; 15 000 times more potent than sucrose). The "L-shaped" structure, which we believe to be responsible for sweet taste, is accessible to all six molecules in solution. This structure is characterized by a zwitterionic ring formed by the AH- and B-containing moieties located along the +y axis and by the hydrophobic group X pointing into the +x axis. Extended conformations with the AH- and B-containing moieties along the +y axis and the hydrophobic group X pointing into the -y axis were observed for all six sweeteners. For compound 5, the crystal-state conformation was also determined by an X-ray diffraction study. The result indicates that compound 5 adopts an L-shaped structure even in the crystalline state. The extraordinary potency of the N-arylalkylated or N-alkylated compounds 1-6, as compared with that of the unsubstituted aspartame-based sweet taste ligands, can be explained by the effect of a second hydrophobic binding domain in addition to interactions arising from the L-shaped structure. In our examination of the unexplored D zone of the Tinti-Nofre model, we discovered a sweet-potency-enhancing effect of arylalkyl substitution on dipeptide ligands, which reveals the importance of hydrophobic (aromatic)-hydrophobic (aromatic) interactions in maintaining high potency.

2. New dsDNA binding unnatural oligopeptides with pyrimidine selectivity

Zhenyu Zhang, Patrick Chaltin, Arthur Van Aerschot, Jeff Lacey, Jef Rozenski, Roger Busson, Piet Herdewijn Bioorg Med Chem. 2002 Nov;10(11):3401-13. doi: 10.1016/s0968-0896(02)00268-7.

Solid phase peptide library screening followed by extension of a lead recognition element for binding to a dsDNA sequence (NF binding site of IL6) using solution phase screening, delivered a new DNA binding peptide, Ac-Arg-Ual-Sar-Chi-Chi-Tal-Arg-CONH2. In the present research, the contribution of the different amino acid side chains to the binding strength of the peptide to dsDNA was investigated using an ethidium bromide displacement test. Based on these results, the lead structure was optimized by deconvolution. Eight new unnatural amino acids were evaluated at two positions of the heptapeptide replacing the Ual-Sar fragment. The strongest dsDNA binding was observed using ([(3-chlorophenyl)methyl]amino)acetic acid (Cbg) and beta-cyclohexyl-l-alanine (Cha) respectively, at those two positions. A 10-fold increase in affinity compared to the Ual-Sar sequence was obtained. Further enhancement of dsDNA binding was obtained with hybrid molecules linking the newly developed peptide fragment to an acridine derivative with a flexible spacer. This resulted in ligands with affinities in the microM range for the dsDNA target (K(d) of 2.1 x 10(-6) M). DNase I footprinting with the newly developed oligopeptide motifs showed the presence of a pronounced pyrimidine specificity, while conjugation to an intercalator seems to redirect the interaction to mixed sequences. This way, new unnatural oligopeptide motifs and hybrid molecules have been developed endowed with different sequence selectivities. The results demonstrate that the unnatural peptide library approach combined with subsequent modification of selected amino acid positions, is very suited for the discovery of novel sequence-specific dsDNA binding ligands.