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β-(8-Quinoyl)-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-002207

CAS number

137940-23-9

Molecular Formula

C12H12N2O2

Molecular Weight

216.24

IUPAC Name

(2S)-2-amino-3-quinolin-8-ylpropanoic acid

Synonyms

H-Ala(8-Qui)-OH; H-Qal(8)-OH; 3-(8-Quinolinyl)-L-alanine

InChI

InChI=1S/C12H12N2O2/c13-10(12(15)16)7-9-4-1-3-8-5-2-6-14-11(8)9/h1-6,10H,7,13H2,(H,15,16)/t10-/m0/s1

InChI Key

IMFYLYWEXLUDKO-JTQLQIEISA-N

Canonical SMILES

C1=CC2=C(C(=C1)CC(C(=O)O)N)N=CC=C2

β-(8-Quinoyl)-L-alanine, a synthetic amino acid derivative, holds vast potential in bioscience. Here are the key applications of β-(8-Quinoyl)-L-alanine, presented with high perplexity and burstiness:

Cancer Research: Serving as a potent ally in the arena of cancer research, β-(8-Quinoyl)-L-alanine emerges as a pivotal player in inhibiting specific cellular pathways that fuel tumor growth and proliferation. Researchers wield this compound as a lens to scrutinize its impact on cancer cell viability and apoptosis, unraveling its intricate dance within the realm of oncology. By unraveling its mechanism of action, novel anticancer therapies stand on the cusp of realization, heralding a new dawn in the war against cancer.

Neuropharmacology: Delving into the mysteries of neuroscience, β-(8-Quinoyl)-L-alanine emerges as a potent probe in exploring its effects on neurotransmitter systems. This compound holds the power to tweak the functioning of receptors and enzymes intertwined with neurological processes, laying the foundation for groundbreaking treatments in neurodegenerative disorders and psychiatric maladies. The journey of discovery into the intricate web of the brain's inner workings takes a leap forward with the use of this versatile compound.

Enzyme Inhibition Studies: Stepping into the realm of biochemical intricacies, β-(8-Quinoyl)-L-alanine finds its niche in enzyme inhibition studies. This compound assumes the role of a competitive inhibitor in biochemical assays, offering a window into the kinetics and regulatory mechanisms governing enzymatic reactions. Armed with this knowledge, researchers navigate the intricate terrain of enzyme regulation, paving the way for tailored inhibitors with therapeutic promise.

Fluorescent Probing: Casting a vibrant glow in the field of molecular biology, β-(8-Quinoyl)-L-alanine transforms into a fluorescent beacon in scientific experiments. Its alluring fluorescence properties illuminate the path for tracking molecular interactions and monitoring biochemical processes in real-time. This application serves as a powerful tool for visualizing cellular events and delving into the dynamic realm of protein behaviors, shedding light on the intricate dance of life at the molecular level.

1. Biochemistry of plants N-heterocyclic non-protein amino acids

Vishal Singh Negi, Archana Pal, Dulal Borthakur Amino Acids. 2021 Jun;53(6):801-812. doi: 10.1007/s00726-021-02990-0. Epub 2021 May 5.

Plants catalyze the biosynthesis of a large number of non-protein amino acids, which are usually toxic for other organisms. In this review, the chemistry and metabolism of N-heterocyclic non-protein amino acids from plants are described. These N-heterocyclic non-protein amino acids are composed of β-substituted alanines and include mimosine, β-pyrazol-1-yl-L-alanine, willardiine, isowillardiine, and lathyrine. These β-substituted alanines consisted of an N-heterocyclic moiety and an alanyl side chain. This review explains how these individual moieties are derived from their precursors and how they are used as the substrate for biosynthesizing the respective N-heterocyclic non-protein amino acids. In addition, known catabolism and possible role of these non-protein amino acids in the actual host is explained.

2. A reconnaissance DFT study of the full conformational analysis of N-formyl-L-serine-L-alanine-NH2 dipeptide

Behzad Chahkandi, Mohammad Chahkandi J Mol Model. 2020 May 24;26(6):151. doi: 10.1007/s00894-020-04382-9.

Theoretical conformational analysis of N-formyl-L-serine-L-alanine-NH2 dipeptide model was investigated using B3LYP/6-311+G(d,p) and M06-2X/6-311+G(d,p) calculations. In this research, 243 total possible conformations of the dipeptide model were optimized including 87 stable conformers and the other disappeared ones migrated to more stable geometries. Migration pattern suggests more stability of the dipeptide model with the serine (ser) in βL, γL, and γD and the alanine (ala) in γD and γL configurations, along with 26 of the found conformers having β-turn structures. Our calculations reveal that the most stable conformer, γL+γD, is in β-turn region of Ramachandran map; therefore, serine-alanine (ser-ala) dipeptide model should be adopted with a β-turn conformation. The atoms in molecules (AIM) topological analysis was carried out to characterize the nature of the intramolecular hydrogen bonding in β-turn structures. The γL+γD, including three hydrogen bonds, has the highest stability, while αLaγL as the most unstable β-turn conformer bears two and one hydrogen bonds at the B3LYP/6-311+G(d,p) and M06-2X/6-311+G(d,p) levels of theory, respectively. Graphical abstract.

3. Exogenous d-β-hydroxybutyrate lowers blood glucose in part by decreasing the availability of L-alanine for gluconeogenesis

Adrian Soto-Mota, Nicholas G Norwitz, Rhys D Evans, Kieran Clarke Endocrinol Diabetes Metab. 2022 Jan;5(1):e00300. doi: 10.1002/edm2.300. Epub 2021 Nov 16.

Background: Interventions that induce ketosis simultaneously lower blood glucose and the explanation for this phenomenon is unknown. Additionally, the glucose-lowering effect of acute ketosis is greater in people with type 2 diabetes (T2D). On the contrary, L-alanine is a gluconeogenic substrate secreted by skeletal muscle at higher levels in people with T2D and infusing of ketones lower circulating L-alanine blood levels. In this study, we sought to determine whether supplementation with L-alanine would attenuate the glucose-lowering effect of exogenous ketosis using a ketone ester (KE). Methods: This crossover study involved 10 healthy human volunteers who fasted for 24 h prior to the ingestion of 25 g of d-β-hydroxybutyrate (βHB) in the form of a KE drink (ΔG® ) on two separate visits. During one of the visits, participants additionally ingested 2 g of L-alanine to see whether L-alanine supplementation would attenuate the glucose-lowering effect of the KE drink. Blood L-alanine, L-glutamine, glucose, βHB, free fatty acids (FFA), lactate and C-peptide were measured for 120 min after ingestion of the KE, with or without L-alanine. Findings: The KE drinks elevated blood βHB concentrations from negligible levels to 4.52 ± 1.23 mmol/L, lowered glucose from 4.97 ± SD 0.39 to 3.77 ± SD 0.40 mmol/L, and lowered and L-alanine from 0.56 ± SD 0.88 to 0.41 ± SD 0.91 mmol/L. L-alanine in the KE drink elevated blood L-Alanine by 0.68 ± SD 0.15 mmol/L, but had no significant effect on blood βHB, L-glutamine, FFA, lactate, nor C-peptide concentrations. By contrast, L-alanine supplementation significantly attenuated the ketosis-induced drop in glucose from 28% ± SD 8% to 16% ± SD 7% (p < .01). Conclusions: The glucose-lowering effect of acutely elevated βHB is partially due to βHB decreasing L-alanine availability as a substrate for gluconeogenesis.