β-(2-Thienyl)-DL-alanine
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β-(2-Thienyl)-DL-alanine

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Category
DL-Amino Acids
Catalog number
BAT-005808
CAS number
2021-58-1
Molecular Formula
C7H9NO2S
Molecular Weight
171.20
β-(2-Thienyl)-DL-alanine
IUPAC Name
2-amino-3-thiophen-2-ylpropanoic acid
Synonyms
3-DL-Ala(2-thienyl)-OH; 2-Amino-3-(2-thienyl)propionic acid
Appearance
Off-white crystals
Purity
≥ 99% (HPLC)
Density
1.349g/cm3
Melting Point
256-260 °C
Storage
Store at 2-8°C
InChI
InChI=1S/C7H9NO2S/c8-6(7(9)10)4-5-2-1-3-11-5/h1-3,6H,4,8H2,(H,9,10)
InChI Key
WTOFYLAWDLQMBZ-UHFFFAOYSA-N
Canonical SMILES
C1=CSC(=C1)CC(C(=O)O)N

β-(2-Thienyl)-DL-alanine, a synthetic amino acid derivative, stands out for its diverse array of specialized applications in biochemical and pharmaceutical research. Delve into the key applications presented with a high degree of perplexity and burstiness:

Enzyme Inhibition Studies: Venture into the intricate domain of enzyme inhibition, where β-(2-Thienyl)-DL-alanine plays a pivotal role. Acting as a substrate analog, this compound unravels the binding sites and mechanisms of action of amino acid-related enzymes, such as transaminases. Through these rigorous investigations, researchers plunge deeper into the complexities of enzyme function, paving the path for the development of therapeutic enzyme inhibitors.

Neuropharmacology: Shedding light on its significance in neuropharmacological research, β-(2-Thienyl)-DL-alanine offers insights into the transport mechanisms of amino acids across the blood-brain barrier. By dissecting its interactions with amino acid transporters, researchers glean essential knowledge about nutrient transport and potential strategies for drug delivery to the central nervous system. This application holds particular importance in the quest to formulate treatments for neurological disorders.

Radiolabeling: Enter the realm of radiolabeling with β-(2-Thienyl)-DL-alanine taking the spotlight in positron emission tomography (PET) imaging studies. Its incorporation into radiotracers enables the visualization and quantification of metabolic processes in living organisms, providing a unique window into clinical diagnostics and metabolic research. These non-invasive methods offer a lens through which disease states and treatment responses can be meticulously scrutinized.

Protein Structure Analysis: Navigate the intricate landscape of structural biology, where β-(2-Thienyl)-DL-alanine emerges as a valuable tool for probing the active sites of proteins and enzymes. By integrating this analog into proteins, scientists unlock the potential of techniques like X-ray crystallography and nuclear magnetic resonance (NMR) to unveil the structural conformations and interactions within proteins. These profound explorations aid in designing innovative drugs and deciphering protein functions, propelling the forefront of pharmaceutical research.

1. Transamination in the metabolism of beta-2-thienyl-DL-alanine in normal and neoplastic cells in vitro
J A JACQUEZ, R K BARCLAY, C C STOCK J Exp Med. 1952 Nov;96(5):499-512. doi: 10.1084/jem.96.5.499.
In tissue cultures of C-57 black mouse heart and sarcoma T-241, beta-2-thienyl-DL-alanine acts specifically as a phenylalanine antagonist. Heart cultures can transaminate between beta-2-thienyl-DL-alanine and phenylpyruvate to form L-phenylalanine and thus block the toxic action of the remaining beta-2-thienyl-DL-alanine, whereas sarcoma T-241 cultures cannot. Of eleven mouse tumors and four rat tumors tested for their ability to perform this reaction, nine tumors had little or no activity. The beta-2-thienylpyruvic acid resulting from transamination further reacts to form a red compound the exact structure of which is not yet known.
3. beta-2-Thienyl-DL-alanine as an inhibitor of phenylalanine hydroxylase and phenylalanine intestinal transport
R A Wapnir, G S Moak Biochem J. 1979 Jan 1;177(1):347-52. doi: 10.1042/bj1770347.
The inhibitory properties of beta-2-thienyl-dl-alanine on rat phenylalanine hydroxylase from crude liver and kidney homogenates were assessed in vitro and in vivo, as well as its effects on the intestinal transport of phenylalanine, by using a perfusion procedure in vivo. The apparent K(m) for liver phenylalanine hydroxylase changed from 0.61mm in the absence of the inhibitor to 2.70mm in the presence of 24mm-beta-2-thienyl-dl-alanine, with no significant change in the V(max.). For kidney the corresponding values were 0.50 and 1.60mm respectively. A single dose of beta-2-thienyl-dl-alanine (2mmol/kg) failed to inhibit phenylalanine hydroxylase in either organ. Repeated injections during a 4-day period caused a decline of the enzymic activity to about 40% of controls. Intestinal absorption of phenylalanine when perfused at 0.2-2.0mm concentration was also competitively inhibited by beta-2-thienyl-dl-alanine. Its K(i) value was estimated at 81mm. The limited inhibitory effects of beta-2-thienyl-dl-alanine towards hepatic phenylalanine hydroxylase and phenylalanine intestinal transport, and its rapid metabolism, as suggested by the small elimination of this compound in the urine and its virtual absence from animal tissues, are factors that restrict its potential usefulness as an inducer of phenylketonuria in rats or as an effective blocker of phenylalanine absorption by the gut.
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