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γ-(2-Furyl)-L-β-homoalanine

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

Category

β−Amino Acids

Catalog number

BAT-007540

CAS number

270263-05-3

Molecular Formula

C8H11NO3

Molecular Weight

169.18

IUPAC Name

(3S)-3-amino-4-(furan-2-yl)butanoic acid

Synonyms

H-Ala(2-Furyl)-(C#CH2)OH; (S)-3-Amino-4-(2-furyl)butanoic acid; L-β-HomoAla(2-furyl)-OH; (2-Furyl)-L-β-homoalanine; 3-azanyl-4-(furan-2-yl)butanoic acid; (S)-3-amino-4-(furan-2-yl)butanoic acid; (2-Furyl)-L-b-homoalanine

Appearance

Gray to off-gray or yellow powder

Purity

≥ 99% (HPLC)

Density

1.237 g/cm3 (Predicted)

Melting Point

191-195 °C (dec.)

Boiling Point

306.5 °C at 760 mmHg

Storage

Store at 2-8 °C

InChI

InChI=1S/C8H11NO3/c9-6(5-8(10)11)4-7-2-1-3-12-7/h1-3,6H,4-5,9H2,(H,10,11)/t6-/m0/s1

InChI Key

ZIAIKPBTLUWDMG-LURJTMIESA-N

Canonical SMILES

C1=COC(=C1)CC(CC(=O)O)N

γ-(2-Furyl)-L-β-homoalanine, a distinctive amino acid derivative, finds diverse applications across biochemistry, pharmaceuticals, and synthetic chemistry. Explore its key applications with elevated perplexity and burstiness:

Pharmaceutical Development: In the realm of pharmaceutical research, γ-(2-Furyl)-L-β-homoalanine emerges as a promising candidate for designing and synthesizing novel therapeutic agents. Its intricate structure serves as a template for drug development, potentially heralding breakthrough treatments for ailments like cancer and infectious diseases. Through strategic modifications, researchers can amplify its biological efficacy while mitigating toxicity risks.

Biocatalysis: Within the domain of industrial biocatalysis, γ-(2-Furyl)-L-β-homoalanine assumes a pivotal role as an enzyme substrate, facilitating precise chemical transformations. Leveraging this amino acid derivative, enzymatic processes witness heightened efficiency and selectivity, fostering the production of fine chemicals and pharmaceuticals. This integration advances industrial operations, driving sustainability and cost-effectiveness.

Peptide Synthesis: Delving into the realm of peptide synthesis, γ-(2-Furyl)-L-β-homoalanine proves instrumental in crafting peptides endowed with distinct properties. Its incorporation into peptide sequences imparts altering structural and functional attributes, offering avenues for developing innovative biomaterials and delving into protein-protein interactions. This application promises novel insights and opportunities for the biotechnological landscape.

Chemical Biology: Underscoring the significance of γ-(2-Furyl)-L-β-homoalanine in chemical biology, researchers harness its potential as a tool for investigating protein dynamics and interactions. Through targeted integration into proteins via site-specific mutagenesis, scientists unravel intricate details regarding protein function, stability, and molecular mechanisms underlying biological processes. This exploration fuels the development of cutting-edge therapeutic approaches and deepens our understanding of life's intricate molecular choreography.

1. Mediators of non-adrenergic non-cholinergic inhibitory neurotransmission in porcine jejunum

N M Matsuda, S M Miller, L Sha, G Farrugia, J H Szurszewski Neurogastroenterol Motil. 2004 Oct;16(5):605-12. doi: 10.1111/j.1365-2982.2004.00574.x.

The purpose of this study was to determine the non-adrenergic non-cholinergic inhibitory neurotransmitter in pig jejunum. Intracellular electrical activity was recorded from circular smooth muscle cells. Inhibitory junction potentials (IJPs) evoked by electrical field stimulation were inhibited by tetrodotoxin (1 micromol L(-1)), omega-conotoxin GVIA (0.1 micromol L(-1)) tetrodotoxin, apamin (1 micromol L(-1)), 1-[6-((17beta-3-methoxyestra-1,3,5(10)-trien-17-yl)amino)hexyl]-1H-pyrrole-2,5-dione (U-73122; 10 micromol L(-1)) but not by N omega-nitro-l-arginine (l-NNA; 100 micromol L(-1)), haemoglobin (10 micromol L(-1)), 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one (ODQ; 10 micromol L(-1)) or 9-(tetrahydro-2-furyl)adenine (SQ-22536; 10 micromol L(-1)). S-nitroso-N-acetylpenicillamine (SNAP) hyperpolarized the membrane potential. This was inhibited by ODQ (3 micromol L(-1)) and charybdotoxin (0.1 micromol L(-1)). Adenosine-5-triphosphate (ATP; 100 micromol L(-1)) and 2-methylthio ATP (2-MeS-ATP; 100 micromol L(-1)) did not hyperpolarize the membrane potential and 6-N-N-diethyl-beta- gamma -dibromomethylene-d-adenosine-5'-triphosphate (ARL67156; 100 micromol L(-1)) did not modify IJPs. Carbon monoxide (CO; 10%) and tricarbonyl dichlororuthenium dimer ([Ru(CO3Cl2)]2; 100 micromol L(-1)) hyperpolarized the membrane potential however zinc, copper and tin protoporphyrin IX (100 micromol L(-1)) did not alter IJPs. Vasoactive intestinal peptide (VIP) hyperpolarized the membrane potential but 4-Cl-d-Phe6-Leu17-VIP (1 micromol L(-1)) did not modify IJPs. Pituitary adenylate cyclase activating peptide (PACAP)38 (0.5 micromol L(-1)) hyperpolarized the membrane potential. This was inhibited by apamin (1 micromol L(-1)) but not by tetrodotoxin (1 micromol L(-1)). Pituitary adenylate cyclase activating peptide6-38 (1 micromol L(-1)) inhibited IJPs. These data suggest that inhibitory neurotransmission in pig jejunum is mediated partly by PACAP.

2. Inhibitors of synaptosomal gamma-hydroxybutyrate transport

S J McCormick, G Tunnicliff Pharmacology. 1998 Sep;57(3):124-31. doi: 10.1159/000028233.

Synaptosomes prepared from mouse brain possess a Na+-dependent transport system for gamma-hydroxybutyrate displaying saturation kinetics, the transport constant (Kt) for which was calculated as 31 +/- 9 micromol/l. Several gamma-hydroxybutyrate and gamma-aminobutyric acid (GABA) structural analogues were tested as potential inhibitors of gamma-hydroxybutyrate transport. The most effective inhibitor was harmaline (Ki = 94 +/- 21 micromol/l), a known competitive inhibitor of Na+ binding to certain transport proteins. 2-Hydroxycinnamic acid, 3-(2-furyl)acrylic acid and citrazinic acid also inhibited transport and were competitive with respect to gamma-hydroxybutyrate. The least effective gamma-hydroxybutyrate analogues were 3-hydroxypropane sulfonic acid (Ki = 4.1 +/- 0.8 mmol/l) 3,5-dihydroxybenzoic acid (Ki = 6.1 +/- 2. 8 mmol/l) and 3-hydroxybenzoic acid (Ki = 6.9 +/- 3.3 mmol/l), although 2-hydroxypropane sulfonic acid and kynurenic acid had no measurable effects. Four inhibitors of GABA transport - nipecotic acid, guvacine, ketamine and beta-alanine and GABA itself, were without effect on gamma-hydroxybutyrate transport. These results show that certain drugs that structurally resemble gamma-hydroxybutyrate have the capacity to compete with gamma-hydroxybutyrate at its recognition site on the transporter. By examining the structure of such inhibitors, we can learn more about the properties of the substrate binding site on the carrier protein. Moreover, the absence of inhibition by GABA uptake inhibitors shows that gamma-hydroxybutyrate transport is a separate entity from GABA transport.