β-(2-Thienyl)-L-β-homoglycine
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β-(2-Thienyl)-L-β-homoglycine

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Category
β−Amino acids
Catalog number
BAT-007519
CAS number
73495-10-0
Molecular Formula
C7H9NO2S
Molecular Weight
171.22
β-(2-Thienyl)-L-β-homoglycine
IUPAC Name
(3R)-3-amino-3-thiophen-2-ylpropanoic acid
Synonyms
H-Gly(2-Thienyl)-(C#CH2)OH; H-Thg(2)-(C#CH2)OH; (R)-3-Amino-3-(2-thienyl)propanoic acid; 3-Amino-3-(2-thienyl)propanoic acid; (R)-3-Amino-3-(thiophen-2-yl)propanoic acid; (3R)-3-amino-3-thiophen-2-ylpropanoic acid; L-β-Ala-(2-thienyl)-OH; (R)-2-Thienyl-β-phenylalanine; H-β-Ala-(2-thienyl)-OH
Appearance
White powder
Purity
≥ 99% (Chiral purity)
Density
1.345±0.06 g/cm3 (Predicted)
Melting Point
220-225 °C (dec)
Boiling Point
327.6±32.0 °C (Predicted)
Storage
Store at 2-8 °C
InChI
InChI=1S/C7H9NO2S/c8-5(4-7(9)10)6-2-1-3-11-6/h1-3,5H,4,8H2,(H,9,10)/t5-/m1/s1
InChI Key
GYAYLYLPTPXESE-RXMQYKEDSA-N
Canonical SMILES
C1=CSC(=C1)C(CC(=O)O)N
1. Synthesis and some pharmacological properties of (3-beta-(2-thienyl)-L-alanine)-8-lysine-vasopressin
C W Smith, M F Ferger, W Y Chan J Med Chem. 1975 Aug;18(8):822-5. doi: 10.1021/jm00242a012.
[3-beta-(2-Thienyl)-L-alanine]-8-lysine-vasopressin was synthesized by solution techniques. The partially protected heptapeptide Boc-Cys(Ec)-Tyr-Thi-Gln-Asn-Cys(Ec)-Pro (1) was synthesized in a stepwise manner using the active ester method or the dicyclohexylcarbodiimide (DCC) coupling technique mediated by 1-hydroxybenzotriazole (HBt). The protected nonapeptide amide Boc-Cys(Ec)-Tyr-Thi-Gin-Asn-Cys(Ec)-Pro-Lys(Coc)-Gly-NH2 (2) was prepared by coupling 1 with Lys(Coc)-Gly-NH2 using DCC-HBt. From 2, [3-thienylalanine]-8-lysine-vasopressin was obtained by removing the Boc-protecting groups with trifluoroacetic acid and ethylcarbamoyl (Ec) protecting groups in refluxing liquid NH3 followed by oxidative cyclization in H2O-MeOH using ICH2CH2I. Purification was effected by partition chromatography followed by gel filtration. The highly purified product possesses activities in the oxytocic, avian vasodepressor, rat pressor, and antidiuretic assays of 19.0 +/- 0.5, 87 +/- 4, 243 +/- 5, and 332 +/- 32 units/mg, respectively. Thus [3-thienylalanine]-8-lysine-vasopressin has higher oxytocic, avian vasodepressor, and antidiuretic potencies than does 8-lysine-vasopressin, whereas its pressor potency is about the same as or slightly lower than that of 8-lysine-vasopressin.
2. Competitive antagonists of bradykinin
R J Vavrek, J M Stewart Peptides. 1985 Mar-Apr;6(2):161-4. doi: 10.1016/0196-9781(85)90033-6.
The first sequence-related competitive inhibitors of the classic kinin in vitro (rat uterus guinea pig ileum) and in vivo (rat blood pressure) assays have been developed. Replacement of the proline residue at position 7 of bradykinin (BK) with a D-phenylalanine residue is the key modification which converts BK agonists into antagonists. [D-Phe7]-BK exhibits moderate (pA2 = 5.0) inhibition of BK activity on the guinea pig ileum but possesses weak BK-like myotropic activity on the isolated rat uterus and 2-4% of BK depressor potency in the rat blood pressure assay. The additional replacement of the phenylalanine residues at positions 5 and 8 of [D-Phe7]-BK with the isosteric beta-(2-thienyl)-alanine residue produces a potent antagonist of BK activity on the uterus (pA2 = 6.4), ileum (pA2 = 6.3), and in the rat blood pressure assay. The antagonism of BK action on smooth muscle is specific for kinins (BK, kallidin, Met-Lys-BK), but neither inhibitor antagonizes the smooth muscle activity of angiotensin or substance P. Inhibition is competitive and fully reversible.
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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