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D-Isovaline

目录号 : GC68169

D-Isovaline 是一种缬氨酸衍生物。

D-Isovaline Chemical Structure

Cas No.:3059-97-0

规格 价格 库存 购买数量
500mg
¥2,250.00
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Sample solution is provided at 25 µL, 10mM.

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产品描述

D-Isovaline is a valine derivative[1].

Amino acids and amino acid derivatives have been commercially used as ergogenic supplements. They influence the secretion of anabolic hormones, supply of fuel during exercise, mental performance during stress related tasks and prevent exercise induced muscle damage. They are recognized to be beneficial as ergogenic dietary substances[1].

[1]. Luckose F, et al. Effects of amino acid derivatives on physical, mental, and physiological activities. Crit Rev Food Sci Nutr. 2015;55(13):1793-1144.

Chemical Properties

Cas No. 3059-97-0 SDF Download SDF
分子式 C5H11NO2 分子量 117.15
溶解度 储存条件 Store at -20°C
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 8.5361 mL 42.6803 mL 85.3606 mL
5 mM 1.7072 mL 8.5361 mL 17.0721 mL
10 mM 0.8536 mL 4.268 mL 8.5361 mL
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Research Update

Lipovelutibols A-D: Cytotoxic Lipopeptaibols from the Himalayan Cold Habitat Fungus Trichoderma velutinum

J Nat Prod 2018 Feb 23;81(2):219-226.PMID:29373791DOI:10.1021/acs.jnatprod.6b00873.

Four novel lipovelutibols A (1), B (2), C (3), and D (4) containing six amino acid residues with leucinol at the C-terminus and a fatty acyl moiety (n-octanoyl) at its N-terminus were isolated from the psychrotrophic fungus Trichoderma velutinum collected from the Himalayan cold habitat. The structures (1-4) were determined by NMR and MS/MS, and the stereochemistry of amino acids by Marfey's method. Lipopeptaibols 2 and 4 were found to contain D-Isovaline, a nonproteinogenic amino acid, but lacked α-aminoisobutyric acid, characteristic of peptaibols. Cytotoxic activity of 2 and 4 was observed against HL-60, LS180, MDA-MB-231, and A549 cancer cell lines.

Sequence diversity of the peptaibol antibiotic suzukacillin-A from the mold Trichoderma viride

J Pept Sci 2006 May;12(5):321-7.PMID:16245259DOI:10.1002/psc.728.

From the culture broth of the mold Trichoderma viride, strain 63 C-I, the polypeptide antibiotic suzukacillin (SZ) was isolated. A peptide mixture named SZ-A was obtained by crystallization from crude SZ. Individual peptides from SZ-A were isolated by semipreparative HPLC and sequences were determined by HPLC-ESI-MS. The data confirm a general sequence of SZ-A published previously and in addition establish the individual sequences of 15 acetylated eicosa peptides with C-terminal alcohols. The major peptide SZ-A4 (21% of all peptides) shows the sequence:Ac-Aib-Ala-Aib-Ala-Aib-Ala(6)-Gln-Aib-Lx(9)-Aib-Gly-Aib(12)-Aib-Pro-Vx(15)-Aib-Vx(17)-Gln-Gln-Fol. Amino acid exchanges of the peptaibol are located in position 6 (Ala/Aib), 9 (Vx/Lx), 12 (Aib/Lx), 17 (Aib/Vx) and possibly at position15 (Val/Iva) (uncommon abbreviations: Aib (alpha-aminoisobutyric acid); Iva (D-Isovaline); Lx (L-leucine or L-isoleucine); Vx (L-valine or D-Isovaline); Fol (L-phenylalaninol)).

Trichotoxin A40. Purification by counter-current distribution and sequencing of isolated fragments

Biochim Biophys Acta 1985 Jan 21;827(1):51-62.PMID:2578292DOI:10.1016/0167-4838(85)90100-1.

The isolation of the membrane-modifying polypeptide antibiotics from the mycelium of Trichoderma viride 5242 was optimized via extraction with dichloromethane and chromatography on Sephadex LH-20. The components trichotoxin A40 and A50 were separated from each other and purified by multiplicative counter-current distribution. The sequence of proteinase-resistant trichotoxin A40 was determined by combined gas chromatography and mass spectrometry of three isolated N-acetylated dodecapeptides and two N-prolylhexapeptides obtained after selective trifluoroacetolysis. Including amino acid exchanges due to natural microheterogeneity, the sequence is Ac-Aib-Gly(LAla)-Aib-LLeu-Aib-LGln-Aib-Aib-Aib(LAla )-LAla-Aib-Aib-LPro-LLeu -Aib-DIva(Aib)-LGlu-LValol. In contrast to the eicosapeptide alamethicin, trichotoxin A40 contains only 18 residues, with a higher proportion of alpha-aminoisobutyric acid (Aib), C-terminal L-valinol (Vol), one D-Isovaline (Iva) and no proline at the N-terminal part.

Fungal biosynthesis of non-ribosomal peptide antibiotics and alpha, alpha-dialkylated amino acid constituents

J Pept Sci 2005 Jun;11(6):331-8.PMID:15635654DOI:10.1002/psc.621.

Zervamicins (Zrv) IIA and IIB are membrane modifying peptide antibiotics of fungal origin, characterized by a sequence of 15 amino acid residues. The primary structure of Zrv-IIA contains five alpha-aminoisobutyric acid residues at positions 4, 7, 9, 12 and 14 of the linear peptide. The sequence of Zrv-IIB is similar, but contains a D-Isovaline at position 4. When the free amino acid Aib was added to the peptone-glucose culture medium, the fungus Emericellopsis salmosynnemata produced Zrv-IIA as the major secondary metabolite, whereas addition of DL-Iva to the culture led to a high production of Zrv-IIB. This observation is rationalized by a lack of selectivity of the non-ribosomal peptide synthetase with respect to the thiolester activated amino acid substrates during step 12 of peptide synthesis. Analysis of the configuration of the Iva residue of Zrv-IIB showed a high enantiomeric purity of the D-enantiomer, indicating a high stereoselectivity of the peptide synthetase for this substrate.When the culture was supplemented with [(15)N]DL-Iva, the nitrogen isotope was not only found at the D-Iva residue, but surprisingly also at the Aib residues as well as at the proteinogenic residues of Zrv. The partial catabolism of exogenous [(15)N]DL-Iva is explained by the assumption of a decarboxylation-dependent transamination reaction, catalysed by 2,2-dimethylglycine decarboxylase. The same enzyme might also be involved in the reversed carboxylation reactions of acetone and 2-butanone, during the anabolic biosynthesis of Aib and Iva, respectively. Zrv might possibly act as a thermodynamic sink to shift these equilibrium reactions towards the reversed side.