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(R)-3-Hydroxybutanoic acid Sale

(Synonyms: (R)-3-羟基丁酸,(R)-(-)-3-Hydroxybutanoic acid; (R)-3-Hydroxybutyric acid) 目录号 : GC30210

(R)-3-Hydroxybutanoic acid (R-3HB, D-3-hydroxybutyric acid) is a monomer of PHB (poly[(R)-3-hydroxybutyrate]) with wide industrial and medical applications. (R)-3-hydroxybutyric acid can also serve as chiral precursor for synthesis of pure biodegradable PHB and its copolyesters.

(R)-3-Hydroxybutanoic acid Chemical Structure

Cas No.:625-72-9

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产品描述

(R)-3-Hydroxybutanoic acid (R-3HB, D-3-hydroxybutyric acid) is a monomer of PHB (poly[(R)-3-hydroxybutyrate]) with wide industrial and medical applications. (R)-3-hydroxybutyric acid can also serve as chiral precursor for synthesis of pure biodegradable PHB and its copolyesters.

[1] Yutaka Tokiwa, Charles U Ugwu. J Biotechnol. 2007 Nov 1;132(3):264-72.

Chemical Properties

Cas No. 625-72-9 SDF
别名 (R)-3-羟基丁酸,(R)-(-)-3-Hydroxybutanoic acid; (R)-3-Hydroxybutyric acid
Canonical SMILES C[C@@H](O)CC(O)=O
分子式 C4H8O3 分子量 104.1
溶解度 Water : ≥ 25 mg/mL (240.15 mM) 储存条件 Store at -20°C
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1 mM 9.6061 mL 48.0307 mL 96.0615 mL
5 mM 1.9212 mL 9.6061 mL 19.2123 mL
10 mM 0.9606 mL 4.8031 mL 9.6061 mL
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Research Update

Proof for a nonproteinaceous calcium-selective channel in Escherichia coli by total synthesis from (R)-3-Hydroxybutanoic acid and inorganic polyphosphate

Proc Natl Acad Sci U S A 1997 Aug 19;94(17):9075-9.9256437 PMC23036

Traditionally, the structure and properties of natural products have been determined by total synthesis and comparison with authentic samples. We have now applied this procedure to the first nonproteinaceous ion channel, isolated from bacterial plasma membranes, and consisting of a complex of poly(3-hydroxybutyrate) and calcium polyphosphate. To this end, we have now synthesized the 128-mer of hydroxybutanoic acid and prepared a complex with inorganic calcium polyphosphate (average 65-mer), which was incorporated into a planar lipid bilayer of synthetic phospholipids. We herewith present data that demonstrate unambiguously that the completely synthetic complex forms channels that are indistinguishable in their voltage-dependent conductance, in their selectivity for divalent cations, and in their blocking behavior (by La3+) from channels isolated from Escherichia coli. The implications of our finding for prebiotic chemistry, biochemistry, and biology are discussed.

Beta-peptidic peptidomimetics

Acc Chem Res 2008 Oct;41(10):1366-75.18578513 10.1021/ar700263g

For more than a decade now, a search for answers to the following two questions has taken us on a new and exciting journey into the world of beta- and gamma-peptides: What happens if the oxygen atoms in a 3i-helix of a polymeric chain composed of (R)-3-Hydroxybutanoic acid are replaced by NH units? What happens if one or two CH2 groups are introduced into each amino acid building block in the chain of a peptide or protein, thereby providing homologues of the proteinogenic alpha-amino acids? Our journey has repeatedly thrown up surprises, continually expanding the potential of these classes of compound and deepening our understanding of the structures, properties, and multifaceted functions of the natural "models" to which they are related. Beta-peptides differ from their natural counterparts, the alpha-peptides, by having CH2 groups inserted into every amino acid residue, either between the C=O groups and the alpha-carbon atoms (beta(3)) or between the alpha-carbon and nitrogen atoms (beta(2)). The synthesis of these homologated proteinogenic amino acids and their assembly into beta-peptides can be performed using known methods. Despite the increased number of possible conformers, the beta-peptides form secondary structures (helices, turns, sheets) even when the chain lengths are as short as four residues. Furthermore, they are stable toward degrading and metabolizing enzymes in living organisms. Linear, helical, and hairpin-type structures of beta-peptides can now be designed in such a way that they resemble the characteristic and activity-related structural features ("epitopes") of corresponding natural peptides or protein sections. This Account presents examples of beta-peptidic compounds binding, as agonists or antagonists (inhibitors), to (i) major histocompatibility complex (MHC) proteins (immune response), (ii) the lipid-transport protein SR-B1 (cholesterol uptake from the small intestine), (iii) the core (1-60) of interleukin-8 (inflammation), (iv) the oncoprotein RDM2, (v) the HIVgp41 fusion protein, (vi) G-protein-coupled somatostatin hsst receptors, (vii) the TNF immune response receptor CD40 (apoptosis), and (viii) DNA. Short-chain beta-peptides may be orally bioavailable and excreted from the body of mammals; long-chain beta-peptides may require intravenous administration but will have longer half-lives of clearance. It has been said that an interesting field of research distinguishes itself in that the results always throw up new questions; in this sense, the structural and biological investigation of beta-peptides has been a gold mine. We expect that these peptidic peptidomimetics will play an increasing role in biomedical research and drug development in the near future.

Herstellung von ( S)-4-Methyloxetan-2-on( β-Butyrolacton) durch Lactonisierung von ( R)-3-Hydroxy-buttersäure mit Orthoessigsäure-triethylester

Chimia (Aarau) 2006 Jun 1;44(6):216-218.28340641

The readily available (R)-3-Hydroxybutanoic acid (1) was treated with triethyl orthoacetate, with azeotropic removal of ethanol, to yield (6R)-2-ethoxy-2,6-dimethyl-1,3-dioxan-4-one (3a). Pyrolysis of 3a led to the β-Lactone of (S)-3-hydroxybutanoic acid and other products. The influence of pressure, temperature, solvents, and some additives has been tested. A procedure for preparing (S)-4-methyloxetan-2-one (4) in a 0.25-mol scale is described.

A high-conductance mode of a poly-3-hydroxybutyrate/calcium/polyphosphate channel isolated from competent Escherichia coli cells

FEBS Lett 2005 Sep 26;579(23):5187-92.16150446 10.1016/j.febslet.2005.08.032

Reconstitution into planar lipid bilayers of a poly-3-hydroxybutyrate/calcium/polyphosphate (PHB/Ca(2+)/polyP) complex from Escherichia coli membranes yields cationic-selective, 100 pS channels (Das, S., Lengweiler, U.D., Seebach, D. and Reusch, R.N. (1997) Proof for a non-proteinaceous calcium-selective channel in Escherichia coli by total synthesis from (R)-3-Hydroxybutanoic acid and inorganic polyphosphate. Proc. Natl. Acad. Sci. USA 94, 9075-9079). Here, we report that this complex can also form larger, weakly selective pores, with a maximal conductance ranging from 250pS to 1nS in different experiments (symmetric 150mM KCl). Single channels were inhibited by lanthanum (IC(50)=42+/-4microM, means+/-S.E.M.) with an unusually high Hill coefficient (8.4+/-1.2). Transition to low-conductance states (<250pS) was favored by increased membrane polarization (/V/ >or=50mV). High conductance states (>250pS) may reflect conformations important for genetic transformability, or "competence", of the bacterial cells, which requires the presence of the PHB/Ca(2+)/polyP complex in the membrane.

Rhizobium leguminosarum bv. viciae produces a novel cyclic trihydroxamate siderophore, vicibactin

Microbiology (Reading) 1998 Mar;144(3):781-791.33757232 10.1099/00221287-144-3-781

Trihydroxamate siderophores were isolated from iron-deficient cultures of three strains of Rhizobium leguminosarum biovar viciae, two from Japan (WSM709, WSM710) and one from the Mediterranean (WU235), and from a Tn5-induced mutant of WSM710 (MNF7101). The first three all produced the same compound (vicibactin), which was uncharged and could be purified by solvent extraction into benzyl alcohol. The gallium and ferric complexes of vicibactin were extractable into benzyl alcohol at pH 5.0, while metal-free vicibactin could be extracted with good yield at pH 8.0. The trihydroxamate from MNF7101 (vicibactin 7101) could not be extracted into benzyl alcohol, but its cationic nature permitted purification by chromatography on Sephadex CM-25 (NH+ 4 form). Relative molecular masses and empirical formulae were obtained from fast-atom-bombardment MS. The structures were derived from one- and two-dimensional 1H and 13C NMR spectroscopy, using DQF-COSY, NOESY, HMQC and HMBC techniques on the compounds dissolved in methanol-d 4 and DMSO-d 6. Vicibactin proves to be a cyclic molecule containing three residues each of (R)-2,5-diamino-N 2-acetyl-N 5-hydroxypentanoic acid (N 2-acetyl-N 5-hydroxy-D-ornithine) and (R)-3-Hydroxybutanoic acid, arranged alternately, with alternating ester and peptide bonds. Vicibactin 7101 differed only in lacking the acetyl substitution on the N2 of the N 5-hydroxyornithine, resulting in net positive charge; it was still functional as a siderophore and promoted 55Fe uptake by iron-starved cells of WSM710 in the presence of an excess of phosphate. The rate of vicibactin biosynthesis by iron-deficient cells of WSM710 was essentially constant between pH 5.5 and 7.0, but much decreased at pH 5.0. When iron-starved cultures were supplemented with potential precursors for vicibactin, the rates of its synthesis were consistent with both β-hydroxybutyrate and ornithine being precursors. At least three genes seem likely to be involved in synthesis of vicibactin from ornithine and β-hydroxybutyrate: a hydroxylase adding the -OH group to the N5 of ornithine, an acetylase adding the acetyl group to the N2 of ornithine, and a peptide synthetase system.