116783-26-7

Usage

Uses

Used in Pharmaceutical Synthesis:
S-2-Aminooctanoic acid is utilized as a key component in the synthesis of pharmaceuticals, leveraging its unique structural properties to contribute to the development of new medications.
Used as a Chiral Building Block:
In the production of chiral drugs, S-2-Aminooctanoic acid serves as a chiral building block, which is essential for the creation of enantiomerically pure compounds, a critical aspect in drug efficacy and safety.
Used in the Development of Biodegradable Polymers:
S-2-Aminooctanoic acid is employed in the development of biodegradable polymers, which are environmentally friendly materials that have applications in various industries, including packaging and medical devices.
Used as a Precursor for Specialty Chemicals:
This amino acid also functions as a precursor for the production of specialty chemicals, indicating its versatility and importance in the chemical industry.
Used in Neurological Disorder Treatment:
S-2-Aminooctanoic acid may have potential therapeutic applications in the treatment of neurological disorders, suggesting its possible role in medicine for addressing specific health conditions.
Used as a Neuroprotective Agent:
Furthermore, it has potential as a neuroprotective agent, indicating its use in safeguarding the nervous system from damage or degeneration, which could be significant in the field of neurology and neurodegenerative disease research and treatment.

Upstream product

• 90977-20-1 N-Dichloracetyl-DL-2-amino-octansaeure 
• 638-45-9 1-Iodohexane 
• 56-40-6 glycine 
• 119817-31-1 (2S)-2-{[(benzyloxy)carbonyl]amino}octanoic acid 
• 328-51-8 2-oxooctanoic acid 
• 106749-00-2 (S)-2-Chloro-octanoic acid (1S,2R,4R)-1-[(dicyclohexylsulfamoyl)-methyl]-7,7-dimethyl-bicyclo[2.2.1]hept-2-yl ester 
• 2627-86-3 (S)-1-phenyl-ethylamine 
• 617-73-2 2-hydroxy-octanoic acid 
• 124-07-2 Octanoic acid 
• 644-90-6 2-aminooctanoic acid 
• 106749-07-9 (R)-2-Azido-octanoic acid (1S,2R,4R)-1-[(dicyclohexylsulfamoyl)-methyl]-7,7-dimethyl-bicyclo[2.2.1]hept-2-yl ester 
• 628-17-1 amyl iodide 
• 834898-09-8 (2S,4S)-2-(1,1-dimethylethyl)-4-hexyl-5-oxo-3-oxazolidinecarboxylic acid phenylmethyl ester 
• 6294-94-6 2-benzoylamino-octanoic acid 

Downstream Products

• 1339952-65-6 (S)-2-(3-((S)-1-carboxyheptyl)ureido)-6-(4-iodobenzamido)hexanoic acid 

Relevant academic research and scientific papers

Biocatalytic asymmetric synthesis of unnatural amino acids through the cascade transfer of amino groups from primary amines onto keto acids

Flee to the hills: An unfavorable equilibrium in the amino group transfer between amino acids and keto acids catalyzed by α-transaminases was successfully overcome by coupling with a ω-transaminase reaction as an equilibrium shifter, leading to efficient asymmetric synthesis of diverse unnatural amino acids, including L-tert-leucine and D-phenylglycine. Copyright

Semi-rational hinge engineering: modulating the conformational transformation of glutamate dehydrogenase for enhanced reductive amination activity towards non-natural substrates

The active site is the common hotspot for rational and semi-rational enzyme activity engineering. However, the active site represents only a small portion of the whole enzyme. Identifying more hotspots other than the active site for enzyme activity engineering should aid in the development of biocatalysts with better catalytic performance. Glutamate dehydrogenases (GluDHs) are promising and environmentally benign biocatalysts for the synthesis of valuable chirall-amino acids by asymmetric reductive amination of α-keto acids. GluDHs contain an inter-domain hinge structure that facilitates dynamic reorientations of the domains relative to each other. Such hinge-bending conformational motions of GluDHs play an important role in regulating the catalytic activity. Thus, the hinge region represents a potential hotspot for catalytic activity engineering for GluDHs. Herein, we report semi-rational activity engineering of GluDHs with the hinge region as the hotspot. Mutants exhibiting significantly improved catalytic activity toward several non-natural substrates were identified and the highest activity increase reached 104-fold. Molecular dynamics simulations revealed that enhanced catalytic activity may arise from improving the open/closed conformational transformation efficiency of the protein with hinge engineering. In the batch production of three valuablel-amino acids, the mutants exhibited significantly improved catalytic efficiency, highlighting their industrial potential. Moreover, the catalytic activity of several active site tailored GluDHs was also increased by hinge engineering, indicating that hinge and active site engineering are compatible. The results show that the hinge region is a promising hotspot for activity engineering of GluDHs and provides a potent alternative for developing high-performance biocatalysts toward chirall-amino acid production.

Combinatorial Mutation Analysis of ω-Transaminase to Create an Engineered Variant Capable of Asymmetric Amination of Isobutyrophenone

ω-Transaminase (ω-TA) is an important enzyme for asymmetric synthesis of chiral amines. Rapid creation of a desirable ω-TA variant, readily available for scalable process operation, is demanded and has attracted intense research efforts. In this study, we aimed to develop a quantitative mutational analysis (i. e., R-analysis) that enables prediction of combinatorial mutation outcomes and thereby provides reliable guidance of enzyme engineering through combination of already characterized mutations. To this end, we determined three mutatable active-site residues of ω-TA from Ochrobactrum anthropi (i. e., leucine 57, tryptophan 58 and valine 154) by examining activities of nine alanine-scanning mutants for seven substrate pairs. The R-analysis of the mutatable residues is based on assessment of changes in relative activities for a series of structurally analogous substrates. Using three sets of substrates (five α-keto acids, six arylalkylamines and three arylalkyl ketones), we found that combination of two point mutations display additive effects of each mutational outcome such as steric relaxation for bulky substrates or catalytic enhancement for amination of ketones. Consistent with the R-analysis-based prediction, the ω-TA variant harboring triple alanine mutations, i. e. L57A, W58A and V154A, showed high activity improvements for bulky substrates, e. g. a 3.2×104-fold activity increase for 1-phenylbutylamine. The triple mutant even enabled asymmetric amination of isobutyrophenone, carrying a branched-chain alkyl substituent to be accepted in a small binding pocket that normally shows a steric limit up to an ethyl group, with >99% ee of a resulting (S)-amine. (Figure presented.).

Preparative Asymmetric Synthesis of Canonical and Non-canonical a-amino Acids through Formal Enantioselective Biocatalytic Amination of Carboxylic Acids

Chemical and biocatalytic synthesis of non-canonical a-amino acids (ncAAs) from renewable feedstocks and using mild reaction conditions has not efficiently been solved. Here, we show the development of a three-step, scalable and modular one-pot biocascade for linear conversion of renewable fatty acids (FAs) into enantiopure l-a-amino acids. In module 1, selective a-hydroxylation of FAs is catalyzed by the P450 peroxygenase P450CLA. By using an automated H2O2 supplementation system, efficient conversion (46 to >99%; TTN>3300) of a broad range of FAs (C6:0 to C16:0) into valuable a-hydroxy acids (a-HAs; >90% a-selective) is shown on preparative scale (up to 2.3 gL1 isolated product). In module 2, a redox-neutral hydrogen borrowing cascade (alcohol dehydrogenase/amino acid dehydrogenase) allowed further conversion of a-HAs into l-a-AAs (20 to 99%). Enantiopure l-a-AAs (e.e. >99%) including the pharma synthon l-homo-phenylalanine can be obtained at product titers of up to 2.5 gL1. Based on renewables and excellent atom economy, this biocascade is among the shortest and greenest synthetic routes to structurally diverse and industrially relevant ncAAs.

Preparative Asymmetric Synthesis of Canonical and Non-canonical α-amino Acids Through Formal Enantioselective Biocatalytic Amination of Carboxylic Acids

Chemical and biocatalytic synthesis of non-canonical α-amino acids (ncAAs) from renewable feedstocks and using mild reaction conditions has not efficiently been solved. Here, we show the development of a three-step, scalable and modular one-pot biocascade for linear conversion of renewable fatty acids (FAs) into enantiopure l-α-amino acids. In module 1, selective α-hydroxylation of FAs is catalyzed by the P450 peroxygenase P450CLA. By using an automated H2O2 supplementation system, efficient conversion (46 to >99%; TTN>3300) of a broad range of FAs (C6:0 to C16:0) into valuable α-hydroxy acids (α-HAs; >90% α-selective) is shown on preparative scale (up to 2.3 g L?1 isolated product). In module 2, a redox-neutral hydrogen borrowing cascade (alcohol dehydrogenase/amino acid dehydrogenase) allowed further conversion of α-HAs into l-α-AAs (20 to 99%). Enantiopure l-α-AAs (e.e. >99%) including the pharma synthon l-homo-phenylalanine can be obtained at product titers of up to 2.5 g L?1. Based on renewables and excellent atom economy, this biocascade is among the shortest and greenest synthetic routes to structurally diverse and industrially relevant ncAAs. (Figure presented.).

Asymmetric Transamination of α-Keto Acids Catalyzed by Chiral Pyridoxamines

A new type of novel chiral pyridoxamines 3a-g containing a side chain has been developed. The pyridoxamines displayed catalytic activity and promising enantioselectivity in biomimetic asymmetric transamination of α-keto acids, to give various α-amino acids in 47-90% yields with up to 87% ee's under very mild conditions. An interesting effect of the side chain on enantioselectivity was observed in the reaction.

Synthesis and in vitro evaluation of a library of modified endomorphin 1 peptides

Endomorphin 1 (Endo-1 = Tyr-Pro-Trp-Phe-NH2), an endogenous opioid with high affinity and selectivity for μ-opioid receptors, mediates acute and neuropathic pain in rodents. To overcome metabolic instability and poor membrane permeability, the N- and C-termini of Endo-1 were modified by lipoamino acids (Laa) and/or sugars, and 2′,6′-dimethyltyrosine (Dmt) replacement of Tyr. Analogues were assessed for μ-opioid receptor affinity, inhibition of cAMP accumulation, enzymatic stability, and permeability across Caco-2 cell monolayers. C-Terminus modification decreased receptor affinity, while N-terminus C8-Laa improved stability and permeability with slight change in receptor affinity. Dmt provided a promising lead compound: [C8Laa-Dmt[1]]-Endo-1 is nine times more stable (t1/2 = 43.5 min), >8-fold more permeable in Caco-2 cell monolayers, and exhibits 140-fold greater μ-opioid receptor affinity (Kiμ = 0.08 nM).

Creation of a broad-range and highly stereoselective D-amino acid dehydrogenase for the one-step synthesis of D-amino acids

Using both rational and random mutagenesis, we have created the first known broad substrate range, nicotinamide cofactor dependent, and highly stereoselective D-amino acid dehydrogenase. This new enzyme is capable of producing D-amino acids via the reductive amination of the corresponding 2-keto acid with ammonia. This biocatalyst was the result of three rounds of mutagenesis and screening performed on the enzyme meso-diaminopimelate D-dehydrogenase. The first round targeted the active site of the wild-type enzyme and produced mutants that were no longer strictly dependent on the native substrate. The second and third rounds produced mutants that had an increased substrate range including straight-and branched-aliphatic amino acids and aromatic amino acids. The very high selectivity toward the D-enantiomer (95 to >99% ee) was shown to be preserved even after the addition of the five mutations found in the three rounds of mutagenesis and screening. This new enzyme could complement and improve upon current methods for D-amino acid synthesis.

Practical and efficient enantioselective synthesis of α-amino acids in aqueous media

Enantiomerically pure natural and unnatural α-amino acids have been synthesized from a chiral melhyleneoxazolidinone by means of a highly diastereoselective 1,4-conjugate addition of alkyl iodides in aqueous media. The zinc-copper conjugate addition reaction exhibits high chemoselectivity, with the possibility of using functionalized iodides, to afford a single diastereomer in short reaction times and with good yields.

Highly efficient catalytic synthesis of α-amino acids under phase-transfer conditions with a novel catalyst/substrate pair

A facile and fast enantioselective synthesis of α-amino acids with high ee values was achieved by the asymmetric alkylation of the glycine derivative 1 under phase-transfer conditions with (R)-2-amino-2′-hydrozy-1,1′-binaphthyl (NOBIN; see sceme). The ee value of the amino acid products. This occures as a results of a significant positive nonlinear effect in the alkylation reaction.