42491-84-9

Usage

Uses

Used in Pharmaceutical Synthesis:
(S)-6-Amino-2-hydroxyhexanoic acid is used as a building block for the development of new pharmaceutical compounds. Its unique structure allows for the creation of novel drugs with potential therapeutic applications in various medical fields.
Used in Food Additives Industry:
(S)-6-Amino-2-hydroxyhexanoic acid is used as an additive in the food industry, where it can enhance the taste, texture, or nutritional value of certain products. Its role in the urea cycle also suggests potential benefits for human health when consumed as part of the diet.
Used in Biochemistry and Molecular Biology Research:
(S)-6-Amino-2-hydroxyhexanoic acid serves as a valuable research tool in the fields of biochemistry and molecular biology. Its unique properties and involvement in the urea cycle make it an important molecule for studying various biological processes and pathways, contributing to a deeper understanding of cellular functions and the development of new therapeutic strategies.

Upstream product

• 56-87-1 L-lysine 
• 59221-35-1 (S)-6-[[(Phenylmethoxy)carbonyl]amino]-2-hydroxyhexanoic acid 
• 657-27-2 L-Lysine hydrochloride 
• 1155-64-2 N₆-[(benzyloxy)carbonyl]-L-lysine 

Downstream Products

• 59221-35-1 (S)-6-[[(Phenylmethoxy)carbonyl]amino]-2-hydroxyhexanoic acid 
• 126187-75-5 Lithium; (2S,4S)-1-{(S)-6-amino-2-[hydroxy-(4-phenyl-butyl)-phosphinoyloxy]-hexanoyl}-4-phenylsulfanyl-pyrrolidine-2-carboxylate 
• 107504-50-7 (S)-2-<oxy>-6-<(trifluoroacetyl)amino>hexanoic acid 
• 126110-84-7 (2S,4R)-1-[(S)-2-[Hydroxy-(4-phenyl-butyl)-phosphinoyloxy]-6-(2,2,2-trifluoro-acetylamino)-hexanoyl]-4-methylsulfanyl-pyrrolidine-2-carboxylic acid methyl ester 
• 126110-84-7 (2S,4S)-1-[(S)-2-[Hydroxy-(4-phenyl-butyl)-phosphinoyloxy]-6-(2,2,2-trifluoro-acetylamino)-hexanoyl]-4-methylsulfanyl-pyrrolidine-2-carboxylic acid methyl ester 
• 60369-22-4 (S)-2-Hydroxy-6-tosylamido-hexansaeuremethylester 
• 111496-31-2 1-<(S)-2-<<(phenylmethoxy)(2-phenethyl)phosphinyl>oxy>-1-oxo-6-<<(phenylmethoxy)carbonyl>amino>hexyl>-L-proline phenylmethyl ester 
• 111496-58-3 (S)-1-((S)-6-Benzyloxycarbonylamino-2-{[4-(4-fluoro-phenyl)-butyl]-hydroxy-phosphinoyloxy}-hexanoyl)-pyrrolidine-2-carboxylic acid benzyl ester 
• 111497-23-5 (S)-1-[(S)-6-Benzyloxycarbonylamino-2-(4-pyridin-3-yl-butylphosphinoyloxy)-hexanoyl]-pyrrolidine-2-carboxylic acid benzyl ester 
• 111496-60-7 1-<(S)-2-<phosphinyl>oxy>-1-oxo-6-<<(phenylmethoxy)carbonyl>amino>hexyl>-L-proline phenylmethyl ester 
• 111496-56-1 (S)-1-{(S)-6-Benzyloxycarbonylamino-2-[hydroxy-(5-phenyl-pentyl)-phosphinoyloxy]-hexanoyl}-pyrrolidine-2-carboxylic acid benzyl ester 
• 111497-22-4 (S)-1-[(S)-6-Benzyloxycarbonylamino-2-(4-phenyl-butylphosphinoyloxy)-hexanoyl]-pyrrolidine-2-carboxylic acid benzyl ester 
• 111496-52-7 (S)-1-{(S)-6-Benzyloxycarbonylamino-2-[hydroxy-(3-phenyl-propyl)-phosphinoyloxy]-hexanoyl}-pyrrolidine-2-carboxylic acid benzyl ester 
• 111496-71-0 (S)-1-[(S)-6-Benzyloxycarbonylamino-2-(decyl-hydroxy-phosphinoyloxy)-hexanoyl]-pyrrolidine-2-carboxylic acid benzyl ester 

Relevant academic research and scientific papers

Synthesis of four lysine-linked cereulide analogues showing ionophoric activity towards potassium cations as lead compounds for emetic toxin-detection by immunoassays

An improved total synthesis of the emetic toxin cereulide and the preparation of four lysine-linked cereulide analogues is described. The cereulide analogues are prepared by replacing one of the amino acid residues in cereulide with lysine. The cereulide analogues demonstrate ionophoric activity towards alkali metal ions and inorganic ammonium ions, and are currently being used to develop an enzyme-linked immunosorbent assay for cereulide. Georg Thieme Verlag Stuttgart.

Simultaneous and site-directed incorporation of an ester linkage and an azide group into a polypeptide by in vitro translation

A method is presented by which an azide-containing side chain can be introduced into any internal position of a polypeptide chain by in vitro translation. For this, 2′-deoxy-cytidylyl-(3′→5′)- adenosine was acylated on the 3′(2′)-hydroxyl group of adenosine with 6-azido-2(S)-hydroxyhexanoic acid (AHHA), an α-hydroxy- and ε-azide derivative of l-lysine. The acylated dinucleotide was enzymatically ligated with a tRNA transcript to provide chemically stable E. coli suppressor AHHA-tRNACys(CUA). The esterase 2 gene from Alicyclobacillus acidocaldarius was modified by the amber stop codon (UAG) on position 118. Using AHHA-tRNACys(CUA) in an E. coli in vitro translation/transcription system, the site-directed introduction of an azide group linked to a backbone ester into the esterase polypeptide was achieved. The yield of the synthesized modified protein reached 80% compared to translation of the native esterase. Subsequently, azide coupling with an alkyne-modified oligodeoxynucleotide demonstrated the feasibility of this approach for conjugation of polypeptides.

POLYBIOTIN COMPOUNDS FOR MAGNETIC RESONANCE IMAGINING AND DRUG DELIVERY

The invention relates generally to biotin-containing compounds that are useful as imaging agents and drug-delivery agents. Another aspect of the invention relates to the aforementioned compounds chelated to a metal atom. In a preferred embodiment, the metal atom is a gadolinium. Another aspect of the invention relates to a compound comprising three biotin moieties and a pharmaceutical agent covalently bound to a heterocyclic core. In certain embodiments, the pharmaceutical agent is an antibiotic, antiviral, or radionuclide. Another aspect of the present invention relates to a method of treating disease involving administering the compounds of the invention to a mammal. Another aspect of the present invention relates to a method of acquiring a magnetic resonance image using the compounds of the invention.

Linker nucleoside, and production and use of the same

The present invention relates to a linker nucleoside, its preparation and use for the covalent bonding of biomolecules to oligonucleotides, in particular p-RNA oligonucleotides.

Reactivite du nitrite de sodium. V. Action sur les amino-acides, peptides et proteines

The action of sodium nitrite on various amino-acids was re-examined in conditions approximating to a biological medium. 13C-NMR provides evidence of the existence of intramolecular ring closures and the formation of 5-membered rings with ornithine, citrulline and arginine.The reaction of cystine shows the opening of the sulphur bridges, whereas cysteine leads to the formation of carboxy-thiiran and 3-sulpho-lactic acid.The hydrolysis of the amide bonds of asparagine and glutamine is complete whereas the peptides studied - carnosine and aspartam - do not undergo hydrolysis of the peptide linkage.However, the first deamination of glutathion (γ-Glu-Cys-Gly) induces the peptide link to be broken and a cyclization with the formation of lactone to occur.A second deamination takes place on the cysteinyl residue released and allows the formation of a thiiran by intramolecular cyclization with the thiol group.The formation of thiiran was also observed with oxidized glutathion which has an S-S bridge.Finally, the formation of nitrosamines was detected by 15N-NMR during the reaction of sodium nitrite with two commercial products available to the general public.

ORALLY ACTIVE PHOSPHONYL HYDROXYACYL PROLINES

This invention is directed to orally active antihypertensive agents of the formula STR1 wherein R 1 is certain alkyl or aralkyl groups.

A-acylamino aminoalkyl phophonate angiotensin converting enzyme inhibitors

Compounds of the formula wherein X is various amino or imino acids and esters are disclosed. These compounds are useful as anti-hypertensive agents due to their angiotensin converting enzyme inhibition activity and depending upon the definition of X may a

(Phosphinyloxy)acyl amino acid inhibitors of angiotensin converting enzyme (ACE). 1. Discovery of (S)-1-[6-amino-2-[[hydroxy(4-phenylbutyl)phosphinyl]oxy]-1-oxohexyl]- -proline, a novel orally active inhibitor of ACE

The synthesis of a series of orally active, phosphinyloxyacyl proline inhibitors of angiotensin converting enzyme (ACE) is described. The in vitro and in vivo ACE inhibitory activities are reported for each compound. The structure-activity relationship fo