4877-23-0

Upstream product

• 4582-71-2 benzoyl-DL-serine 
• 56-45-1 L-serin 
• 98-88-4 benzoyl chloride 
• 6756-74-7 S-benzoyl coenzyme A 
• 302-84-1 serin 
• 1102900-87-7 N-(p-methylbenzoyl)-L-serine 
• 99-94-5 p-Toluic acid 
• 100-44-7 benzyl chloride 
• 138739-05-6 2-benzoylamino-3-hydroxypropionic acid benzyl ester 
• 65-85-0 benzoic acid 
• 10144-46-4 N-benzoyl-L-serine methyl ester 
• 50-00-0 formaldehyd 
• 1199-01-5 2-phenylazlactone 
• 70326-37-3 phenyl(2-thioxothiazolidin-3-yl)methanone 

Downstream Products

• 75624-34-9 O-benzyl-α-N-benzoyl-L-serine hydroxamate 
• 99184-99-3 (4S)-2-phenyl-4,5-dihydrooxazole-4-carboxylic acid 
• 10144-46-4 N-benzoyl-L-serine methyl ester 
• 24153-31-9 2-benzoylaminoacrylic acid methyl ester 
• 138739-05-6 2-benzoylamino-3-hydroxypropionic acid benzyl ester 
• 1522124-79-3 (S)-N-(3-hydroxy-1-((4-methoxyphenethyl)amino)-1-oxopropan-2-yl)benzamide 
• 1522125-05-8 C₃₃H₃₆N₂O₁₀P₂*C₆H₁₅N 
• 1522124-83-9 (S)-2-benzamido-3-((4-methoxyphenethyl)amino)-3-oxopropyl dihydrogen phosphate 
• 1522124-82-8 (S)-2-benzamido-3-((4-methoxyphenethyl)amino)-3-oxopropyl dibenzyl phosphate 
• 75624-40-7 2-Phenyl-4,5-dihydro-oxazole-4-carboxylic acid benzyloxy-amide 
• 75624-39-4 1-(benzyloxy)-3-benzamido-2-azetidinone 

Relevant academic research and scientific papers

Switching Lysophosphatidylserine G Protein-Coupled Receptor Agonists to Antagonists by Acylation of the Hydrophilic Serine Amine

Three human G protein-coupled receptors (GPCRs)—GPR34/LPS1, P2Y10/LPS2, and GPR174/LPS3—are activated specifically by lysophosphatidylserine (LysoPS), an endogenous hydrolysis product of a cell membrane component, phosphatidylserine (PS). LysoPS consists of-serine, glycerol, and fatty acid moieties connected by phosphodiester and ester linkages. We previously generated potent and selective GPCR agonists by modification of the three modules and the ester linkage. Here, we show that a novel modification of the hydrophilic serine moiety, that is, N-acylations of the serine amine, converted a GPR174 agonist to potent GPR174 antagonists. Structural exploration of the amide functionality provided access to a range of activities from agonist to partial agonist to antagonist. The present study would provide a new strategy for the development of lysophospholipid receptor antagonists.

GRANZYME B DIRECTED IMAGING AND THERAPY

Provided herein are heterocyclic compounds useful for imaging Granzyme B. Methods of imaging Granzyme B, combination therapies, and kits comprising the Granzyme B imaging agents are also provided.

NEW DIFLUOROKETAMIDE DERIVATIVES AS HTRA1 INHIBITORS

The invention provides novel compounds having the general formula (I) wherein wherein R1, R2, R3, R4, R5, R6, R7, R3, R8, R9, R10, R11, R12 and R23 are as described herein, compositions including the compounds and methods of using the compounds.

Synthesis method of ramipril key intermediate

The invention discloses a synthesis method of a ramipril key intermediate. The ramipril key intermediate is 2-azabicyalo [3.3.0] octane-3-carboxylic acid hydrochloride. The 2-azabicyalo [3.3.0] octane-3-carboxylic acid hydrochloride is obtained through sequential dehydration cyclization, formaldehyde condensation, hydrolysis, removal, Michael addition, cyclization and palladium-carbon catalytic hydrogenation reduction of N-benzoyl-glycine as a raw material. According to the synthesis method of the ramipril key intermediate, the required raw material and reagent are cheap and available, the yield is relatively high, the operation is simple, the cost is low and the method is suitable for industrial production.

Chemical pyrophosphorylation of functionally diverse peptides

A highly selective and convenient method for the synthesis of pyrophosphopeptides in solution is reported. The remarkable compatibility with functional groups (alcohol, thiol, amine, carboxylic acid) in the peptide substrates suggests that the intrinsic nucleophilicity of the phosphoserine residue is much higher than previously appreciated. Because the methodology operates in polar solvents, including water, a broad range of pyrophosphopeptides can be accessed. We envision these peptides will find widespread applications in the development of mass spectrometry and antibody-based detection methods for pyrophosphoproteins.

A "catch-and-release" protocol for alkyne-tagged molecules based on a resin-bound cobalt complex for peptide enrichment in aqueous media

The development of new and mild protocols for the specific enrichment of biomolecules is of significant interest from the perspective of chemical biology. A cobalt-phosphine complex immobilised on a solid-phase resin has been found to selectively bind to a propargyl carbamate tag, that is, "catch", under dilute aqueous conditions (pH 7) at 4-°C. Upon acidic treatment of the resulting resin-bound alkyne-cobalt complex, the Nicholas reaction was induced to "release" the alkyne-tagged molecule from the resin as a free amine. Model studies revealed that selective enrichment of the alkyne-tagged molecule could be achieved with high efficiency at 4-°C. The proof-of-concept was applied to an alkyne-tagged amino acid and dipeptide. Studies using an alkyne-tagged dipeptide proved that this protocol is compatible with various amino acids bearing a range of functionalities in the side-chain. In addition, selective enrichment and detection of an amine derived from the "catch and release" of an alkyne-tagged dipeptide in the presence of various peptides has been accomplished under highly dilute conditions, as determined by mass spectrometry. Catch and release: The specific enrichment of alkyne-tagged molecules has been achieved by using cobalt beads. A cobalt complex bound to a resin was found to selectively "catch" a propargyl carbamate tag under dilute aqueous conditions (see scheme). Upon acidic treatment of the alkyne-cobalt complex, the Nicholas reaction was induced to "release" an amine. Studies using an alkyne-tagged dipeptide proved its compatibility with various amino acids and peptides under highly dilute conditions.

In vivo neurochemical monitoring using benzoyl chloride derivatization and liquid chromatography-mass spectrometry

In vivo neurochemical monitoring using microdialysis sampling is important in neuroscience because it allows correlation of neurotransmission with behavior, disease state, and drug concentrations in the intact brain. A significant limitation of current practice is that different assays are utilized for measuring each class of neurotransmitter. We present a high performance liquid chromatography (HPLC)-tandem mass spectrometry method that utilizes benzoyl chloride for determination of the most common low molecular weight neurotransmitters and metabolites. In this method, 17 analytes were separated in 8 min. The limit of detection was 0.03-0.2 nM for monoamine neurotransmitters, 0.05-11 nM for monoamine metabolites, 2-250 nM for amino acids, 0.5 nM for acetylcholine, 2 nM for histamine, and 25 nM for adenosine at sample volume of 5 μL. Relative standard deviation for repeated analysis at concentrations expected in vivo averaged 7% (n = 3). Commercially available 13C benzoyl chloride was used to generate isotope-labeled internal standards for improved quantification. To demonstrate utility of the method for study of small brain regions, the GABAA receptor antagonist bicuculline (50 μM) was infused into a rat ventral tegmental area while recording neurotransmitter concentration locally and in nucleus accumbens, revealing complex GABAergic control over mesolimbic processes. To demonstrate high temporal resolution monitoring, samples were collected every 60 s while neostigmine, an acetylcholine esterase inhibitor, was infused into the medial prefrontal cortex. This experiment revealed selective positive control of acetylcholine over cortical glutamate.

PREVENTING OR AMELIORATING AGENT FOR PIGMENTATION

An object is to provide an external preparation for skin preferably usable to prevent or ameliorate pigmentation. The object is achieved by providing a preventing or ameliorating agent for pigmentation, consisting of a compound represented by the following general formula (1), an isomer thereof, and/or a pharmacologically acceptable salt thereof, and an external preparation for skin containing the same as a component: [wherein R1 represents an unsubstituted aromatic group or an aromatic group having any substituent; R2 represents a hydrogen atom, a linear chain or branched chain alkyl group having a number of carbon atom or atoms of 1 to 4, or an acyl group having a linear or branched alkyl chain having a number of carbon atom or atoms of 1 to 4; and R3 represents a hydrogen atom or a linear chain or branched chain alkyl group having a number of carbon atom or atoms of 1 to 4.]

The utilization of alanine, glutamic acid, and serine as amino acid substrates for glycine N-acyltransferase.

The conjugation of benzoyl-CoA with the aliphatic and acidic amino acids by glycine N-acyltransferase, as well as the amides of the latter group, was investigated. Bovine and human liver benzoyl-amino acid conjugation were investigated using electrospray ionization tandem mass spectrometry (ESI-MS-MS). Bovine glycine N-acyltransferase catalyzed conjugation of benzoyl-CoA with Gly (Km(Gly) = 6.2 mM), Asn (Km(Asn) = 129 mM), Gln (Km(Gln) = 353 mM), Ala (Km(Ala) = 1573 mM), Glu (Km(Glu) = 1148 mM) as well as Ser in a sequential mechanism. In the case of the human form, conjugation with Gly (Km(Gly) = 6.4 mM), Ala (Km(Ala) = 997 mM), and Glu was detected. The presence of these alternative conjugates did not inhibit bovine glycine N-acyltransferase activity significantly. Considering the relatively low levels at which these conjugates are formed, it is unlikely that they will have a significant contribution to acyl-amino acid conjugation under normal conditions in vivo. However, their cumulative contribution to acyl-amino acid conjugation under metabolic disease states may prove to have a useful contribution to detoxification of elevated acyl-CoAs.

Peptide-bond Formation, Chemoselective Acylation of Amino Acids, and Crosslinking Reaction between Amino Acids Utilizing a Functional Five-membered Heterocycle, 1,3-Thiazolidine-2-thione

The monitored aminolysis of 3-acyl-1,3-thiazolidine-2-thiones has been extended to the peptide-bond formation, the chemoselective acylation of amino acids having multifunctional groups, and the crosslinking reaction between amino acids.