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Application Area

Benzoyl-D-alanine

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category

D-Amino Acids

Catalog number

BAT-003470

CAS number

17966-60-8

Molecular Formula

C10H11NO3

Molecular Weight

193.20

IUPAC Name

(2R)-2-benzamidopropanoic acid

Synonyms

Bz-D-Ala-OH

Appearance

Off-white to light yellow solid

Purity

≥ 98% (HPLC)

Density

1.224 g/cm3

Melting Point

128-134 °C

Boiling Point

452.3°C at 760 mmHg

Storage

Store at 2-8 °C

InChI

InChI=1S/C10H11NO3/c1-7(10(13)14)11-9(12)8-5-3-2-4-6-8/h2-7H,1H3,(H,11,12)(H,13,14)/t7-/m1/s1

InChI Key

UAQVHNZEONHPQG-SSDOTTSWSA-N

Canonical SMILES

CC(C(=O)O)NC(=O)C1=CC=CC=C1

Benzoyl-D-alanine, a versatile chiral compound with multifaceted applications in bioscience and industry, finds itself at the intersection of scientific exploration and innovation. Here are the key applications of Benzoyl-D-alanine, presented with a high degree of perplexity and burstiness:

Enzyme Inhibition Studies: Delving into the intricate world of enzymatic studies, Benzoyl-D-alanine emerges as a pivotal substrate or inhibitor, shedding light on enzyme specificity and activity. Scientists harness this compound to unravel the mechanisms of specific enzymes within metabolic pathways, paving the way for targeted enzyme inhibitors with therapeutic potential. Through this exploration, a deeper understanding of enzymatic processes is achieved, propelling advancements in biomedicine.

Peptide Synthesis: Within the realm of peptide synthesis, Benzoyl-D-alanine takes center stage as a foundational building block for crafting bespoke peptides. Its integration into peptide chains imparts specific characteristics, such as enhanced stability and proteolytic resistance. This strategic utilization is essential for shaping peptides with diverse therapeutic applications and for driving forward research endeavors aimed at unlocking the potential of peptide-based interventions.

Chiral Resolution: Serving as a linchpin in chiral resolution endeavors, Benzoyl-D-alanine facilitates the separation of enantiomers of chiral compounds through its role as a resolving agent. This process of isolating pure enantiomers is paramount in pharmaceutical contexts, where the biological activities of enantiomeric drugs can vary significantly. By ensuring the purity of enantiomers, this application safeguards drug efficacy and safety, underscoring its critical importance in the pharmaceutical landscape.

Pharmacological Research: Positioned at the frontier of pharmacological inquiry, Benzoyl-D-alanine is a subject of intense scrutiny for its potential therapeutic properties and interactions with biological targets. Researchers delve into its bioactivity, pharmacokinetics, and pharmacodynamics, aiming to unearth novel drug candidates that could revolutionize disease treatment. Through unraveling the intricate dance of drug-receptor interactions, this compound holds the promise of illuminating new pathways towards addressing unmet medical needs and improving patient outcomes.

1. Acyltransferase activities of the high-molecular-mass essential penicillin-binding proteins

M Adam, C Damblon, M Jamin, W Zorzi, V Dusart, M Galleni, A el Kharroubi, G Piras, B G Spratt, W Keck Biochem J. 1991 Oct 15;279 ( Pt 2)(Pt 2):601-4. doi: 10.1042/bj2790601.

The high-molecular-mass penicillin-binding proteins (HMM-PBPs), present in the cytoplasmic membranes of all eubacteria, are involved in important physiological events such as cell elongation, septation or shape determination. Up to now it has, however, been very difficult or impossible to study the catalytic properties of the HMM-PBPs in vitro. With simple substrates, we could demonstrate that several of these proteins could catalyse the hydrolysis of some thioesters or the transfer of their acyl moiety on the amino group of a suitable acceptor nucleophile. Many of the acyl-donor substrates were hippuric acid or benzoyl-D-alanine derivatives, and their spectroscopic properties enabled a direct monitoring of the enzymic reaction. In their presence, the binding of radioactive penicillin to the PBPs was also inhibited.

2. Trapping of an acyl-enzyme intermediate in a penicillin-binding protein (PBP)-catalyzed reaction

Pauline Macheboeuf, David Lemaire, Nathalie Teller, Alexandre Dos Santos Martins, André Luxen, Otto Dideberg, Marc Jamin, Andréa Dessen J Mol Biol. 2008 Feb 15;376(2):405-13. doi: 10.1016/j.jmb.2007.10.066. Epub 2007 Nov 1.

Class A penicillin-binding proteins (PBPs) catalyze the last two steps in the biosynthesis of peptidoglycan, a key component of the bacterial cell wall. Both reactions, glycosyl transfer (polymerization of glycan chains) and transpeptidation (cross-linking of stem peptides), are essential for peptidoglycan stability and for the cell division process, but remain poorly understood. The PBP-catalyzed transpeptidation reaction is the target of beta-lactam antibiotics, but their vast employment worldwide has prompted the appearance of highly resistant strains, thus requiring concerted efforts towards an understanding of the transpeptidation reaction with the goal of developing better antibacterials. This goal, however, has been elusive, since PBP substrates are rapidly deacylated. In this work, we provide a structural snapshot of a "trapped" covalent intermediate of the reaction between a class A PBP with a pseudo-substrate, N-benzoyl-D-alanylmercaptoacetic acid thioester, which partly mimics the stem peptides contained within the natural, membrane-associated substrate, lipid II. The structure reveals that the D-alanyl moiety of the covalent intermediate (N-benzoyl-d-alanine) is stabilized in the cleft by a network of hydrogen bonds that place the carbonyl group in close proximity to the oxyanion hole, thus mimicking the spatial arrangement of beta-lactam antibiotics within the PBP active site. This arrangement allows the target bond to be in optimal position for attack by the acceptor peptide and is similar to the structural disposition of beta-lactam antibiotics with PBP clefts. This information yields a better understanding of PBP catalysis and could provide key insights into the design of novel PBP inhibitors.