2503-31-3

Usage

Uses

Used in Pharmaceutical Industry:
Z-DL-ALA-GLY-OH is used as a building block for the development of new antibiotics, given its presence of D-alanine, which is an important component in the formation of the bacterial cell wall. This property may contribute to the creation of novel antimicrobial agents targeting specific bacterial structures.
Used in Biochemistry Research:
Z-DL-ALA-GLY-OH serves as a valuable compound for studying protein synthesis and the role of amino acids in various biological processes. Its unique structure, combining D-alanine and glycine, may provide insights into the mechanisms of protein folding, stability, and function.
Used in Molecular Biology Applications:
Z-DL-ALA-GLY-OH is utilized as a component in the design of peptide-based drugs and therapeutic agents. Z-DL-ALA-GLY-OH's ability to incorporate both D-alanine and glycine may offer advantages in the development of targeted therapies with enhanced specificity and efficacy.

Upstream product

• 2503-32-4 ethyl N-(benzyloxycarbonyl)-L-alanylglycinate 
• 4840-29-3 Z-L-Ala-Gly-OMe 
• 17126-93-1 Benzyloxycarbonyl-L-alaninphenylthiolester 
• 56-40-6 glycine 
• 5572-41-8 N-benzyloxycarbonyl-L-alanylaminoethanol 
• 56-41-7 L-alanin 
• 1168-87-2 benzyloxycarbonylalanine p-nitrophenyl ester 
• 76413-56-4 3-(N-benzyloxycarbonyl-L-alanyl)-1,3-thiazolidine-2-thione 
• 3401-36-3 (N-benzyloxycarbonyl)-L-alanine N-hydroxysuccinimide ester 
• 6233-97-2 Z-Ala-OPcp 
• 1142-20-7 N-Cbz-Ala 
• 501-53-1 benzyl chloroformate 
• 820239-42-7 benzyl N-[(1S)-2-(1H-1,2,3-benzotriazol-1-yl)-1-methyl-2-oxoethyl]carbamate 
• 64562-95-4 methyl N-benzyloxycarbonylalaninate 

Downstream Products

• 97615-49-1 S-benzyl-N-{N-[N-(N-benzyloxycarbonyl-L-alanyl)-glycyl]-L-valyl}-L-cysteine benzyl ester 
• 687-69-4 alanylglycine 
• 49705-73-9 Z-Ala-Gly-Boc Hydrazid 
• 66962-63-8 C₅₂H₆₄N₆O₁₅ 
• 112120-49-7 Z-(Ala-Gly)2-OMe 
• 112120-50-0 Z-(Ala-Gly)3-OMe 
• 156916-70-0 t-butyl N^α-benzyloxycarbonyl-L-alanylglycyl-L-(β-t-butoxy)aspartyl-L-valinate 
• 151990-28-2 Z-L-Ala-Gly-L-Glu(OtBu)-Ser(tBu)-OtBu 
• 128228-46-6 [(S)-1-(5-Oxo-4,5-dihydro-oxazol-2-yl)-ethyl]-carbamic acid benzyl ester 
• 36735-50-9 N-Benzoyloxycarbonyl-L-alanylglycinpentachlorophenylester 
• 17784-27-9 ((S)-2-Benzyloxycarbonylamino-propionylamino)-acetic acid 4-methylsulfanyl-phenyl ester 
• 277334-75-5 (S)-1-phenylallyl N-benzyloxycarbonyl-(S)-alanylglycinate 
• 277334-77-7 (S)-1-phenyl-1-penten-3-yl N-benzyloxycarbonyl-(S)-alanylglycinate 
• 511303-01-8 Z-Ala-Gly-Ala-OMe 

Relevant academic research and scientific papers

CROSS-LINKED PYRROLOBENZODIAZEPINE DIMER (PBD) DERIVATIVE AND ITS CONJUGATES

A novel cross-linked cytotoxic agents, pyrrolobenzo-diazepine dimer (PBD) derivatives, and their conjugates to a cell-binding molecule, a method for preparation of the conjugates and the therapeutic use of the conjugates.

CONJUGATION LINKERS CONTAINING 2,3-DIAMINOSUCCINYL GROUP

Provided is a conjugate of a cytotoxic drug/molecule to a cell-binding molecule with a bis-linker (adual-linker) containing a 2, 3-diaminosuccinyl group. It also relates to preparation of the conjugate of a cytotoxic drug/molecule to a cell-binding molecule with the bis-linker, particularly when the drug having functional groups of amino, hydroxyl, diamino, amino-hydroxyl, dihydroxyl, carboxyl, hydrazine, aldehyde and thiol for conjugation with the bis-linker in a specific manner, as well as the therapeutic use of the conjugates.

CONJUGATION OF A CYTOTOXIC DRUG WITH BIS-LINKAGE

What provided is the conjugation of cytotoxic to a cell-binding molecule with a bis-linker(dual-linker) as shown in Formula (I). It provides bis-linkage methods of making a conjugate of a cytotoxic drug molecule to a cell-binding agent in a specific manner. It also relates to application of the conjugates for the treatment of a cancer, or an autoimmune disease, or an infectious disease.

Engineered Substrate for Cyclooxygenase-2: A Pentapeptide Isoconformational to Arachidonic Acid for Managing Inflammation

Beyond the conventional mode of working of anti-inflammatory agents through enzyme inhibition, herein, COX-2 was provided with an alternate substrate. A proline-centered pentapeptide isoconformational to arachidonic acid, which exhibited appreciable selectivity for COX-2, overcoming acetic acid- and formalin-induced pain in rats to almost 80%, was treated as a substrate by the enzyme. Remarkably, COX-2 metabolized the pentapeptide into small fragments consisting mainly of di- and tripeptides that ensured the safe breakdown of the peptide under in vivo conditions. The kinetic parameter Kcat/Km for COX-2-mediated metabolism of the peptide (6.3 × 105 M-1 s-1) was quite similar to 9.5 × 105 M-1 s-1 for arachidonic acid. Evidenced by the molecular dynamic studies and the use of Y385F COX-2, it was observed that the breakage of the pentapeptide has probably been taken place through H-bond activation of the peptide bond by the side chains of Y385 and S530.

Synthesis of selenoxo peptides and oligoselenoxo peptides employing LiAlHSeH

Synthesis of selenoxo peptides by the treatment of Nα- protected peptide esters with a combination of PCl5 and LiAlHSeH is delineated. The method is simple, high-yielding, and free from racemization. Thus obtained selenoxo peptides are used as units for N-terminal chain extension through Nα-deprotection/coupling to yield peptide-selenoxo peptide hybrids. Multiple selenation is demonstrated by conversion of two peptide bonds of tripeptides into selenoxo peptide bonds. Amino acid derived arylamides are also converted into aryl selenoamides. C6H 5-CSeNH-Val-OMe 8f is obtained as single crystal, and its structure was determined through X-ray diffraction study.

Chemical ligation of S-scylated cysteine peptides to form native peptides via 5-, 11-, and 14-membered cyclic transition states

Cysteine-containing dipeptides 3a-l, (3b+3b′) (compound numbers in parentheses are used to indicate racemic mixtures; thus (3b+3b′) is the racemate of 3b and 3b′), and tripeptide 13 were synthesized in 68-96% yields by acylation of cysteine with N-(Pg-α-aminoacyl)- and N-(Pg-α-dipeptidoyl)benzotriazoles (where Pg stands for protecting group in the nomenclature for peptides throughout the paper) in the presence of Et3N. Cysteine-containing peptides 3a-l and 13 were S-acylated to give S-(Pg-α-aminoacyl)dipeptides 5a-l and S-(Pg-α-aminoacyl) tripeptide 14 without racemization in 47-90% yields using N-(Pg-α- aminoacyl)benzotriazoles 2 in CH3CN-H2O (7:3) in the presence of KHCO3. (In our peptide nomenclature, the prefixes di-, tri-, etc. refer to the number of amino acid residues in the main peptide chain; amino acid residues attached to sulfur are designated as S-acyl peptides. Thus we avoid use of the prefix "iso".) Selective S-acylations of serine peptide 3k and threonine peptide 3l containing free OH groups were thus achieved in 58% and 72% yield, respectively. S-(Pg-α-aminoacyl)cysteines 4a,b underwent native chemical ligations to form native dipeptides 3f,i via 5-membered cyclic transition states. Microwave irradiation of S-(Pg-α-aminoacyl)tripeptide 15 and S-(Pg-α-aminoacyl)tetrapeptide 17 in the presence of NaH2PO4/Na2HPO 4 buffer solution at pH 7.8 achieved chemical ligations, involving intramolecular migrations of acyl groups, via 11- and 14-membered cyclic transition states from the S-atom of a cysteine residue to a peptide terminal amino group to form native peptides 19 and 20 in isolated yields of 26% and 23%, respectively.

Total Synthesis of Thymosin β4, 3. Conventional Synthesis of the Fragment of Thymosin β4

As part of our total synthesis of thymosin β4, an optimized synthesis of the C-terminal part of thymosin β4 is described.Side chain functional residues of the tridecapeptide are masked by tert-butyl and the α-amino-acids residues are protected by the Z groups.The fully protected peptide derivative was obtained by WSCI/HOBt coupling of three fragments representing the segments , and . Key words: Thymosin β4; fragment ; peptide; solution synthesis; thymosins.

Active esters used for production of esters or amides and process for producing esters or amides

This invention is characterized by synthesizing an active ester represented by the general formula STR1 using an active esterifying agent consisting of a sulfonium salt represented by the general formula STR2 and further reacting the above-said active ester with a nucleophilic agent represented by the general formula H--B--Y to produce an ester or amide represented by the general formula (W)d.A--B--Y.

Amino alcohols as C-Terminal Protecting Groups in Peptide Synthesis

The synthesis of peptides using amino alcohols as C-terminal protecting groups is described.C-Terminal protection of amino acid could be accomplished by reduction of the terminal carboxyl group to a hydroxymethyl group, and regeneration of the carboxyl group could be achieved by Jones' oxidation.This method was applied to the formation of di- and tripeptides.