5845-58-9

Upstream product

• 24959-68-0 N-Cbz-L-Ala-L-Leu 
• 1001249-92-8 C₂F₆NO₄S₂^(1-)*C₃₃H₄₈N₃O₅⁽¹⁺⁾ 
• 905984-90-9 C₂F₆NO₄S₂^(1-)*C₃₈H₅₀N₃O₆⁽¹⁺⁾ 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 15761-38-3 L-N-Boc-Ala 
• 59515-79-6 ((S)-2-aminopropanoyl)-L-leucine methyl ester hydrochloride 
• 95083-32-2 (S)-methyl 2-((S)-2-((tert-butoxycarbonyl)amino)propanamido)-4-methylpentanoate 
• 7517-19-3 methyl (L)-leucinate hydrochloride 
• 4864-39-5 N-carbobenzoxy-L-alanyl-L-leucine methyl ester 
• 5845-57-8 L-alanyl-L-leucine methyl ester 
• 7298-84-2 Leu-Ala 

Downstream Products

• 17498-50-9 L-valine hydrochloride 
• 6003-05-0 L-alanine hydrochloride 

Relevant academic research and scientific papers

Anti-biofilm and anti-adherence properties of novel cyclic dipeptides against oral pathogens

Microorganisms embedded in a biofilm are significantly more resistant to antimicrobial agents and the defences of the human immune system, than their planktonic counterpart. Consequently, compounds that can inhibit biofilm formation are of great interest for novel therapeutics. In this study, a screening approach was used to identify novel cyclic dipeptides that have anti-biofilm activity against oral pathogens. Five new active compounds were identified that prevent biofilm formation by the cariogenic bacterium Streptococcus mutans and the pathogenic fungus Candida albicans. These compounds also inhibit the adherence of microorganisms to a hydroxylapatite surface. Further investigations were conducted on these compounds to establish the structure–activity relationship, and it was deduced that the common cleft pattern is required for these molecules to act effectively against biofilms.

Interfacial supramolecular biomimetic epoxidation catalysed by cyclic dipeptides

We synthesised a library of cis- and trans-cyclic dipeptides and evaluated their efficacy as catalysts in the asymmetric Weitz-Scheffer epoxidation of trans-chalcone. A thorough investigation relying on structure-activity studies and computational studies provided insights into the mechanism of the process. Our results revealed some structural features required for efficient conversion and for introduction of chirality into the product. The cyclic dipeptide acts as a catalyst by templating a supramolecular arrangement at the aqueous-organic interface required for efficient transformations to occur. Among all cyclic dipeptides investigated, cyclo(Leu-Leu) was the most efficient supramolecular catalyst.

Cyclic dipeptides exhibit potency for scavenging radicals

Twenty kinds of cyclic dipeptides containing l-leucine were synthesized, and their antioxidant activity against .OH and O2·- was investigated. Compounds possessing polar amino acid residues, such as Asp, Cys, Glu, Lys, Pro, Ser, and Trp, exhibited higher antioxidant activity against .OH than vitamin E. However, only cyclo(l-Cys-l-Leu) scavenged O2·-.

Onium salt supported peptide synthesis

Task specific ionic liquids and onium salts have been used as soluble supports for peptide synthesis. These new supports combine easy monitoring, high loading capacities, large scale preparation, and homogeneous kinetics characteristics while keeping adva

Structures, sensory activity, and dose/response functions of 2,5-diketopiperazines in roasted cocoa nibs (Theobroma cacao)

The taste compounds inducing the blood-like, metallic bitter taste sensation reported recently for a dichloromethane extract prepared from roasted cocoa nibs were identified as a series of 25 diketopiperazines by means of HPLC degustation, LC-MS/MS, and i

15N NMR Spectroscopy. 19 - Spectroscopic Characterization of Cyclodipeptides (2,5-Dioxopiperazines)

Various cyclodipeptides containing glycine, alanine, leucine, valine, phenylalanine, phenylglycine and sarcosine units were synthesized by cyclization of dipeptide pentachlorophenyl esters.The 13C and natural abundance 15N NMR spectra of these heterocycles were measured in trifluoroacetic acid and compared with the spectra of the corresponding amino acids and polypeptides.The 13C NMR carbonyl signals of all cyclodipeptides show a 1.5-4.0 ppm upfield shift relative to the corresponding polypeptides.The 15N NMR signals show no such consistent relationship.The substituent effects and the neighbouring residue effects observed in the 15NMR spectra of the cyclodipeptides are different from those of polypeptides, while the one bond N-H coupling constant of cis and trans amide groups was almost identical.The nitrogen and the carbonyl signal of the Gly units in cyclo-Gly-Phe show an extraordinary downfield shift, reflecting the interaction of the phenyl group with the 2,5-dioxopiperazine ring.