42280-29-5

Upstream product

• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 2462-31-9 benzyl 2-aminoacetate hydrochloride 
• 1738-68-7 Gly-OBz 
• 1738-76-7 glycine benzyl ester p-toluenesulfonic acid salt 
• 25616-33-5 2-((2S)-2-((tert-butoxycarbonyl)amino)-3-phenylpropanamido)acetic acid 
• 100-39-0 benzyl bromide 

Downstream Products

• 75895-24-8 Z-Arg(Mts)-Phe-Gly-OBzl 
• 75895-25-9 Z(OMe)-Asp(OBzl)-Arg(Mts)-Phe-Gly-OH 
• 1270202-28-2 Boc-GFGFP-OH 
• 1374975-58-2 C₄₃H₅₄N₆O₉ 
• 82487-57-8 Boc-D-Ala-Phe-Gly-OBzl 
• 1433858-12-8 [2-phenyl-1-(prop-2-ynylcarbamoylmethyl-carbamoyl)-ethyl]-carbamic acid tert-butyl ester 

Relevant academic research and scientific papers

Gram-Scale Synthesis of a Hexapeptide by Fragment Coupling in a Ball Mill

Synthesis of long peptides is generally considered as a challenge to peptide chemists, in addition to producing significant amounts of toxic waste, such as DMF. Here we show that using solvent-less methods, such as ball milling, enabled the production of

π-Stacking assisted redox active peptide-gallol conjugate: Synthesis of a new generation of low-toxicity antimicrobial silver nanoparticles

In this study, we describe the rational design and synthesis of a redox-active petide-gallol conjugate and explore its application in the preparation of antimicrobial silver nanoparticles. Increase in acidity and redox activity of peptide-gallol compounds

Synthesis, binding affinities and metabolic stability of dimeric dermorphin analogs modified with β3-homo-amino acids

In this study, proteinogenic amino acids residues of dimeric dermorphin pentapeptides were replaced by the corresponding β3-homo-amino acids. The potency and selectivity of hybrid α/β dimeric dermorphin pentapeptides were evaluated by competeti

Development of fluorescent peptide substrates and assays for the key autophagy-initiating cysteine protease enzyme, ATG4B

Abstract An efficient assay for monitoring the activity of the key autophagy-initiating enzyme ATG4B based on a small peptide substrate has been developed. A number of putative small fluorogenic peptide substrates were prepared and evaluated and optimized

Structure-Based Rationale Design and Synthesis of Aurantiamide Acetate Analogues - Towards a New Class of Potent Analgesic and Anti-inflammatory Agents

A series of new aurantiamide acetate analogues were synthesized by modifying its N-terminal substitution and the amino acid residue. The structure of all these compounds was established on the basis of analytical and spectral studies. All the new derivatives were evaluated in vivo for their analgesic activity by tail flick method in mice and anti-inflammatory activity against carrageenan-induced oedema in albino rats at different doses (25, 50 and 100mg/kg body weight). All the compounds exhibited significant pharmacological activity with no ulcerogenic liability. In particular, pentapeptides and tricosamers (30 amino acids) containing analogues have demonstrated high potency than the reference standards. These compounds hold promise for further development.

Design and synthesis of tryptophan containing peptides as potential analgesic and anti-inflammatory agents

A new series of smaller peptides with tryptophan at C-terminal and varying N-protected amino acids/peptides were designed, synthesized and characterized by analytical and spectroscopic techniques. Analgesic and anti-inflammatory properties of these peptides were carried out in vivo using tail-flick method and carrageenan-induced paw edema method, respectively, at different doses and different time intervals. Most of the peptides synthesized displayed enhanced activity, and particularly tetra and hexapeptides 29-31 were found to be even more potent than the reference standards used. Moreover, some peptides have exhibited promising activity even after 24h of administration, whereas the reference standards were active only up to 3h. Further, the compounds did not present any ulcerogenic liability.

Kinetic studies on oxidation of Gly-Val-Gly, Gly-Phe-Ply and Ala-Val-Gly using Mn(III)

The fragments of elastin sequences, glycyl-valyl-glycine (GVG), glycyl-phenylalanyl-glycine (GFG) and alanyl-valyl-glycine (AVG) have been synthesized by classical solution phase method and characterized. Kinetics of oxidation of these tripeptides (TP) by Mn(III) has been studied in the presence of sulphate ions in acidic medium at 25°C. The reaction follows spectrophotometrically at Λmax 500 nm. A first order dependence of rate on both [Mn(III)] and [TP] has been observed. The rate is independent of concentrations of reduction product, Mn(II) and hydrogen ions. Effects of varying dielectric constant of the medium and addition of anions such as sulphate, chloride and perchlorate have been studied. Activation parameters have been evaluated using Arrhenius and Erying plots. The oxidation products are isolated and characterized. A tentative mechanism involving the reaction of TP with Mn(III) in the rate-limiting step is suggested. The effect of hydrophobicity of amino acids on the rate of oxidation is discussed.

Synthesis of immunoaduvant conjugates with HIV-derived peptide inducing peptide-specific antibody

MDP and lipopeptide analog conjugates inducing HIV-derived peptide-specific antibody without adding further macromolecular carriers or adjuvants were synthesized.