19669-38-6Relevant academic research and scientific papers
PREPARATION AND USE OF REACTIVE OXYGEN SPECIES SCAVENGER
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Page/Page column 94, (2019/03/17)
A compound of Formula (I), pharmaceutically acceptable salts thereof, and individual enantiomers or diastereomers thereof are disclosed. Compositions and methods useful for treatment or suppression of diseases, developmental delays and symptoms related to
Design, synthesis and primary activity assay of bi- or tri-peptide analogues with the scaffold l-arginine as amino-peptidase N/CD13 inhibitors
Mou, Jiajia,Fang, Hao,Liu, Yingzi,Shang, Luqing,Wang, Qiang,Zhang, Lei,Xu, Wenfang
scheme or table, p. 887 - 895 (2010/05/02)
A series of bi- or tri-peptide analogues with the scaffold l-arginine were designed, synthesized and evaluated for their inhibitory activities against amino-peptidase N (APN) and metalloproteinase-2 (MMP-2). The primary activity assay showed that all the compounds exhibited higher inhibitory activities against APN than MMP-2. Within this series, compounds C6 and C7 (IC50 = 4.2 and 4.3 μM) showed comparable APN inhibitory activities with the positive control bestatin (IC50 = 3.8 μM).
Total synthesis and antimicrobial activity of a natural cycloheptapeptide of marine origin
Dahiya, Rajiv,Gautam, Hemendra
body text, p. 2384 - 2394 (2010/10/20)
The present study deals with the first total synthesis of the proline-rich cyclopolypeptide stylisin 2 via a solution phase technique by coupling of the Boc-L-Pro-L-Ile-L-Pro-OH tripeptide unit with the L-Phe-L-Pro-L-Pro-L-Tyr-OMe tetrapeptide unit, follo
Use of di-tert-butyl-dicarbonate both as a protecting and activating group in the synthesis of dipeptides
Laulloo, S. Jhaumeer,Khodaboccus,Hemraz,Sunnassee
, p. 4191 - 4197 (2008/03/13)
Amide formation from amino acids was achieved in an easy and convenient one-pot procedure using di-tert-butyl dicarbonate both as a protecting and an activating agent. A number of dipeptides have been synthesized in good yields. Copyright Taylor & Francis Group, LLC.
A rapid and efficient synthesis of β-casomorphin employing Boc-amino acids and 9-fluorenylmethyl chloroformate as a coupling agent
Babu, V.V. Suresh,Tantry
, p. 2708 - 2712 (2007/10/03)
The synthesis of β-casomorphin H-Tyr-Pro-Phe-Pro-Gly-OH employing Boc group for Nα-protection and 9-fluorenylmethyl chloroformate (Fmoc-Cl) for the formation of peptide bond is described. The protocol employing Fmoc-Cl as coupling reagent is found to be simple, efficient and rapid. All the intermediate peptides as well as the final protected peptide Boc-Tyr( iBu)-Pro-Phe-Pro-Gly-OMe have been isolated and fully characterized. They have been obtained in good yield and with high purity.
Serine-Protease-Assisted Synthesis of Peptide Substrates for α-Chymotripsin
Bizzozero, Spartaco A.,Rovagnati, Bruno A.,Dutler, Hans
, p. 1707 - 1719 (2007/10/02)
δ-Chymotrypsin catalyzes peptide-bond formation between acylated amino-acid and peptide esters as the carboxyl component and amino-acid and peptide amides as the amino component.The conditions under which enzyme-catalyzed coupling can be used for fragment condensation in peptide synthesis is investigated.To illustrate the method the synthesis of tetra-, penta and hexapeptides of the structure Ac-Lxn-...-Lxl-Lyl-...-Lym-NH2 with Lxl = Tyr, designed as substrates for α-chymotrypsin is described.
