65671-71-8

Upstream product

• 21760-98-5 L-valine benzyl ester 
• 4070-48-8 L-Valine methyl ester 
• 15761-39-4 1-(tert-butoxycarbonyl)-L-proline 
• 6306-52-1 L-valine methylester hydrochloride 
• 16652-76-9 L-valine benzyl ester p-toluenesulfonate salt 
• 74912-90-6 tert-butyl (2S)-2-((2S)-1-methoxy-3-methyl-1-oxo-butan-2-ylcarbamoyl)pyrrolidine-1-carboxylate 
• 53363-79-4 N-(tert-butoxycarbonyl)-L-prolyl-L-valine benzyl ester 

Downstream Products

• 1013917-16-2 C₂₈H₄₄N₄O₆ 
• 1433896-33-3 rhodamine(Arg-(Cbz)2-Pro-Val-NHBoc)₂ 
• 99909-27-0 Boc-Pro-Val-Arg(NO₂)-Gly-OBzl 

Relevant academic research and scientific papers

Synthesis of novel proline-based imidazolium ionic liquids

Abstract: A series of eight novel proline functionalized dipeptide imidazolium ionic liquids (DPILs), i.e. Boc-[Pro-Pro-EMIM], Boc-[Pro-Val-EMIM], Boc-[Pro-Ala-EMIM], Boc-[Pro-Phe-EMIM] containing [Cl] and [NTf2] anions were synthesized via a f

Total Synthesis of Reniochalistatin e

Reniochalistatin E (1) is one of the five related cyclic peptides isolated from the marine sponge Reniochalina stalagmitis. The discovery of these compounds resulted from a screening program directed toward the identification of proline-rich bioactive compounds. Reniochalistatin E is the only member of the family to possess a tryptophan amino acid residue. Given the cytotoxicity observed for 1, efforts were directed toward developing a synthetic route to 1. The first total synthesis of 1 has been accomplished in a 15-step route in an overall 5.0% yield. The synthetic sample of reniochalistatin E was shown to have similar activity toward HeLa and RPMI-8226 cell lines compared to the natural sample, with IC50 values of 16.9 vs 17.3 μM and 4.5 vs 4.9 μM, respectively. Interestingly, both of the fully deprotected octapeptides constructed toward the synthesis of reniochalistatin E were shown to have cytotoxicity. The route provides a means to probe the structure-activity relationship of 1 and further biological investigations.

Towards the first total synthesis and anticancer screening of polycarponin C: A cyclic octapeptide

The present study describes designing, synthesis and anticancer screening of a proline rich cyclic octapeptide polycarponin C, by solution phase synthesis. The synthesis was carried out by coupling a tetrapeptide Boc-Pro-Thr-Leu-Pro-OH with another tetrap

Water promoted enantioselective aldol Reaction by proline-cholesterol and -diosgenin based amphiphilic organocatalysts

A series of proline-cholesterol and -diosgenin based amphiphilic organocatalysts were developed for the first time, and their catalytic activities for the enantioselective aldol reaction were investigated. The results indicated that water can significantl

Synthesis, characterization and antimicrobial studies on some newer imidazole analogs

A novel series of 3,5-diiodo-4-(2-methyl-1H-imidazol-5-yl)benzoic acid analogs of amino acids, dipeptides and tripeptides was synthesized by using dicyclohexylcarbodiimide and diisopropylcarbodiimide (DCC/DIPC) as coupling agents and triethylamine (TEA) as base. Structures of all the newly synthesized compounds were confirmed by elemental analysis and IR, 1H NMR, 13C NMR and mass spectral data. Imidazolopeptides were investigated for their antimicrobial activity and some of newly synthesized compounds 2c, 2d, 2h and their hydrolyzed analogs 3b, 3d exhibited potent bioactivity against pathogenic fungi Candida albicans and dermatophytes Trichophyton mentagrophytes and Microsporum audouinii with MIC values of 12.5-6 μg/ml, as compared to the reference drug - griseofulvin. In addition, moderate activity against gram negative bacteria Pseudomonas aeruginosa and Klebsiella pneumoniae was also observed for synthesized imidazolopeptides. Oesterreichische Apotheker-Verlagsgesellschaft m. b. H.

Bitter Taste of Synthetic C-Terminal Tetrapeptide of Bovine β-Casein, H-Pro196-Val-Leu-Gly-Pro-Arg-Gly-Pro-Phe-Pro-Ile-Ile-Val209-OH, and Its Related Peptides

The primary structure of bovine β-casein contains the partial sequence of -Pro196-Val-Leu-Gly-Pro-Val-Arg-Gly-Pro-Phe-Pro-Ile-Ile-Val209 in the C-terminal portion.We previously reported that the synthetic C-terminal octapeptide, Arg202-Val209, is extremly bitter with its threshold value 0.004 mM, 250 times as strong as that of caffeine.To further investigate the bitter taste of the C-terminal portion of β-casein, we synthesized the C-terminal tetrapeptide, Pro196-Val209, and some its fragments.A hydrophobic hexapeptide, Pro196-Val201, was twice as bitter as caffein.The bitter taste of decapeptide, Pro200-Val209, was the same as that of Arg202-Val209.Although the tetradecapeptide, Pro196-Val209, was composed of two bitter peptides, Pro196-Val201 and Arg202-Val209, its bitter taste was weaker than that of Arg202-Val209 and its threshold value was 0.015 mM.We suggested that the increase of bitterness in peptides through the introduction of hydrophobic amino acids depended on the number of hydrophobic amino acids added.In addition, the synthetic retro analog of Arg202-Val209 (H-Val-Ile-Ile-Pro-Phe-Pro-Gly-Arg-OH) was not as bitter as Arg202-Val209.This indicated that the sequence of Arg202-Val209 is important for extreme bitterness.

Structure of N-(tert-Butoxycarbonyl)-L-prolyl-L-valylglycine Hemihydrate

C17H29N3O6*1/2H2O, Mr = 380.44, P21, a = 15.783(2), b = 13.428(2), c = 9.815(2) Angstroem, β = 90.94(1) deg, Do = 1.19, Dc (Z = 4) = 1.21 Mg m-3, m.p. 444-445 K; there are two independent molecules in

A Convenient Test for Racemization in Peptide Synthesis by Separation of Diasteremers of Tetrapeptide by GLC on Packed Column

The complete separation of diastereomers of some Tfa-tetrapeptide-OMe by gas chromatography of a packed column provided a simple method for assessing racemization during peptide synthesis using well known coupling reagents and various model reactions.The coupling method with diethyl phosphorocyonidate in dimethyl formamide was confirmed to be almost free of racemization.