37783-45-2Relevant academic research and scientific papers
Synthesis and biological activity of the prodrug of class I major histocompatibility peptide GILGFVFTL activated by β-glucuronidase
Rawale, Sharad,Hrihorczuk, Lew M.,Wei, Wei-Zen,Zemlicka, Jiri
, p. 937 - 943 (2007/10/03)
The first synthesis of a prodrug of HLA-A2.1 associated antigenic influenza peptide 2a was accomplished. Two methods for synthesis of prodrugs of antigenic peptides activated by β-glucuronidase and comprising a self-immolative 3-nitrobenzyloxycarbonyl moiety were investigated. Reaction of β-glucuronic acid glycoside of 4-hydroxy-3-nitrobenzyl alcohol (3) with N,N′-disuccinimidyl carbonate (DSC) followed by conjugation with AlaOMe, Gly, Thr, Phe-Leu, and Leu-Arg gave carbamates 4a-4f. Deacetylation of 4b and 4e with MeONa/MeOH gave β-glucuronides 5b and 5e. Compound 5e was converted to β-glucuronic acid conjugate 6e by the action of pig liver esterase (PLE). Compound 6e is a substrate for β-glucuronidase. Method of a direct introduction of the prodrug residue into antigenic nonapeptide GILGFVFTL (2b) failed. Alternately, glycine conjugate 5b was activated to pentafluorophenyl ester 10. Model coupling of 10 with Phe-Leu gave tripeptide conjugate ester 11a which was hydrolyzed by PLE to uronic acid 12. Condensation of 10 with octapeptide ILGFVFTL (9) gave prodrug precursor 11b. Octapeptide 9 was prepared by de novo synthesis using a racemization-free fragment coupling method. Ester hydrolysis with Ba(OH)2/MeOH gave the target prodrug 2a which is a substrate for β-glucuronidase. Prodrug 2a does not bind to HLA-A2.1 of T2 human cells defective in major histocompatibility complex I (MHC I)-associated peptide processing. Addition of β-glucuronidase restored the binding to the level observed with parent nonapeptide 2b although higher concentrations of prodrug 2a and enzyme were necessary.
Hydrophobicity profile of amino acid residues: A differential scanning calorimetry and circular dichroism study of leucine and isoleucine co-polypeptides of the protein-based polymers of elastin
Gowda, D. Channe,Baba, A. Ramesha,Luan, Chi-Hao
, p. 2606 - 2613 (2007/10/03)
The inverse temperature transition of hydrophobic folding and assembly of a "host-guest" model system based on the elastin derived polypentapeptide, poly(VPGVG), is employed to determine the relative hydrophobicity of amino acid residues of proteins and p
Peptide Enolates. C-Alkylation of Glycine Residues in Linear Tri-, Tetra-, and Pentapeptides via Dilithium Azadienediolates
Bossler, Hans G.,Seebach, Dieter
, p. 1124 - 1165 (2007/10/02)
The Boc-protected tripeptides Boc-Val-Gly-Leu-OH (1), Boc-Leu-Sar-Leu-OH (2), Boc-Leu-Gly-MeLeu-OH (3), and Boc-Val-BzlGly-Leu-OMe (64), tetrapeptide Boc-Leu-Gly-Pro-Leu-OH (9), and pentapeptides Boc-Val-Leu-Gly-Abu-Ile-OH (4), Boc-Val-Leu-Sar-MeAbu-Ile-O
ANTIHERPETIC AGENTS
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, (2008/06/13)
A series of carboxyl-containing N-alkyldipeptides have been found to posess antiviral potency-specifically against herpes simplex virus-by selectively inhibiting the viral ribonucleotide reductase enzyme
1-(o-NITROPHENYLSULPHONYLOXY)BENZOTRIAZOLE, REAGENT FOR THE CONDENSATION OF CARBOXYLIC ACIDS WITH AMINES
Topuzyan, V. O.,Martirosyan, M. S.
, p. 2148 - 2153 (2007/10/02)
With the Schotten-Baumann reaction we have synthesized 1-(o-nitrophenylsulfonyloxy)benzotriazole and have shown its suitability for the synthesis of esters of 1-hydroxybenzotriazole and carboxylic amides, and also of peptides.
ATRIOPEPTINS. I. SYNTHESIS OF C-TERMINAL FRAGMENTS
Ovchinnikov, Mikhail V.,Bespalova, Zhanna D.,Molokoedov, Aleksandr S.,Revenko, Inna V.,Sepetov, Nikolai F.,et al
, p. 772 - 783 (2007/10/02)
Peptides, corresponding to the C-terminal sequence in atriopeptins, have been synthesized using classical methods of peptide synthesis in solution and characterized by various physicochemical methods.The synthetic strategy and methods are discussed.
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
Shinoda, Ichizo,Fushimi, Akira,Kato, Hironobu,Okai, Hideo,Fukui, Sazuko
, p. 2587 - 2596 (2007/10/02)
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.
