145038-52-4Relevant articles and documents
Synthesis of chlorophyll-amino acid conjugates as models for modification of proteins with chromo/fluorophores
Tamiaki, Hitoshi,Isoda, Yasuaki,Tanaka, Takuya,Machida, Shinnosuke
, p. 1421 - 1428 (2014)
A chlorophyll-a derivative bonded directly with epoxide at the peripheral position of the chlorin π-system was reacted with N-urethane and C-ester protected amino acids bearing an alcoholic or phenolic hydroxy group as well as a carboxy group at the residue to give chlorophyll-amino acid conjugates. The carboxy residues of N,C-protected aspartic and glutamic acids were esterified with the epoxide in high yields. The synthetic conjugates in dichloromethane had absorption bands throughout the visible region including intense red-side Qy and blue-side Soret bands. By their excitation at the visible bands, strong and efficient fluorescence emission was observed up to the near-infrared region. The chromo/fluorophores are promising for preparation of functional peptides and modification of proteins.
Hydantoin and thiohydantoin derivatives as antiviral drugs
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Paragraph 0280-0281, (2013/12/03)
The present invention relates to a compound of the following formula (I), or a salt, solvate, tautomer, enantiomer, diastereoisomer or racemic mixture thereof: as well as its use as a drug, notably in the treatment of hepatitis C, its preparation process, and the pharmaceutical compositions containing such a compound.
Design and preparation of serine-threonine protein phosphatase inhibitors based upon the nodularin and microcystin toxin structures. Part 3
Webster,Maude,O'Donnell,Mehrotra,Gani
, p. 1673 - 1695 (2007/10/03)
Nodularin and microcystins are complex natural cyclic isopeptidic hepatotoxins that serve as subnanomolar inhibitors of the eukaryotic serine-threonine protein phosphatases PP1 and PP2A, enzymes that are intimately involved in controlling cellular metabolism. Previously we described a solution-phase synthesis of stripped-down nodularin analogues; cyclo[-β-Ala-(R)-Glu-α-OMe-γ-Sar-(R)-Asp-α-OMe- β-(S)-Phe-] 3 and cyclo[-(3R)-3-hydroxymethyl-β-Ala-(R)-Glu-α-OMe-γ-Sar-(R)- Asp-α-OMe-β-(S)-Phe-] 5. The synthetic strategy was designed to allow post-macrocyclisation elaboration. Here we examine alternative methods for introducing diversity and achieving macrolactamisation and compare the relative efficiency of solution- vs. solid-phase peptide syntheses of the macrocycles. Syntheses and the biological activities of the macrocycles cyclo{-[(2R)-α-4-benzylpiperidinylamido-Asp]-β-[(R)-Glu]-γ- Sar-[(R)-Asp]-β-(S)-Phe-} 29 and cyclo{-(2S)-Phe-[(2R)-α-4-benzylpiperidinylamido-Asp]-(R)-Glu-γ- (S)-Pro-β-(R)-Asp-} 65 are compared. Both compounds contain sufficient side-chain functionality to interact with a hydrophobic groove at the enzyme active site. The proline containing analogues 30, 31 (R3 = CH3) where sarcosine is replaced in macrocycles 3 and 4, were also synthesised in order to correlate conformational properties with biological activity. In accord with predictions macrocycles 29 and 65 were found to be weak inhibitors of PP1 with IC50 2.9 and 2.7 mM respectively.