100945-15-1Relevant articles and documents
Total synthesis of isoroquefortine C
Schiavi, Bruno M.,Richard, David J.,Joullie, Madeleine M.
, p. 620 - 624 (2002)
A short and efficient total synthesis of isoroquefortine C, the 3,12-(Z)-isomer of roquefortine C, from L-tryptophan methyl ester hydrochloride and 4(5)-(hydroxy)methylimidazole hydrochloride is described.
Reversible Folding of a β-Hairpin Peptide by a Metal-Chelating Amino Acid
Reutzel, Jan,Diogo, Timm M.,Geyer, Armin
supporting information, p. 8450 - 8456 (2017/06/28)
5-(1-Hydroxy-pyridin-2(1H)-onyl)-l-alanine (Hop) is a N-hydroxy-1,2-pyridone functionalized α-amino acid with the desired metal-chelating properties of DOPA (3,4-dihydroxy phenylalanine) but without its unwanted redox activity. The Fmoc-protected amino acid Fmoc-l-Hop(tBu)-OH (11) was synthesized from glycine phosphonate followed by enzymatic hydrolysis of the methyl ester yielding the Hop l-isomer in 96 % ee. The amino acid 11 is used in automated peptide synthesis for the assembly of a 14mer β-hairpin peptide with the sequence [dsb1, 14]H-CHXETGKHGHKLVC-OH (X=W, l-Hop). While the 10 π electron containing indole side chain of l-Trp in peptide 14 completes the formation of a hydrophobic cluster and results in 90 % folding, the folded fraction is significantly decreased to approximately 30 % for the 6 π electron l-Hop side chain in peptide 16. Metal chelation of Ga3+ reconstitutes the folding of 16 to above 60 % due to the formation of the Ga(16)3 trimer. The chelation process of 16 is monitored by NMR spectroscopy and the subsequent release of Ga3+ by a competitive metal chelator exemplifies the reversible oligomerization of peptide epitopes by metal chelation, bearing the opportunity to synthesize protein-sized aggregates on the basis of reversible chemistry in water.
Preparation of horner-wadsworth-emmons reagent: Methyl 2- benzyloxycarbonylamino-2-(dimethoxy-phosphinyl)acetate
Azuma, Hiroki,Okano, Kentaro,Fukuyama, Tohru,Tokuyama, Hidetoshi
, p. 152 - 161 (2014/04/03)
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