160916-46-1Relevant academic research and scientific papers
Total synthesis and antifungal evaluation of cyclic aminohexapeptides
Klein, Larry L.,Li, Leping,Chen, Hui-Ju,Curty, Cynthia B.,Degoey, David A.,Grampovnik, David J.,Leone, Christina L.,Thomas, Sheela A.,Yeung, Clinton M.,Funk, Kenneth W.,Kishore, Vimal,Lundell, Edwin O.,Wodka, Dariusz,Meulbroek, Jon A.,Alder, Jeffrey D.,Nilius, Angela M.,Lartey, Paul A.,Plattner, Jacob J.
, p. 1677 - 1696 (2007/10/03)
The need for new therapies to treat systemic fungal infections continues to rise. Naturally occurring hexapeptide echinocandin B (1) has shown potent antifungal activity via its inhibition of the synthesis of β-1,3 glucan, a key fungal cell wall component. Although this series of agents has been limited thus far based on their physicochemical characteristics, we have found that the synthesis of analogues bearing an aminoproline residue in the 'northwest' position imparts greatly improved water solubility (>5 mg/mL). The synthesis and structure-activity relationships (SAR) based on whole cell and upon in vivo activity of the series of compounds are reported. Copyright (C) 2000 Elsevier Science Ltd.
Synthesis of novel chiral amino acids possessing a porphyrin moiety
Tamiaki, Hitoshi,Onishi, Motoki
, p. 1029 - 1032 (2007/10/03)
Phenylalanine derivatives bearing a porphyrin moiety at the para- position were prepared in an enantiomerically pure form. The synthetic nonnatural aromatic amino acid reacted with amines and acids to give novel functionalized peptides without loss of the
Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 2. Peptide structure- activity studies
Dragovich, Peter S.,Webber, Stephen E.,Babine, Robert E.,Fuhrman, Sheila A.,Patick, Amy K.,Matthews, David A.,Reich, Siegfried H.,Marakovits, Joseph T.,Prins, Thomas J.,Zhou, Ru,Tikhe, Jayashree,Littlefield, Ethel S.,Bleckman, Ted M.,Wallace, Michael B.,Little, Thomas L.,Ford, Clifford E.,Meador III, James W.,Ferre, Rose Ann,Brown, Edward L.,Binford, Susan L.,DeLisle, Dorothy M.,Worland, Stephen T.
, p. 2819 - 2834 (2007/10/03)
The structure-based design, chemical synthesis, and biological evaluation of various peptidederived human rhinovirus (HRV) 3C protease (3CP) inhibitors are described. These compounds are comprised of an ethyl propenoate Michael acceptor moiety and a tripeptidyl binding determinant. The systematic modification of each amino acid residue present in the binding determinant as well as the N-terminal functionality is described. Such modifications are shown to provide irreversible HRV-14 3CP inhibitors with anti-3CP activities (k(obs)/[I]) ranging from 60 to 280 000 M-1 s-1 and antiviral EC50's which approach 0.15 μM. An optimized inhibitor which incorporates several improvements identified by the structure-activity studies is also described. This molecule displays very rapid irreversible inhibition of HRV-14 3CP (k(obs)/[I] = 800 000 M-1 s-1) and potent antiviral activity against HRV-14 in cell culture (EC50 = 0.056 μM). A 1.9 A? crystal structure of an S-alkylthiocarbamate-containing inhibitor complexed with HRV-2 3CP is also detailed.
An improved preparation of 4-hydroxymethyl-L-phenylalanine
Morera, Enrico,Ortar, Giorgio,Varani, Aurelio
, p. 4279 - 4285 (2007/10/03)
Palladium-catalyzed hydroformylation of methyl esters of N-Boc-L- tyrosine triflate (1a) and N-Boc-4-iodo-L-phenylalanine (1b) followed by reduction with sodium borohydride and standard deprotection procedures affords the title compound in 77 and 83% over
