Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Oliver Flögel"'
Publikováno v:
Reaction Chemistry & Engineering. 5:645-650
The development of new protocols for peptide bond formation which avoid side reactions, including epimerization, are very important. The acyl azide method for the preparation of peptides is very good at maintaining chiral integrity, however; acyl azi
Autor:
Scheghajeh Kord Daoroun Kalai, Ghislaine Marlyse Okala Amombo, Stefan Schoder, Hans-Ulrich Reissig, Oliver Flögel, Ulrike Warzok
Publikováno v:
European Journal of Organic Chemistry. 2017:1965-1972
Autor:
Dieter Seebach, Raveendra I. Mathad, Jiirg V. Schreiber, Oliver Flögel, Berhard Jaun, James Gardiner
Publikováno v:
Helvetica Chimica Acta. 92:2698-2721
β3-Peptides consisting of six, seven, and ten homologated proteinogenic amino acid residues have been attached to an α-heptapeptide (all d-amino acid residues; 4), to a hexaethylene glycol chain (PEGylation; 5c), and to dipicolinic acid (DPA deriva
Publikováno v:
Helvetica Chimica Acta. 91:2035-2056
The new electrophilic trifluoromethylating 1-(trifluoromethyl)-benziodoxole reagents A and B (Scheme 1) have been used to selectively attach CF3 groups to the S-atom of cysteine side chains of α- and β-peptides (up to 13-residues-long; products 7
Autor:
Michael Limbach, Estelle Dubost, Daniel Hoyer, Raveendra I. Mathad, Hans Widmer, Stefania Capone, Dieter Seebach, Albert K. Beck, Daniel Langenegger, Oliver Flögel, Dominique Monna, Bernhard Jaun, James Gardiner, Markus Löweneck
Publikováno v:
Helvetica Chimica Acta. 91:1736-1786
Cyclo-β-tetrapeptides are known to adopt a conformation with an intramolecular transannular hydrogen bond in solution. Analysis of this structure reveals that incorporation of a β2-amino-acid residue should lead to mimics of ‘α-peptidic β-turns
Autor:
Bernhard Jaun, Jeroen D. C. Codée, Dieter Seebach, Peter H. Seeberger, Andrew D. Abell, Markus Löweneck, Michael K. Edmonds, James Gardiner, Oliver Flögel, Florian H. M. Graichen, Raveendra I. Mathad
Publikováno v:
Helvetica Chimica Acta. 90:2251-2273
To further study the preference of the antiperiplanar (ap) conformation in α-fluoro-amide groups, two β-peptides, 1 and 2, containing a (2-F)-β3hAla and a (2-F)-β2hPhe residue, have been synthesized. Their NMR-solution structures in CD3OH were de
Publikováno v:
Helvetica Chimica Acta. 90:1651-1666
The title compounds, 4 and 7, have been prepared from the corresponding α-amino acid derivative selenocystine (1) by the following sequence of steps: cleavage of the SeSe bond with NaBH4, p-methoxybenzyl (PMB) protection of the SeH group, Fmoc or Bo
Publikováno v:
Angewandte Chemie International Edition. 45:7000-7003
Publikováno v:
Angewandte Chemie. 118:7157-7160
Autor:
Raveendra I. Mathad, Michael Limbach, Bernhard Jaun, Sylvain Cottens, Dieter Seebach, Oliver Flögel, Holger Sellner, Radovan Sebesta
Publikováno v:
Helvetica Chimica Acta. 89:1801-1825
Twelve peptides, 1–12, have been synthesized, which consist of alternating sequences of α- and β-amino acid residues carrying either proteinogenic side chains or geminal dimethyl groups (Aib). Two peptides, 13 and 14, containing 2-methyl-3-aminob