200406-90-2Relevant academic research and scientific papers
A new approach to peptide synthesis
Moody, Christopher J.,Ferris, Leigh,Haigh, David,Swann, Elizabeth
, p. 2391 - 2392 (1997)
A new approach to the synthesis of dipeptides is described based on the formation of the NHCHR1CONH-CHR2CO bond by carbenoid N-H insertion, rather than the formation of the peptide bond itself.
C-terminal constrained phenylalanine as a pharmacophoric unit in peptide-based proteasome inhibitors
Baldisserotto, Anna,Marastoni, Mauro,Lazzari, Ilaria,Trapella, Claudio,Gavioli, Riccardo,Tomatis, Roberto
, p. 1403 - 1411 (2008/12/20)
Here we report the synthesis and biological properties of peptide-based molecules bearing constrained analogues of phenylalanine at the C-terminal. Compounds were tested as proteasome subunits' inhibitors. Dehydro-peptides showed good inhibition, in particular against trypsin-like (T-L) proteasome activity while some C-terminal Tic-derivatives inhibit only caspase-like activity in enzymatic β1 subunits with a certain degree of efficacy. The best analogues of the series demonstrated good resistance to proteolysis and a capacity to permeate the cell membrane.
The carbenoid approach to peptide synthesis
Buck, Richard T.,Clarke, Paul A.,Coe, Diane M.,Drysdale, Martin J.,Ferris, Leigh,Haigh, David,Moody, Christopher J.,Pearson, Neil D.,Swann, Elizabeth
, p. 2160 - 2167 (2007/10/03)
A different approach to the synthesis of dipeptides is described based on the formation of the NHCHR1CONH-CHR-CO bond by carbenoid N-H insertion, rather than the formation of the peptide bond itself. Thus decomposition of triethyl diazophosphon
