126402-69-5Relevant academic research and scientific papers
Protease-catalyzed peptide synthesis on solid support
Ulijn, Rein V.,Baragana, Beatriz,Halling, Peter J.,Flitsch, Sabine L.
, p. 10988 - 10989 (2002)
The direct enzymatic synthesis of peptides from amino acids is widely used as a useful alternative to chemical synthesis. However, good yields of such enzyme-catalyzed reactions require altered reaction conditions to overcome the bias for hydrolysis in aqueous medium. We argue that the synthesis/hydrolysis equilibrium can be shifted toward synthesis in aqueous medium by immobilizing the amine on solid support. In this report, we show the first examples of solid-phase peptide synthesis catalyzed by a protease in bulk aqueous buffer. Copyright
Alternative and chemoselective deprotection of the α-amino and carboxy functions of N-Fmoc-amino acid and N-Fmoc-dipeptide methyl esters by modulation of the molar ratio in the AlCl3/N,N-dimethylaniline reagent system
Di Gioia, Maria Luisa,Leggio, Antonella,Le Pera, Adolfo,Liguori, Angelo,Perri, Francesca,Siciliano, Carlo
, p. 4437 - 4441 (2007/10/03)
The amino and carboxy functions in N-Fmoc-α-amino acid and N-Fmoc-peptide methyl esters can be alternatively and chemoselectively deprotected by treatment with the reagent system AlCl3/N,N- dimethylaniline (DMA). The chemoselectivity of the process is controlled by modulating the relative molar ratio of the Lewis acid and DMA. Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2004.
Understanding protease catalysed solid phase peptide synthesis
Ulijn, Rein V.,Bisek, Nicola,Halling, Peter J.,Flitsch, Sabine L.
, p. 1277 - 1281 (2007/10/03)
A protease (thermolysin) was used to directly synthesise a number of dipeptides from soluble Fmoc-amino acids onto a solid support (PEGA1900) in bulk aqueous media, often in very good yields. This shift in equilibrium toward synthesis is remarkable because for soluble dipeptides in aqueous solution hydrolysis rather than synthesis is observed. Three possible reasons for the equilibrium shift were considered: (i) using a solid support makes it easy to use an excess of reagents, so mass action contributes towards synthesis; (ii) reduction in the unfavourable hydrophobic hydration of the Fmoc group within the solid support compared with the free amino acid in solution and (iii) suppression of the ionization of amino groups linked to the solid phase due to mutual electrostatic repulsion. It was found that under the conditions studied the second effect was most important.
