Ulijn, R.V. and Bisek, N. and Halling, P.J. and Flitsch, S.L. (2003) Understanding protease catalysed solid phase peptide synthesis. Organic and Biomolecular Chemistry, 1 (8). pp. 1277-1281. ISSN 1477-0520Full text not available in this repository. (Request a copy from the Strathclyde author)
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.
|Keywords:||protease, dipeptides, Fmoc-amino acids, reagents, hydrophobic hydration, mutual electrostatic repulsion, Chemistry, Biochemistry, Organic Chemistry, Physical and Theoretical Chemistry|
|Subjects:||Science > Chemistry|
|Department:||Faculty of Science > Pure and Applied Chemistry|
|Depositing user:||Users 16 not found.|
|Date Deposited:||10 Mar 2006|
|Last modified:||06 Jan 2017 03:23|