Issue 8, 2003
From the journal:

Organic & Biomolecular Chemistry

Understanding protease catalysed solid phase peptide synthesis

Rein V. Ulijn,a   Nicola Bisek,a   Peter J. Hallingb  and  Sabine L. Flitsch*a  

* Corresponding authors

a Department of Chemistry, The University of Edinburgh, King's Buildings, West Mains Road, Edinburgh, Scotland, UK
Fax: +44(0)131 650 4737
Tel: +44(0)131 650 4737

b Department of Chemistry, The University of Strathclyde, Thomas Graham Building, Cathedral Street, Glasgow, Scotland, UK
Fax: +44(0)141 552 4822
Tel: +44(0)141 548 2683

Abstract

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.

Graphical abstract: Understanding protease catalysed solid phase peptide synthesis

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Article information

DOI
https://doi.org/10.1039/B211890D
Article type
Paper
Submitted
05 Dec 2002
Accepted
04 Mar 2003
First published
19 Mar 2003

Org. Biomol. Chem., 2003,1, 1277-1281

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Understanding protease catalysed solid phase peptide synthesis

R. V. Ulijn, N. Bisek, P. J. Halling and S. L. Flitsch, Org. Biomol. Chem., 2003, 1, 1277 DOI: 10.1039/B211890D

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