Hostname: page-component-586b7cd67f-gb8f7 Total loading time: 0 Render date: 2024-11-28T22:24:20.106Z Has data issue: false hasContentIssue false
  • English
  • Français

Enzyme Triggered Gelation of Arginine Containing Ionic-Peptides

Published online by Cambridge University Press:  01 February 2011

Jean-Baptiste A M Guilbaud ,
Aline Miller  and
Alberto Saiani
Jean-Baptiste A M Guilbaud
Affiliation:
jb.guilbaud@manchester.ac.uk, The University of Manchester, School of Materials, Manchester, United Kingdom
Aline Miller
Affiliation:
aline.miller@manchester.ac.uk, The University of Manchester, School of Chemical Engineering and Analytical Sciences, Manchester, United Kingdom
Alberto Saiani
Affiliation:
a.saiani@scholarone.com, The University of Manchester, School of Materials, Manchester, United Kingdom
Get access

Abstract

We have investigated the possibility of using the protease enzyme thermolysin to catalyse the synthesis and gelation of ionic-complementary peptides from non-gelling peptide precursors. In the described system, thermolysin was added at a fixed concentration (0.3 mg mL−1) to solutions (25 - 100 mg mL−1) of a short tetra-peptide FEFR. Initially, the protease partially hydrolysed the tetrapeptide into di-peptides in all samples. Subsequently, longer peptide sequences were found to form through reverse-hydrolysis and their stability was found to be dependent on their self-assembling properties. The sequences that self-assembled into anti-parallel β-sheet rich fibres became the stable products for the reverse hydrolysis reaction, while the others formed were unstable and disappeared with increasing incubation time. Ultimately, the main product of the system was octa-peptide, which suggests that it represents the thermodynamically favoured product of this dynamic library.

Keywords

biomaterialsol-gelfiber
Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 1272: Symposia KK/LL/NN/OO/PP – Integrated Miniaturized Materials-From Self-Assembly to Device Integration , 2010 , 1272-NN05-04
Copyright
Copyright © Materials Research Society 2010

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

1 Zhang, S. G., Lockshin, C., Cook, R. and Rich, A., Biopolymers 34, (1994)Google Scholar
2 Zhang, S. G., Holmes, T., Lockshin, C. and Rich, A., Proc. Natl. Acad. Sci. U. S. A. 90, (1993)Google Scholar
3 Mohammed, A., Miller, A. F. and Saiani, A., Macromol. Symp. 251, (2007)10.1002/masy.200750512Google Scholar
4 Saiani, A., Mohammed, A., Frielinghaus, H., Collins, R., Hodson, N., Kielty, C. M., Sherratt, M. J. and Miller, A. F., Soft Matter 5, (2009)Google Scholar
5 Guilbaud, J. B., Vey, E., Boothroyd, S., Smith, A. M., Ulijn, R. V., Saiani, A. and Miller, A. F., submitted for publication to Langmuir (2010)Google Scholar
6 Morihara, K. and Tsuzuki, H., Eur. J. Biochem. 15, (1970)Google Scholar
7 Barth, A., Biochim. Biophys. Acta-Bioenerg. 1767, (2007)Google Scholar
8 Barth, A. and Zscherp, C., Q. Rev. Biophys. 35, (2002)Google Scholar