Effect of sequence on the mechanical properties of β-sheet peptide hydrogels with identical charges Jacek
1 Wychowaniec *,
Andrew
1 Smith , Aline
F.
2 Miller ,
and Alberto
1 Saiani
1School
of Materials and Manchester Institute of Biotechnology, University of Manchester, UK. 2School of CEAS and Manchester Institute of Biotechnology, University of Manchester, UK. *
[email protected]
1. Introduction
3. Peptide titration
1mg/ml 10 mg/ml net charge
2. Aim
pKa C−terminus = 2.18
pKa Glutamic acid (E) = 4.25
1mg/ml 10 mg/ml net charge
4. Choice of +2 charge F8
pKa N−terminus = 9.13
pKa Lysine (K) = 10.53
1mg/ml 10 mg/ml net charge SC
10 10 Z N i pH N pKai pKaj j pH 10 10 10 10 j i pKai
pH
2
BE
5. Physical properties a)
35.7 mM b) Concentration + 2 charge
F8 SC BE + 2 charge
F8 SC BE
β-sheet
F8
SC
6. Conclusions
BE
1. 2. 3. Acknowledgements: The authors would like to thank: the EPSRC Fellowship (Grant no: EP/K016210/1), EPSRC DTC NOWNANO funding and EPSRC DTA School of Material Science University of Manchester for providing financial support to this project.
While maintaining the same charge state on 3 different peptides, there is a difference in the physical properties of the hydrogels produced. Self-assembly process depends upon charge distribution in the primary peptide sequence. Stress-recovery experiments yield high difference in re-assembly process of selfassembled fibre hydrogels.
References: 1) Castillo Diaz, L. a., Saiani, a., Gough, J. E., & Miller, a. F. (2014).J. Tissue Eng., 5. 2) Tang, C., Miller, A. F., & Saiani, A. (2014). Int. J. Phytorem., 465(1-2), 427–35. 3) Roberts, D., Rochas, C., Saiani, A., & Miller, A. F. Langmuir. 2012 Nov 20; 28(46):16196-206.