Tuning the amino acid sequence of minimalist peptides to present biological signals via charge neutralised self assembly
Alexandra L Rodriguez, Clare L Parish, David R Nisbet, Richard J Williams
SOFT MATTER | ROYAL SOC CHEMISTRY | Published : 2013
Nanofibrous materials yielded by the self-assembly of peptides are rich in potential; particularly for the formation of scaffolds that mimic the landscape of the host environment of the cell. Here, we report a novel methodology to direct the formation of supramolecular structures presenting desirable amino acid sequences by the self-assembly of minimalist peptides which cannot otherwise yield the desired scaffold structures under biologically relevant conditions. Through the rational modification of the pKa, we were able to optimise ordered charge neutralised assembly towards in vivo conditions. © The Royal Society of Chemistry 2013.
Awarded by National Health and Medicine Research Council (NHMRC)
Awarded by Australian Research Council (ARC)
We wish to thank Dr Antonio Tricoli for critical reading of the manuscript. We would also like to thank Dr Navdeep Kaur and Joanne Lee (Centre for Advanced Microscopy, ANU) for their help and guidance in preparing negative stains for TEM imaging. This research was supported by funding from the National Health and Medicine Research Council (NHMRC, APP1020332 to DRN) and from the Australian Research Council (ARC, DP130103131). ALR was supported by an Australian Postgraduate Award; CLP was supported by an NHMRC Career Development Award, and subsequently Senior Medical Research Fellowship provided by the Viertel charitable Foundation, Australia; DRN was supported by an Australian Research Council Australian Postdoctoral Fellowship, and subsequently by a NHMRC Career Development Fellowship; and RJW was supported by an Alfred Deakin Research Fellowship. The authors wish to thank Peta Nisbet for photography.