Our ability to manipulate function at interfaces in native and near-native environments is critical for the fabrication of nanostructured materials and devices. Biomolecular self-assembly lends itself to robust bio-nano systems. However, exact construction strategies to enable desired applications stumble upon the lack of control over self-assembly processes.
De novo peptide design provides a saving solution to this.[1] Small proteins can be designed to deliver functions that are otherwise accessible only to macromolecular subcellular complexes. Examples include gene delivery systems,[2] fibrillar microscopic structures for tissue repair[3] and responsive antimicrobial agents[4]. A key factor in all such designs is their structural and functional relevance to native self-assembling structures, be these viruses, extracellular matrices or host defence systems. Thus, this is our ability to construct such materials at will that advances the development of efficient bio/nano-interface technologies.[5]
References
1. Ryadnov, M. G. (2012) Prescriptive peptide design. In Amino acids, peptide and proteins. (Farkas, E. & Ryadnov, M. G., eds.) SPR, RSC Publishing (2012), v.37.
2. Lamarre, B., Ravi, J. & Ryadnov, M. G. (2011) GeT peptides: a single-domain approach to gene delivery. Chem. Commun., 47, 9045-9047.
3. Bella, A., Ray, S., Shaw, M. & Ryadnov, M. G. (2012) Arbitrary self-assembly of peptide extracellular microscopic matrices. Angew. Chem. Int. Ed., 51, 428-431.
4. Ryadnov, M. G., Mukamolova, G. V., Hawrani, A. S., Spencer, J. & Platt, R. (2009) RE-coil: an antimicrobial peptide regulator. Angew. Chem. Int. Ed. 48, 9676-9679.
5. Ryadnov, M. G. (2009) Bionanodesign: Following the Nature’s touch. RSC Publishing, 250 pp.