Abstract
The self-organization of peptide-based nanostructures at a confined fluid–fluid interface, for example, the air–water or oil–water interface, is important in the context of stabilizing macroscopic soft-matter foams and emulsions. The unique ability to design interfacial nanostructures by controlling the subtle cooperativity that drives peptide self-assembly, and the ability to switch molecular cooperativity by facile triggers such as pH, opens new vistas for controlling macroscopic soft matter in industries as diverse as healthcare and industrial processing. Here we describe research aimed at developing new understanding into soft-matter formation and control, through variation of peptide sequence and bulk conditions. Macroscopic foaming and microfluidic emulsification studies prove particularly useful in visualizing and hence understanding the synergistic link between molecular design, mesoscopic interfacial properties, and bulk soft-matter stability.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Koopmans RJ, Middelberg APJ (2009) Engineering materials from the bottom up—overview. Adv Chem Eng: Eng Aspects Self-Organ Mater 35:1–10
Koopmans RJ, Aggeli A (2010) Nanobiotechnology—quo vadis? Curr Opin Microbiol 13:327–334
Leon L, Logrippo P, Tu R (2010) Self-assembly of rationally designed peptides under two-dimensional confinement. Biophys J 99:2888–2895
Kwak B, Shin K, Seok S et al (2010) Side chain assisted nanotubular self-assembly of cyclic peptides at the air–water interface. Soft Matter 6:4701–4709
Tanaka M, Ogura K, Abiko S et al (2008) Two-dimensional self-assembly of a designed amphiphilic peptide at air/water interface. Polymer J 40:1191–1194
Lepere M, Chevallard C, Hernandez JF et al (2007) Multiscale surface self-assembly of an amyloid-like peptide. Langmuir 23:8150–8155
Zhao XB, Pan F, Lu JR (2009) Interfacial assembly of proteins and peptides: recent examples studied by neutron reflection. J R Soc Interface 6:S659–S670
Khurana E, DeVane RH, Kohlmeyer A et al (2008) Probing peptide nanotube self-assembly at a liquid–liquid interface with coarse-grained molecular dynamics. Nano Lett 8:3626–3630
Middelberg APJ, Radke CJ, Blanch HW (2000) Peptide interfacial adsorption is kinetically limited by the thermodynamic stability of self association. Proc Natl Acad Sci U S A 97:5054–5059
Fairman R, Chao HG, Mueller L et al (1995) Characterization of a new 4-chain coiled-coil—Influence of chain-length on stability. Protein Sci 4:1457–1469
Dexter AF, Malcolm AS, Middelberg APJ (2006) Reversible active switching of the mechanical properties of a peptide film at a fluid–fluid interface. Nat Mater 5:502–506
Malcolm AS, Dexter AF, Middelberg APJ (2006) Foaming properties of a peptide designed to form stimuli-responsive interfacial films. Soft Matter 2:1057–1066
Middelberg APJ, He L, Dexter AF et al (2008) The interfacial structure and Young’s modulus of peptide films having switchable mechanical properties. J R Soc Interface 5:47–54
Malcolm AS, Dexter AF, Katakdhond JA et al (2009) Tuneable control of interfacial rheology and emulsion coalescence. Chemphyschem 10:778–781
Dexter AF, Middelberg APJ (2007) Switchable peptide surfactants with designed metal binding capacity. J Phys Chem C 111:10484–10492
Zhao CX, Middelberg APJ (2011) Effects of fluid–fluid interfacial elasticity on droplet formation in microfluidic devices. AIChE J 57:1669–1677
Jones DB, Middelberg APJ (2002) Mechanical properties of interfacially adsorbed peptide networks. Langmuir 18:10357–10362
Jones DB, Middelberg APJ (2002) Micromechanical testing of interfacial protein networks demonstrates ensemble behavior characteristic of a nanostructured biomaterial. Langmuir 18:5585–5591
Jones DB, Middelberg APJ (2002) Direct determination of the mechanical properties of an interfacially adsorbed protein film. Chem Eng Sci 57:1711–1722
Jones DB, Middelberg APJ (2003) Interfacial protein networks and their impact on droplet breakup. AIChE J 49:1533–1541
Zhao CX, Middelberg APJ (2009) Microfluidic mass-transfer control for the simple formation of complex multiple emulsions. Angew Chem Int Ed 48:7208–7211
Acknowledgements
The authors acknowledge funding from the Australian Research Council (DP1093056 and DP1213683) supporting their studies into peptide self-assembly at two-dimensional interfaces. Dr Chun-Xia Zhao acknowledges support from the Australian Research Council in the form of an Australian Postdoctoral Fellow (DP110100394).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2013 Springer Science+Business Media, New York
About this protocol
Cite this protocol
Zhao, CX., Middelberg, A.P.J. (2013). Stimuli-Responsive Peptide Nanostructures at the Fluid–Fluid Interface. In: Gerrard, J. (eds) Protein Nanotechnology. Methods in Molecular Biology, vol 996. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-354-1_10
Download citation
DOI: https://doi.org/10.1007/978-1-62703-354-1_10
Published:
Publisher Name: Humana Press, Totowa, NJ
Print ISBN: 978-1-62703-353-4
Online ISBN: 978-1-62703-354-1
eBook Packages: Springer Protocols