Biological and Bio-inspired Nanomaterials

<div>1) Nanozymes&nbsp;</div><div>Xiyun Yan (Institute of Biophysics, CAS, China)&nbsp;</div><div>This chapter will describe the discovery of nanoparticles with intrinsic catalytic activity, and their subsequent use in applications ranging from environmental chemistry to tumour diagnosis.&nbsp;</div><div><br></div><div>2) DNA origami&nbsp;</div><div>Ned Seeman (New York University, USA)</div><div>This chapter will describe exploitation of the sequence-specific binding properties of DNA to direct the assembly of materials at the nanoscale to give final structures with well-defined spacings, orientations, and stereo-relationships.&nbsp;</div><div><br></div><div>3) DNA sensors and nanopores&nbsp;</div><div>Ulrich Keyser (Cavendish Laboratory, University of Cambridge, UK)&nbsp;</div><div>This chapter will describe the use of DNA origami to create nanopores that can selectively detect specific single biomolecules in solution, thereby mimicking the selectivity of membrane channel proteins.<br></div><div>4) Non-proteinacious bioinspired nanostructures&nbsp;</div><div>Lihi Adler-Abramovich & Ehud Gazit (Tel Aviv University, Israel)&nbsp;</div><div>This chapter will describe the extension of the bionanotechnological paradigm that only peptides and DNA can self-assemble into functional structures. The authors will present results on the self-assembly and materials properties of amino acids, metabolites and peptide nucleic acids.</div><div><br></div><div>5) Composite nanomaterials&nbsp;</div><div>Raffaele Mezzenga (ETH Zurich, Switzerland)&nbsp;</div><div>This chapter will describe the structure and properties of nanomaterials that combine protein with materials such as hydroxyapatite thus mimicking bone, or graphene to form biodegradable and conductive nanomaterials.</div><div><br></div><div>6) Self-assembly of ferritin and its biological properties and applications</div><div>Soumyananda Chakraborti & Pinak Chakrabarti (Bose Institute, Kolkata, India)&nbsp;</div><div>This chapter will describe the properties and applications of ferritins, which are naturally-occurring proteins that self-assemble into hollow cage structures. The interior cavity, which in nature is utilized for sequestration of iron, can be exploited to encapsulate different carrier molecules ranging from cancer drugs to therapeutic proteins. The structure itself can act as a well-defined building block for fabrication, and the exterior surface can be modified to provide further functionality.</div><div><br></div><div>7) Dynamics and control of peptide self-assembly and aggregation</div><div>Paolo Arosio, Chris Dobson & Tuomas Knowles (Dept. of Chemistry, University of Cambridge, UK)&nbsp;</div><div>This chapter will describe how a detailed theoretical understanding of the sequential and parallel elementary molecular reaction steps that lead to peptide self-assembly from monomeric building blocks allows control of the assembly process in both disease-related and functional contexts.</div><div><br></div><div>8) Peptide self-assembly and its modulation: imaging on the nanoscale</div><div>Chen Wang (National Centre Nanoscience and Technology, CAS, China)&nbsp;</div><div>This chapter will describe the use of scanning tunnelling microscopy to obtain site-specific structural information for amyloidal peptides, and to design and screen peptides, small molecules and other modifications that target amyloidal peptides and modulate their assembly.</div><div><br></div><div>9) Spectroscopic properties of peptide nanostructures&nbsp;</div><div>Dorothea Pinotsi & Clemens Kaminski (Dept. of Chemical Engineering and Biotechnology, University of Cambridge, UK)</div><div>This chapter will describe interesting optical and spectroscopic properties of peptide assemblies, such as fibrillar and crystalline structures, which emerge as a consequence of the order of the assemblies.</div><div><br></div><div>10) Single molecule detection of amyloid assembly&nbsp;</div><div>David Klenerman (Dept. of Chemistry, University of Cambridge, UK)&nbsp;</div><div>This chapter will describe the application of single molecule fluorescence techniques to study the molecular mechanism of amyloid assembly, including characterisation of the properties of intermediate species formed.</div><div><br></div><div>11) Mechanisms of aromatic short peptide self-assembly&nbsp;</div><div>Alexander Buell (University of Düsseldorf, Germany) & Ehud Gazit (Tel Aviv University, Israel) &nbsp;</div><div>This chapter will describe recent progress in the mechanistic understanding of the self-assembly of short aromatic peptides into functional materials. Such structures have so far mainly been found by empirical approaches and the lack of mechanistic understanding has hampered our ability to fully exploit peptide self-assembly. The authors will also put these recent results into the wider context of peptide self-assembly in general.</div><div><br></div><div>12) Designed nanomaterials based on spider silk&nbsp;</div><div>Markus Buehler (MIT, USA)&nbsp;</div><div>This chapter will describe the computational mechanics of bio-inspired protein nanomaterials, particularly those based on the structure of spider silk.&nbsp;</div><div><br></div><div><br></div><div>13) Decorating, functionalising and crosslinking protein nanomaterials&nbsp;</div><div>Marie Bongiovanni (University of Cambridge) & Sally Gras (University of Melbourne)</div><div>This chapter will describe how the chemical functionalities of proteins and their ability to fold and self-assemble into micron-scale structures can be exploited to create materials with interesting chemical, mechanical, electrical and biological properties.</div><div><br></div><div>14) Protein nanofibrils as storage forms of peptide drugs and hormones</div><div>Samir Maji (IIT Bombay, India)&nbsp;</div><div>This chapter will describe how the high thermodynamic stability of peptide aggregates is exploited by nature and the pharmaceutical industry for long term storage and slow release of peptide drugs and hormones.</div><div><br></div><div>15) Protein microgels from amyloid fibril networks</div><div>Ulyana Shimanovich, Lianne Roode, Tuomas Knowles (Dept. of Chemistry, University of Cambridge, UK) & Sarah Perrett (Institute of Biophysics, CAS, China)&nbsp;</div><div>This chapter will describe the use of microfluidic techniques to form microgels from self-assembling proteins and their application, for example, as a carrier or scaffold for functional molecules.</div><div><br></div><div>16) Targeted functional peptide assemblies for cancer therapy</div><div>Guangjun Nie (National Centre Nanoscience and Technology, CAS, China)&nbsp;</div><div>This chapter will describe will describe the design and application of peptide assemblies that target and penetrate solid tumours.</div><div><br></div><div>17) Growing cells on amyloid fibrils&nbsp;</div><div>Shuguang Zhang (MIT, USA)</div><div>This chapter will describe the design and application of self-assembling peptides that provide a suitable surface to promote growth of mammalian cells, and can be further functionalised in terms of peptide sequence or surface chemistry to control attachment and growth of the cells.</div><div><br></div><div>18) From lab on a chip to organ on a chip</div><div>Jinhua Qin (Dalian Institute of Chemical Physics, CAS, China)</div><div>This chapter will describe the use of microfluidic techniques to assemble biomimetic tissue-like materials that can be used for drug development and testing as well as diagnostics.</div><div><br></div>