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Bio-Inspired Nanotechnology: From Surface Analysis to Applications PDF

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Marc R. Knecht · Tiffany R. Walsh Editors Bio-Inspired Nanotechnology From Surface Analysis to Applications Bio-Inspired Nanotechnology Marc R. Knecht Tiffany R. Walsh • Editors Bio-Inspired Nanotechnology From Surface Analysis to Applications 123 Editors Marc R. Knecht Tiffany R.Walsh Department of Chemistry InstituteforFrontier Materials Universityof Miami Deakin University CoralGables, FL Geelong,VIC USA Australia ISBN 978-1-4614-9445-4 ISBN 978-1-4614-9446-1 (eBook) DOI 10.1007/978-1-4614-9446-1 Springer New YorkHeidelberg Dordrecht London LibraryofCongressControlNumber:2014936425 (cid:2)SpringerScience+BusinessMediaNewYork2014 Thisworkissubjecttocopyright.AllrightsarereservedbythePublisher,whetherthewholeorpartof the material is concerned, specifically the rights of translation, reprinting, reuse of illustrations, recitation,broadcasting,reproductiononmicrofilmsorinanyotherphysicalway,andtransmissionor informationstorageandretrieval,electronicadaptation,computersoftware,orbysimilarordissimilar methodology now known or hereafter developed. Exempted from this legal reservation are brief excerpts in connection with reviews or scholarly analysis or material supplied specifically for the purposeofbeingenteredandexecutedonacomputersystem,forexclusiveusebythepurchaserofthe work. Duplication of this publication or parts thereof is permitted only under the provisions of theCopyright Law of the Publisher’s location, in its current version, and permission for use must always be obtained from Springer. Permissions for use may be obtained through RightsLink at the CopyrightClearanceCenter.ViolationsareliabletoprosecutionundertherespectiveCopyrightLaw. The use of general descriptive names, registered names, trademarks, service marks, etc. in this publicationdoesnotimply,evenintheabsenceofaspecificstatement,thatsuchnamesareexempt fromtherelevantprotectivelawsandregulationsandthereforefreeforgeneraluse. While the advice and information in this book are believed to be true and accurate at the date of publication,neithertheauthorsnortheeditorsnorthepublishercanacceptanylegalresponsibilityfor anyerrorsoromissionsthatmaybemade.Thepublishermakesnowarranty,expressorimplied,with respecttothematerialcontainedherein. Printedonacid-freepaper SpringerispartofSpringerScience+BusinessMedia(www.springer.com) Preface The research encompassing the screening, selection, characterization, and exploitationofpeptidescapableofrecognizingandbindinginorganicmaterials is rapidly growing; however, it remains far from maturity. In the space of two decades, this area has exploded with activity, driving innovations in both the experimental and theory arenas. With the strong encouragement of the team at Springer,weconsideredthisanidealpointtoreflectontheenormousprogressthat has been made thus far, to consolidate these accomplishments, and to highlight some of the new applications and research directions emerging in this new field. Oneofthekeyaudiencesforthisbookisthescientistorscholarwhoisnewto theresearcharea.Theinherentlymultidisciplinarynatureofthisresearchfieldthat embraces chemistry, physics, surface science, structural and molecular biology, genetics, materials science, computational modeling, and informatics, makes a comprehensive entry a challenging prospect. The earlier chapters of this book detailthefoundationalaspectsofthisscientificfield,toassistthosegettingstarted. Anotherkeyaudienceforthisvolumeistheestablishedpractitionerinbio-inspired technologies, who is interested in expanding the horizons of the possible applications of their research. The latter chapters in this volume highlight applications that are currently emerging and could potentially have significant opportunities for growth. This includes the expansion of bio-inspired methodol- ogies and applications that could have important implications in sustainability, which is important for future scientific progression. We are grateful to all of our authors for their outstanding contributions. We would also like to thank Merry Stuber, Allison Waldron, and the team at Springer for their hard work, enthusiasm, organization, support, persistence, and patience. And finally, we would like to thank our colleagues, friends, and especially families, for their support and encouragement. Marc R. Knecht Tiffany R. Walsh v Contents 1 Peptide-Nanoparticle Strategies, Interactions, and Challenges . . . 1 Joseph M. Slocik and Rajesh R. Naik 2 Fundamentals of Peptide-Materials Interfaces. . . . . . . . . . . . . . . 17 Tiffany R. Walsh 3 Experimental Characterization of Peptide–Surface Interactions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 37 Marion J. Limo, Carole C. Perry, A. A. Thyparambil, Yang Wei and Robert A. Latour 4 Interfacial Structure Determination . . . . . . . . . . . . . . . . . . . . . . 95 Peter A. Mirau 5 Understanding Biomineral Growth and Assembly for Engineering Novel Green Nanomaterials . . . . . . . . . . . . . . . . 127 Siddharth Patwardhan 6 Understanding Molecular Recognition on Metallic and Oxidic Nanostructures from a Perspective of Computer Simulation and Theory . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 141 Hendrik Heinz 7 Bio-Inspired Nanocatalysis . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 173 Ryan Coppage and Marc R. Knecht 8 Addressable Biological Functionalization of Inorganics: Materials-Selective Fusion Proteins in Bio-nanotechnology. . . . . . 221 Banu Taktak Karaca, Marketa Hnilova and Candan Tamerler vii viii Contents 9 Environmental Interactions of Geo- and Bio-Macromolecules with Nanomaterials . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 257 Navid B. Saleh, Jamie R. Lead, Nirupam Aich, Dipesh Das and Iftheker A. Khan 10 Mimicking Biomineral Systems: What have we Achieved and Where do we go from Here? . . . . . . . . . . . . . . . . . . . . . . . . 291 James J. De Yoreo Chapter 1 Peptide-Nanoparticle Strategies, Interactions, and Challenges Joseph M. Slocik and Rajesh R. Naik Abstract The ability to control and manipulate peptide-nanoparticle interactions is an important goal in achieving biofunctionalized materials with enhanced propertiesandprecisenanostructures foruseinsensing,catalysis,andbiomedical applications.However,currently, there are many challenges toovercome inorder to obtain better design and create these peptide-based functional nanomaterials. These include aneed tobetterourunderstandingofthemechanisms/forces which drive peptide-nanomaterial interactions, improve characterization techniques to probe the peptide-nanoparticle interfaces, to design and identify new nanomate- rial-binding peptides with greater affinities using a combination of advanced combinatorial techniques and next-gen sequencing, and to effectively utilize computational modeling to guide/predict peptide-nanomaterial binding. In this chapter, we describe these technical challenges and highlight recent examples of peptide-nanoparticleinteractions,theirresultantproperties,andhowsomeofthese challenges are being addressed. 1.1 Introduction Naturehasevolvedmoleculesthatpossessfunctionalpropertiesintheformofself- assembly, signaling, sensing, catalysis, motion, and storage. In addition, nature hybridizes materials (organic and inorganic) in order to produce sophisticated structures and materials. This is best exemplified by the biogenesis of multiscale silica exoskeletons of marine diatoms (Fig. 1.1) and the organic-inorganic com- posite material of nacre from molluscs (Skowronski et al. 2007; Dickerson et al. 2008), the highly orchestrated synthesis and assembly of magnetic nanoparticle J.M.Slocik(cid:2)R.R.Naik(&) SoftMatterMaterialsBranch,MaterialsandManufacturingDirectorate,AirForceResearch Lab,Wright-PattersonAirForceBase,DaytonOH45433-7750,USA e-mail:[email protected] M.R.KnechtandT.R.Walsh(eds.),Bio-InspiredNanotechnology, 1 DOI:10.1007/978-1-4614-9446-1_1,(cid:2)SpringerScience+BusinessMediaNewYork2014 2 J.M.SlocikandR.R.Naik Fig.1.1 Biological Inspiration Organisms, such as diatoms, produce minerals of defined compositionandstructureundercellularconditionsandgeneticcontrol(aandb).Anexampleof nature’smasteryofmineralizationisdepictedaboveinaSEMimagesofa(cleaned)silicacell wall (i.e., frustule) grown by the diatom Coscinodiscus granii. (Image by M. B. Dickerson, DiatomculturedbyY.Fang) (NP) chains (Bazylinski et al. 2007), and the formation of self-assembled protein cagesforthestorageofinorganicmaterials(Flennikenetal.2008).Inallofthese cases, nature has created unique biomolecules with specific functions that repre- sents the ultimate paradigm of control, chemical specificity, geometrical comple- mentarity,andassemblyofwell-definednanostructures.Theabilitytoreplicatethe structures and functions of biomolecules with regard to how they assemble and interact with inorganic materials is highly desired for a range of applications in medicine, sensors, and catalysis. With current advancements in nanotechnology, there have been many breakthroughs in using biomolecules to fabricate and/or functionalizeinorganicnanoparticles(NPs)thatexhibitnewmaterialfunctionality when combined with the electronic, optical, and magnetic properties of nanoma- terials(Pelazetal.2012).Todate,theseincludeusingbiomolecules(e.g.,peptides, DNA)forthesynthesisofdifferentmaterials(inorganicandcarbon-based),toalter NP properties and structure, and more importantly, impart biological activity and molecular recognition function tonanomaterials. Peptides and proteins are anintegralpart ofmaterials synthesis,assembly,and functionalization due to their rich chemical variability (hydrophobic/hydrophilic, aromatic, acidic, basic residues), presence of short segments of secondary struc- tural elements (helices, b-sheets, turns), can be synthesized using standard coupling strategies, and available screening methods in place for identifying material-specific peptides from large combinatorial libraries (Briggs and Knecht 2012). These qualities are appealing given that they are easier to control and manipulate as compared to larger proteins, but provide a lot more chemical and structural diversity unlike single amino acids or DNA bases. Also, a common characteristicofmost,ifnotall,proteinswithknownbiomineralizationactivityis the presence of multiple repeating peptide domains (Dickerson et al. 2008). 1 Peptide-NanoparticleStrategies,Interactions,andChallenges 3 This has provided a means to isolate and study the activity of these domains in a singlepeptiderepeatwithoutthecomplexityofthefullproteinstructure.Thiswas first demonstrated by the use of a silica precipitating peptide R5 identified from silaffins contained in diatoms to replicate the biosilification reaction under labo- ratory conditions (Kroger et al. 1999). In addition to biologically derived peptide sequences for the synthesis and assembly of materials, peptides with specific material-binding sequences isolated through combinatorial screening approaches havebeenusedassynthetictemplatestosynthesize,functionalize,andassemblea widevarietyofNPtypes(Songetal.2013;Nametal.2008;Coppageetal.2011). For example, platinum-binding and silica-binding peptides isolated from phage displayed peptide libraries were reported to control the morphology and shape of platinum (Li and Huang 2010) and silica particles (Patwardhan et al. 2012). Peptide-nanoparticle interactions have been exploited for the synthesis and assembly of higher order complex inorganic structures using protein scaffolds or lipid-like molecules. Using protein scaffolds, peptides are locally/spatially arran- ged in a 3-D geometry around the protein to display multiple repeating peptide sequences with NP templating activity. For example, proteins such as b-silk, S-layer proteins from bacteria, chaperonin proteins, viral capsids, and ferritin protein cages have all been modified with functional peptides for materials syn- thesis and in the assembly of unique nanostructure geometries (Coordination Chemistry2013).Theproteinscaffoldalsoimpartsaddedstabilitytothedisplayed peptides, enhanced solubility in aqueous environments, and diminished immuno- genicortoxicityeffectsinregardstotherapeutictreatments;whiletheconjugated peptide modifies the size of the protein scaffold and adds new functionality. The iron storage protein of ferritin is an example of a biologically important protein scaffold which offers these benefits. Notably, ferritin forms a cage-like nano- structurewithexternalandinternaldiametersbeing12 nmand8 nm,respectively, andcontainsnumerousrepeatingresiduesatfivefoldorsixfoldsymmetrysitesfor genetic or chemical addition of peptides (Coordination Chemistry 2013). As a result,thereismuchinterestinferritinfornotonlyatherapeuticusebutalsoasa scaffold for biomaterial applications. We have previously shown that self-assem- bledferritincagescanbegeneratedthroughengineeringrecombinanthumanlight chainferritinwithasilver-bindingpeptide(Krameretal.2004).Consequently,the peptide modified ferritin allowed for inorganic NP growth of silver within the interior protein cavity and only at the sites where peptides were displayed. Interestingly, bacterial cells that expressed protein cages with silver-binding peptide were resistant to increased concentrations of Ag+ ions. Modified ferritin can also be assembled on the surface of aluminum NPs to generate bio-thermite materialswithenhancedkineticandenergeticproperties(Slociketal.2013).Also, peptides have been conjugated with amphiphilic molecules in the form of short carbon chains (C ) for the self-assembly of new peptide-gold nanostructures. In 12 recent studies by Rosi and coworkers, scaffolds of gold-binding peptide-based conjugates were created through rational design principles for the preparation of complexplasmonicmaterialswithtailorableopticalproperties(Chenetal.2008). Theuseofpeptidesallowedformanipulatingthehelicalcontentinthescaffoldto

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