Self-Assembly of Synthetic and Biological Polymeric Systems of ...

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(54) Almeida, N. L.; Oliveira, C. L. P.; Torriani, I. L.; Loh, W. Calorimetric and Structural Investigation of the Interaction of Lysozyme and Bovine Serum Albumin with Poly(Ethylene Oxide) and its Copolymers. Colloids Surf., B 2004, 38,67–76. (55) Dutta, P.; Manivannan, A.; Seehra, M. S.; Shah, N.; Huffman, G. P. Magnetic Properties of Nearly Defect-Free Maghemite Nanocrystals. Phys. Rev. B 2004, 70, 174428/1–174428/7. (56) Shiomi, T.; Tsunoda, T.; Kawai, A.; Mizukami, F.; Sakaguchi, K. Biomimetic Synthesis of Lysozyme-Silica Hybrid Hollow Particles Using Sonochemical Treatment: Influence of pH and Lysozyme Concentration on Morphology. Chem. Mater. 2007, 19, 4486–4493. (57) Schrinner, M.; Ballauff, M.; Talmon, Y.; Kauffmann, Y.; Thun, J.; Moller, M.; Breu, J. Dynamical Quorum Sensing and Synchronization in Large Populations of Chemical Oscillators. Science 2009, 323, 617–620. (58) Qin, G.; W. Pei, W.; Ma, X.; Xu, X.; Ren, Y.; Sun, W.; Zuo, L. Enhanced Catalytic Activity of Pt Nanomaterials: From Monodisperse Nanoparticles to Self-Organized Nanoparticle-Linked Nanowires. J. Phys. Chem. C 2010, 114, 6909– 6913. (59) Hayakawa, K.; Yoshimura, T.; Esumi, K. Preparation of Gold- Dendrimer Nanocomposites by Laser Irradiation and Their Catalytic Reduction of 4-Nitrophenol, Immobilization and Recovery of Au Nanoparticles from Anion Exchange Resin: Resin-Bound Nanoparticle Matrix as a Catalyst for the Reduction of 4-Nitrophenol. Langmuir 2003, 19, 5517–5521. (60) Praharaj, S.; Nath, S.; Gosh, S. K.; Kundu, S.; Pal, T. Immobilization and Recovery of Au Nanoparticles from Anion Exchange Resin: Resin-Bound Nanoparticle Matrix as a Catalyst for the Reduction of 4-Nitrophenol. Langmuir 2004, 20, 9889–9892. (61) Rashid, M. H.; Bhattacharjee, R. R.; Kotal, A.; Mandal, T. K. Synthesis of Spongy Gold Nanocrystals with Pronounced Catalytic Activities. Langmuir 2006, 22, 7141–7143. (62) Rashid, M. H.; Mandal, T. K. Organic Ligand-Mediated Synthesis of Shape-Tunable Gold Nanoparticles: An Application of Their Thin Film as Refractive Index Sensors. J. Phys. Chem. C 2007, 111, 9684–9693. (63) Esumi, K.; Isono, R.; Yoshimura, T. Preparation of PAMAMand PPI-Metal (Silver, Platinum, and Palladium) Nanocomposites and Their Catalytic Activities for Reduction of 4-Nitrophenol. Langmuir 2004, 20, 237–243. (64) Liu, J.; Qin, G.; Raavendran, P.; Ikushima, Y. Facile “Green” Synthesis, Characterization, and Catalytic Function of β-D- Glucose-Stabilized Au Nanocrystals. Chem.;Eur. J. 2006, 12, 2131–2138. (65) Chen, X.; Zhao, D.; An, Y.; Shi, L.; Hou, W.; Chen, L. Catalytic Properties of Gold Nanoparticles Immobilized on the Surfaces of Nanocarriers. J. Nanopart. Res. 2010, 12, 1877–1887. (66) Li, L.; Wang, Z.; Huang, T.; Xie, J.; Qin, L. Porous Gold Nanobelts Templated by Metal-Surfactant Complex Nanobelts. Langmuir 2010, 26, 12330–12335. (67) Bai, X.; Gao, Y.; Liu, H.-g.; Zheng, L. Synthesis of Amphiphilic Ionic Liquids Terminated Gold Nanorods and Their Superior Catalytic Activity for the Reduction of Nitro Compounds. J. Phys. Chem. C 2009, 113, 17730–17736. (68) Wang, Y.; Wei, G.; Zhang, W.; Jiang, X.; Zheng, P.; Shi, L.; Dong, A. Responsive Catalysis of Thermoresponsive Micelle- Supported Gold Nanoparticles. J. Mol. Catal. A: Chem. 2007, 266, 233–238. (69) Chen, X.; An, Y.; Zhao, D.; He, Z.; Zhang, Y.; Cheng, J.; Shi, L. Core-Shell-Corona Au-Micelle Composites with a Tunable Smart Hybrid Shell. Langmuir 2008, 24, 8198–8204. pubs.acs.org/JPCL (70) Hain, J.; Schrinner, M.; Lu, Y.; Pich, A. Design of Multicomponent Microgels by Selective Deposition of Nanomaterials. Small 2008, 4, 2016–2024. (71) Huang, T.; Meng, F.; Qi, L. Facile Synthesis and One-Dimensional Assembly of Cyclodextrin-Capped Gold Nanoparticles and Their Applications in Catalysis and Surface-Enhanced Raman Scattering. J. Phys. Chem. C 2009, 113, 13636–13642. (72) Lee, J.; Park, L. C.; Song, H. A Nanoreactor Framework of a Au@SiO 2 Yolk/Shell Structure for Catalytic Reduction of p-Nitrophenol. Adv. Mater. 2008, 20, 1523–1528. (73) Rashid, M. H.; Mandal, T. K. Templateless Synthesis of Polygonal Gold Nanoparticles: An Unsupported and Reusable Catalyst with Superior Activity. Adv. Funct. Mater. 2008, 18, 2261–2271. (74) Kumar, S. S.; Kumar, C. S.; Mathiyarasu, J.; Phani, K. L. Stabilized Gold Nanoparticles by Reduction Using 3,4-Ethylenedioxythiophene-polystyrenesulfonate in Aqueous Solutions: Nanocomposite Formation, Stability, and Application in Catalysis. Langmuir 2007, 23, 3401–3408. (75) Burda, C.; Chen, X.; Narayanan, R.; El-Sayed, M. A. Chemistry and Properties of Nanocrystals of Different Shapes. Chem. Rev. 2005, 105, 1025–1102. (76) Knubovets, T.; Osterhout, J. J.; Connolly, P. J.; Klibanov, A. M. Structure, Thermostability, And Conformational Flexibility of Hen Egg-White Lysozyme Dissolved in Glycerol. Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 1262–1267. r XXXX American Chemical Society 2687 DOI: 10.1021/jz101029f |J. Phys. Chem. Lett. 2010, 1, 2680–2687 206
DOI: 10.1002/chem.201003679 One-Dimensional Magnetic Nanowires Obtained by Protein Fibril Biotemplating JosuØ Juµrez, Adriana Cambón, Antonio Topete, Pablo Taboada,* and Víctor Mosquera [a] Abstract: Magnetic nanowires were obtained through the in situ synthesis of magnetic material by Fe-controlled nanoprecipitation in the presence of two different protein (human serum albumin (HSA) and lysozyme (Lys)) fibrils as biotemplating agents. The structural characteristics of the biotemplates were transferred to the hybrid magnetic wires. They exhibited excel- Introduction A key issue in nanotechnology is the development of conceptually simple construction techniques for the mass fabrication of identical nanoscale structures. Interest in one-dimensional (1D) nanoscale materials and devices, often called nanowires, nanotubes or nanorods, has risen sharply in recent years. In particular, 1D magnetic nanostructures exhibit unique magnetic properties due to geometric confinement, magnetostatic interactions and nanoscale domain formation, [1] which endow them with potential applicability in data storage and logic devices, [2a] magneto-transport behaviour, [2b] micromechanical sensors [2c] and biomedicine. [2d] As a result of their high aspect ratios, 1D magnetic entities possess larger dipole moments than individual nanoparticles. This allows their manipulation with lower field strengths [3] and provides them with improved imaging contrast capabilities, which opens up the possibility of their use in new biomedical applications, specifically in the advent of low-field MRI. [4] Here we report the formation of 1D magnetic nanowires and assemblies of magnetic nanoparticles over linear nanosized biopolymer templates formed by spontaneous fibrillation, under suitable conditions, of two proteins— human serum albumin (HSA) and lysozyme (Lys)—by in situ co-precipitation of iron under suitable conditions. These [a] J. Juµrez, A. Cambón, A. Topete, P. Taboada, V. Mosquera Grupo de Física de Coloides y Polímeros Departamento de Física de la Materia Condensada Facultad de Física, Universidad de Santiago de Compostela 15782 Santiago de Compostela (Spain) Fax: (+ 34) 881814112 E-mail: pablo.taboada@usc.es Supporting information for this article is available on the WWW under http://dx.doi.org/10.1002/chem.201003679. 7366 lent magnetic properties as a consequence of the 1D assembly and fusion of magnetite nanoparticles as ascertained by SQUID magnetometry. Prompted by these findings, we also Keywords: biotemplating · imaging agents · magnetic nanowires · nanostructures · protein fibrils checked their potential applicability as MRI contrast agents. The magnetic wires exhibited large r 2* relaxivities and sufficient contrast resolution even in the presence of an extremely small amount of Fe in the magnetic hybrids, which would potentially enable their use as T 2 contrast imaging agents. magnetic 1D nanostructures possess both high saturation magnetisations and spin–spin relaxivities at low magnetic fields, which makes them suitable candidates for use as imaging contrast agents in MRI. There are many literature reports on the fabrication of 1D magnetic nanostructures, which can be assembled by (bio)templating, spontaneous self-assembly by magnetic dipolar interactions of nanoparticles, chemical synthesis, lithographic methods, laser etching or microcontact printing. [5] Owing to its relative simplicity, template-directed synthesis is one of the most attractive methods for preparing magnetic 1D nanomaterials. [5a,b] This approach offers exciting alternatives to the costly nanolithography-based “top-down” technologies or multi-step chemical procedures. Various linear nanometer-scale materials, including molecular dispersed and assembled polymers, [6] carbon nanotubes [5a,7] or biological scaffolds, have been employed to prepare 1D magnetic structures and assemblies. [8] In particular, the capability of biopolymers to generate 1D magnetic nanostructures is really exciting because nature provides a renewable and highly diverse source of nanometer-scale ordered complexes that can be used to replicate inorganic materials as well-defined structures. [9] Dextran, for example, has been used in the creation of elongated assemblies of spherical nanoparticles suitable for use as MRI contrast agents and tumour targeting species. [2d, 10] DNA was also used as a stabiliser for the formation of ordered nanowires of magnetic nanoparticles. [2b, 11] These nanowire assemblies resulted in stable magnetic fluids with high relaxivities at low fields useful for MRI imaging. The protein cage of cowpea chlorotic mottle virus (CCMV) was explored with the same goal, to incorporate high payloads of Gd 3+ with elevated molecular relaxivities, [12] and the formation either of magnetic nanotubes or of magnetic nanowires with the aid of magnetic bacteria (Mag- 2011 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim Chem. Eur. J. 2011, 17, 7366 – 7373
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Grupo de Física de Coloides y Pol
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Agradecimientos A mi Familia A mi P
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v List of papers I. Self-assembly p
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2.3 2.4 2.5 2.6 2.7 2.8 2.9 2.10 2.
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5.4 5.5 5.3.2 5.5.1 Chapter 6 Kinet
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amiloides de la proteína albúmina
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vesiculares son el resultado de la
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origina debido a condiciones ambien
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con las fibras vecinas más cercana
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Abstract In the present work, we in
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[Au]/[protein] molar ratio and numb
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synthetic polymers are obtained fro
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On the other hand, in terms of chem
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Additionally, to obtain a better kn
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therefore, characteristic of solid
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presence of electrostatic charge in
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Contents 2.1 2.2 2.3 2.4 2.5 2.6 2.
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where w is the meniscus’ weight d
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that they exert little force one on
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This oscillating dipole acts as an
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(APD) and its associated optics (pi
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where r is the distance of the dipo
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When , the former equation can be s
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autocorrelation function (ACF). In
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and, therefore, . The autocorrelati
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A transmission electron microscope
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2.5.- Atomic force microscopy (AFM)
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ecause of the energy loss in the ex
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Figure 2.15. Schematic representati
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ackbone of proteins. Since proteins
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According to classical mechanics, t
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chemical composition, configuration
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2.9.1.- Viscoelasticity Many materi
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where is the total strain rate, whi
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Using equations 2.40 and 2.41 in eq
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scattering process that incoming X-
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maximum intensity of the peak, Imax
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translation of the reciprocal latti
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For a single crystal, the chance to
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excitation; namely, a valance elect
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Figure 2.27. Distinction between si
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microscope, there are two polarized
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In particular, we use SQUID to meas
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are aligned by means of an external
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on the digital profile of a drop im
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Laser confocal microscopy. Confocal
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Fluorescence spectroscopy. Fluoresc
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Superconducting quantum interferenc
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temperatures, the chains are mixed
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e detected by a given method. Therm
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subsequently, of their thermodynami
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a) O b) H 2C CH 2 O H 2C CH Figure
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Contents 4.1 4.2 4.3 4.3.1 CHAPTER
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7108 Langmuir, Vol. 24, No. 14, 200
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7112 Langmuir, Vol. 24, No. 14, 200
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7114 Langmuir, Vol. 24, No. 14, 200
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7116 Langmuir, Vol. 24, No. 14, 200
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15704 J. Phys. Chem. C, Vol. 114, N
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4.3.1.- Relevant aspects I. For E12
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Contents 5.1 5.2 5.3 5.4 5.5 5.1.1
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acids whose lateral side chains cha
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adjacent segments of an antiparalle
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5.2.1.- Unfolded state Over the las
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5.2.4.- Energy landscape: protein a
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molecular medicine viewpoint, prote
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shows the typical nucleation-depend
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the energy landscape of the aggrega
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exposed loop region. The secondary
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Biophysical Journal Volume 96 March
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Fibrillation Pathway of HSA 2355 q
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Fibrillation Pathway of HSA 2357 mo
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Fibrillation Pathway of HSA 2359 in
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Page 179 and 180: Influence of Electrostatic Interact
Page 181 and 182: Fibrillation Process of Human Serum
Page 187: Fibrillation Process of Human Serum
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Page 199 and 200: 5 10 15 20 25 30 35 40 45 Soft Matt
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Page 211: 5 65. L. A. Sikkink, M. Ramirez-Alv
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Page 216: pubs.acs.org/JPCL Figure 3. (a) Tim
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Page 230 and 231: temperatures, and solvent polarity.
Page 233 and 234: Conclusions The work has two parts:
Page 235 and 236: equire a highly organized and unsta
Page 237 and 238: References 1. Hiemenz, Paul C. Poly
Page 239 and 240: 33. Wang, Z. L. HANDBOOK OF MICROSC
Page 241 and 242: 67. Polymers Get Organized. Bucknal
Page 243 and 244: 94. Are there Pathways for Protein
Page 245 and 246: 123. Designing conditions for in vi
Page 247: 151. SERS-based diagnosis and biode
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