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

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12398 J. Phys. Chem. B, Vol. 113, No. 36, 2009 Juárez et al. albumin under different solution conditions: spherulites and fibrillar gels. Under conditions where amyloid-like fibrils for this protein were previously detected, that is, upon incubation at 65 °C at both acidic and physiological pH in the presence of different amounts of added electrolyte, spherulite formation was detected. Within spherulites, fibrils display a radial arrangement around a disoganized protein core with sizes of several micrometers, as revealed by POM and confocal microscopy. The spherulites are detected both in solution and embedded in an isotropic matrix of a fibrillar gel. Upon extensive incubation under increasingly added electrolyte and/ or protein concentration, gels are formed. Under conditions where the protein is electrically charged, fibrillar gels were observed. In contrast, at a pH close to the protein isolectric point, particulate gels were observed. Fibrillar gels are formed through intermolecular nonspecific association of amyloid fibrils at a pH far away from the isolectric point of the protein, as observed by TEM, AFM, and ATR-FTIR. For these types of gels, the protein molecules seem to display a “solid-like” behavior due to the existence of non-DLVO intermolecular repulsive forces, as observed by rheometry. As the solution ionic strength increases, a coarsening of this type of gels is observed as seen by AFM, with a decrease in the elastic response. In contrast, at pH 5.5, particulate gels are present as a consequence of a faster protein aggregation which does not allow the necessary structural reorganization to enable the formation of more ordered structures such as fibrils, as observed by their shorter gelation times and the frequencydependent behavior of the loss modulus. On the other hand, the formation of particulate gels with HSA also confirms the possibility that this type of structure may be a generic property of the polypeptide chains under suitable solution conditions. Acknowledgment. Authors thank Ministerio de Educación y Ciencia by project MAT-2007-61604 and Xunta de Galicia for financial support. Supporting Information Available: XRD fibril diffraction pattern and TEM pictures of mature fibrils. This material is available free of charge via the Internet at http://pubs.acs.org. References and Notes (1) Hady, J.; Selkoe, D. Science 2002, 297, 353–356. (2) Dobson, C. M. Nature 2003, 426, 884–890. (3) Stefani, M.; Dobson, C. M. J. Mol. Med. 2003, 81, 678–699. (4) Lansbury, P. T., Jr. Nat. Med. 2004, 10, 13709–13715. (5) Mattson, M. P. Nature 2004, 430, 631–639. (6) Soto, C.; Estrada, L.; Castilla, J. Trends Biochem. Sci. 2006, 31, 150–155. 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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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Page 233 and 234: Conclusions The work has two parts:
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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
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151. SERS-based diagnosis and biode
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