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

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Conclusions The work has two parts: The first one was focused on the characterization of three block copolymers (EO12SO10, EO10SO10EO10, and EO137SO18EO137), meanwhile the second part was dedicated to the study of the fibrillation of the protein human serum albumin that was cover with gold and magnetic nanoparticles. The general conclusions are: 1. - Characterization of the block copolymers EO12SO10, EO10SO10EO10, y EO137SO18EO137, in solution at the air/water and chloroform/water interfaces. I. For E12S10 dilute solutions, the coexistence of spherical micelles with vesicular structures has been observed. In addition, the spontaneous formation of vesicles by poly(oxystyrene)-poly(oxyethylene) block copolymers is reported for the first time, as confirmed by light scattering, polarized light microscopy, and transmission and cryo- scanning electron microscopy data. II. In dilute solution, the self-assembly of copolymer E10S10E10 leads to the formation of elongated micelles as supported by light scattering and transmission electron techniques. III. In the case of copolymer E137S18E137, typical spherical micelles are observed. Tube inversion and rheological measurements were used to define the sol- soft- and gel- hard boundaries of this copolymer. IV. E12S10 and E10S10E10 copolymers did not form gels in the concentration range analysed. However, only certain concentrations of copolymer E10S10E10 were analysed by rheometry. From experimental data, an upturn in the low-frequency range of the stress moduli was observed, denoting the existence of an emerging slow process, which was assigned to the formation of an elastic network. V. Block copolymers E12S10, E10S10E10 and E137S18E137 showed spontaneous adsorption at the air-water interface, which slowed down when the hydrophobicity of the molecule was increased. In contrast, at the chloroform/water interface no measurable effect is observed for copolymer E12S10 due to the slow diffusion of its chains to the interface in 219
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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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7110 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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Fibrillation Pathway of HSA 2361 Fu
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Fibrillation Pathway of HSA 2363 FI
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Fibrillation Pathway of HSA 2365 Wh
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Fibrillation Pathway of HSA 2367 of
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Fibrillation Pathway of HSA 2369 17
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Influence of Electrostatic Interact
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Page 242 and 243: Nelson, Alshakim ; Meijer, E. W.; Y
Page 244 and 245: 109. Unraveling the Mysteries of Pr
Page 246 and 247: 136. Dilatational Rheology of BSA C
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