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Tesi sul tema "Fibrils"

Autore: Grafiati

Pubblicato: 4 giugno 2021

Ultima modifica: 26 luglio 2025

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1

Hernandez, Zurine. "Conditions required for spinning continuous fibres from cellulose nano-fibrils." Thesis, Edinburgh Napier University, 2012. http://researchrepository.napier.ac.uk/Output/5286.

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The thesis describes a programme of work to develop a novel cellulose based fibre. The most important innovative step in this work lies in the manufacture of the fibre from a chiral nematic suspension of plant based cellulose nano-fibrils. In the course of the project a number of key steps have been addressed in the development process. These included: • Developing a method for extraction of nano-fibrils from wood and cotton based pulp and filter paper; • Development of concentrated chiral nematic suspensions of the nano-fibrils suitable for extrusion (spinning); • Spinning a continuous fibre

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2

Rao, Shiva Priya. "Amyloid Fibrils in Bionanomaterials." Thesis, University of Canterbury. Biological Sciences, 2008. http://hdl.handle.net/10092/4415.

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Abstract (sommario):

Amyloid fibrils are a type of protein nanofibres that form when a normally soluble protein aggregates in a regular fashion via self-association. Their organised and repetitive β-sheet structure is thought to be a generic property of all proteins, depending on the environmental conditions. The nanometre size and high stability of these protein nanofibres are attractive features to exploit in bionanomaterials. This thesis aimed to manipulate insulin amyloid fibrils, as a model protein nanofibre system, through investigating the effect of chemical modification on insulin fibril formation in het

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3

Krebs, Mark R. H. "The chemical mystery of amyloid fibrils : hen lysozyme fibrils, seeding and cross-seeding." Thesis, University of Oxford, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.249542.

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4

Smith, Jeffrey F. "Biophysical properties of amyloid fibrils." Thesis, University of Cambridge, 2006. https://www.repository.cam.ac.uk/handle/1810/251999.

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5

Hellewell, Andrew Leslie. "The cytoxocity of amyloid fibrils." Thesis, University of Leeds, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.581878.

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Abstract (sommario):

Amyloid assemblies consist of an organised cross ~-sheet structure and can be formed by many proteins or peptides regardless of peptide sequence. Amyloid has been utilised by many species for a variety of functions, however, inappropriate amyloid formation is associated with a spectrum of devastating amyloid diseases. The nature of the primary cytotoxic species in amyloid disease is widely debated, with the consensus favouring pre-fibrillar, oligomeric entities over mature end-stage fibrils, despite an increasing body of evidence that suggest at least some fibrils may be associated with cytoto

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6

Gras, Sally Louise. "Functionalised amyloid fibrils for bionanotechnology." Thesis, University of Cambridge, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.614046.

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7

Povilonienė, Simona. "Investigation of amyloid fibrils forming proteins." Doctoral thesis, Lithuanian Academic Libraries Network (LABT), 2011. http://vddb.laba.lt/obj/LT-eLABa-0001:E.02~2011~D_20110607_092528-21563.

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Abstract (sommario):

Self-assembly of biomolecules into beta-sheet structures can be applied in the creation of nano-materials with novel electrical, optical, catalytical, or/and mechanical characteristics. This work was directed towards the construction of nano-derivatives based on amyloid fibrils forming proteins (Abeta40 peptide, a-Synuclein (a-Syn), equine lysozyme (EL)). Such nanostructures can be used to produce nanoscale functional systems. Herein, different mutant and hybrid proteins, which were able to form fibrillar structures, were constructed and the properties of fibrils were investigated. Designed cy

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8

Potter, Richard J. "Scrapie associated fibrils and polymeric PrP." Thesis, University of Leicester, 1998. http://hdl.handle.net/2381/29628.

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The conversion of PrPC, the normal form of the prion protein, to PrPSc, the protease-resistant disease specific form, is central to the pathogenesis of the transmissible spongiform encephalopathies. The mechanism underlying this conformational change remains elusive but the demonstration that PrPSc can infer protease-resistance to PrPc in-vitro in the presence of guanidine hydrochloride using a cell-free system offers a useful approach to investigating this process. The limitations of such systems however are that significant efficiencies of conversion are only observed in the presence of an e

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9

Rogers, Salman Samson. "Some physical properties of amyloid fibrils." Thesis, University of Cambridge, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.613906.

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10

剛貴, 田中, and Goki Tanaka. "Structural polymorphism of alpha-synuclein fibrils." Thesis, https://doors.doshisha.ac.jp/opac/opac_link/bibid/BB13115616/?lang=0, 2019. https://doors.doshisha.ac.jp/opac/opac_link/bibid/BB13115616/?lang=0.

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11

Gilpin, Christopher James. "Three-dimensional reconstruction of collagen fibrils." Thesis, University of Manchester, 2001. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.488036.

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12

Rodriguez, Jose. "Polarised vibrational spectroscopy on aligned amyloid fibrils." Thesis, University of Reading, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.542270.

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13

Baldwin, A. J. "Solution-state NMR studies of amyloid fibrils." Thesis, University of Cambridge, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.596307.

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Abstract (sommario):

In this thesis, a protein is designed incorporating an electron transport protein that self-assembles into amyloid fibrils in order to investigate the possibility of producing self-assembling bio-electronic conductors. These fibrils are found to display the electron transport protein and as a consequence, exchange electrons with their surroundings. The effects of non beta-sheet core regions on the properties of amyloid fibrils have been studied. In particular it is shown that non-core regions have sufficient flexibility to average their local magnetic environments to yield sharp resonances whe

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14

Pilkington, Sarah. "Incorporating glucose oxidase activity into amyloid fibrils." Thesis, University of Canterbury. School of Biological Sciences, 2009. http://hdl.handle.net/10092/4435.

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Abstract (sommario):

Amyloid fibrils are a misfolded state formed by many proteins when subjected to denaturing conditions. Their constituent amino acids make them an excellent target for enzyme immobilisation and their strength, stability and nanometre size are attractive features for exploitation in the creation of new bionanomaterials. The aim of this thesis was to functionalise amyloid fibrils by conjugation to glucose oxidase (GOD). GOD is a relatively stable glycoprotein that catalyses the oxidation of glucose and the release of hydrogen peroxide. The consumption of glucose can be measured to assess glucose

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15

Domigan, Laura Joy. "New nanomaterials: amyloid fibrils from waste proteins." Thesis, University of Canterbury. School of Biological Sciences, 2012. http://hdl.handle.net/10092/6718.

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Abstract (sommario):

The current landscape of nanotechnology has focussed attention on materials that self-assemble. The search for such materials has unsurprisingly led to the biological world, where functional nanoscale biomolecular assemblies are in abundance. Amyloid fibrils are one such self-assembling biological structure, formed when native proteins misfold into insoluble fibrous quaternary structures. This research has explored the use of amyloid fibrils formed from waste proteins, namely crude crystallin proteins from fish eye lenses, as biological nanowires. The use of amyloid fibrils as nanowires was in

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16

Wenger, M. P. "Mechanical and structural properties of collagen fibrils." Thesis, University College London (University of London), 2009. http://discovery.ucl.ac.uk/18736/.

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There is a fundamental need for techniques that are capable of determining the mechanical properties of biological fibrils at the nanoscale. This is because of the direct relationship between structure and function of an organism and the mechanical properties of its building blocks. Collagen, for example, which is the most abundant protein in mammals, is best known as the principal tensile element providing the mechanical structure to our bodies. Although collagen has been investigated intensively in the last decades, relatively little is known about its mechanics and inner structure. In this

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17

Jakhria, Toral Chandulal. "Amyloid fibrils are nanoparticles that target lysosomes." Thesis, University of Leeds, 2014. http://etheses.whiterose.ac.uk/7628/.

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Abstract (sommario):

The amyloidoses are a group of debilitating disorders which include neurodegenerative diseases such as Alzheimer’s disease and systemic diseases such as dialysis-related amyloidosis (DRA). Amyloidoses are associated with the aggregation of proteins into amyloid fibrils with a highly organised cross-β structure. Amyloid fibrils are formed by a variety of proteins and peptides despite differences in sequence and native structure. Amyloid formation occurs by a nucleated growth mechanism and proceeds via oligomeric intermediates into mature fibrils. Despite intense research, the molecular mechanis

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18

MONDANI, VALENTINA. "Molecular and thermodynamic characterization of amyloid fibrils." Doctoral thesis, Università degli studi di Pavia, 2022. https://hdl.handle.net/11571/1468345.

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19

MONDANI, VALENTINA. "Molecular and thermodynamic characterization of amyloid fibrils." Doctoral thesis, Università degli studi di Pavia, 2022. https://hdl.handle.net/11571/1468341.

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20

Sharma, Carrie-anne. "Elucidating the topology of cystatin B amyloid fibrils." Thesis, University of Sheffield, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.527226.

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21

Essex, Rosemary Jane. "Photophysical processes in organic semiconductors and amyloid fibrils." Thesis, University of Cambridge, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.598863.

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This thesis is concerned with the photophysics of organic materials and intermolecular order of guest dyes in self-assembled protein structures. Photophysical processes in polyfluorenes and iridium-containing polyfluorenes copolymer complexes were investigated. Interchain singlet energy transfer processes were investigated by studying the copolymers in various concentrations in a polystyrene matrix. The amount of polyfluorenes in the co-polymers was also varied so that intrachain energy transfer processes could be studied. The singlet exciton decays were fitted to a stretched exponential funct

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22

Fitzpatrick, Anthony William Paul. "The structure and physical properties of amyloid fibrils." Thesis, University of Cambridge, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.599062.

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Abstract (sommario):

Amyloid fibrils are associated with a range of highly debilitating neurological disorders including Alzheimer’s disease, Parkinson’s disease and the spongiform encephalopathies. These structures are formed by the misfolding and self-assembly of peptides and proteins varying widely in sequence and in native conformation. Here we combine experimental measurements derived from sold-state NMR, X-ray fibre diffraction and Atomic Force Microscopy to determine the complex, higher order protofilament structure adopted by an 11-amino acid peptide fragment of the human plasma protein transthyretin, TTR<

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23

Raynes, Jared Kenneth. "Immobilising biomolecules on amyloid fibrils for biotechnology applications." Thesis, University of Canterbury. Biological Sciences, 2012. http://hdl.handle.net/10092/6925.

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Abstract (sommario):

Amyloid fibrils are an insoluble, highly ordered, fibrous protein structure, which have increasingly been recognised as having bionanotechnology applications. Their ability to selfassemble allows a bottom-up approach to material design. Their nanometre dimensions affords them a high surface-to-volume ratio and their proteinaceous building blocks from which they are assembled allow for decoration with biomolecules and chemicals through amino acid residues. Amyloid fibrils are therefore a potential nanoscaffold for immobilisation of biomolecules. Immobilisation offers a solution to the problems

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24

Guttenplan, Alexander Pandias Margaronis. "Smart nanomaterials from repeat proteins and amyloid fibrils." Thesis, University of Cambridge, 2018. https://www.repository.cam.ac.uk/handle/1810/273185.

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Abstract (sommario):

Protein-based materials are an important area of research for various reasons. Natural protein materials such as spider silk have mechanical properties which compare favourably to artificial or inorganic materials, and in addition are biodegradable and can be produced from easily available feedstocks. It is also possible to produce materials that incorporate the functionality of a natural protein, such as ligand-binding or catalysis of reactions, thus allowing this functionality to be used in the solid rather than solution phase. Two particularly interesting components for protein-based materi

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25

FARRIS, FRANCESCO. "AMYLOID FIBRILS INDUCE GLYCOCALYX MEDIATED MECHANOTRANSDUCTION IN MELANOMA." Doctoral thesis, Università degli Studi di Milano, 2022. https://hdl.handle.net/2434/946381.

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PMEL is an amyloidogenic protein found overexpressed in melanoma compared to healthy skin. PMEL expression correlates with unfavorable prognosis, but the mechanism beyond the adverse disease outcome is still unknown. Recently, our lab established a link between the presence of PMEL amyloid fibrils in the metastatic melanoma secretome and YAP activation, driving cancer proliferation and drug resistance. In this study, we show that PMEL amyloid fibrils, secreted by cancer cells, are component of the extracellular matrix and modify its stiffness thus activating mechanosignalling. We highlight

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26

Herranz-Trillo, Fatima. "Disentangling structural complexity in proteins by decomposing SAXS data with chemometric approaches." Thesis, Montpellier, 2017. http://www.theses.fr/2017MONTT044/document.

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De nombreux systèmes biologiques sont intrinsèquement polydispersés, présentant de multiples espèces coexistantes, de taille, de forme ou de conformation différentes (c'est-à-dire, mélanges oligomèriques, des complexes faiblement liés se dissociant en composantes individuelles ou des espèces apparaissant lors de processus amyloïdogéniques). L'étude de tels systèmes complexes est une tâche difficile en raison de l'instabilité des espèces concernées, de leurs concentrations relatives faibles et interdépendantes et des difficultés rencontrées pour l'isolation des composantes pures. Dans cette thè

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27

Ito, Keita. "Movement-induced orientation of collagen fibrils in cartilaginous tissues." Thesis, Massachusetts Institute of Technology, 1994. http://hdl.handle.net/1721.1/28066.

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28

Caporini, Marc Anthony. "Structural studies of amyloid fibrils using solid-state NMR." Thesis, Massachusetts Institute of Technology, 2008. http://hdl.handle.net/1721.1/46038.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2008.<br>Vita.<br>Includes bibliographical references.<br>he development of solid-state NMR techniques and application to amyloid fibrils are presented. In addition, a new method of selective inversion based on chemical shift anisotropy is presented. An improved method for highly accurate distance measurement across parallel [beta]-sheets in amyloid fibrils has been developed. This method combines the a double quantum filtered version of the dipolar recoupling sequence DRAWS with the simulation and data fitting program

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29

Shammas, Sarah Lucy. "Factors affecting the aggregation and disaggregation of amyloid fibrils." Thesis, University of Cambridge, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.608875.

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30

Krishnashenoy, Padmabai Jayakrishna Shenoy. "Structural characterization of amyloid fibrils by solid-state NMR." Thesis, Bordeaux, 2020. http://www.theses.fr/2020BORD0245.

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Projet 1- Dissection structurelle de fibrilles amyloïdes de différentes constructions TDP-43 par RMN à l'état solide. La protéine de liaison à l'ADN TAR de 43 kDa (TDP-43) est observée comme le principal composant des inclusions cytoplasmiques des cellules de patients souffrants de la sclérose latérale amyotrophique (SLA) et de la démence lobaire frontotemporale (DLF). La protéine TDP-43 se compose d'un domaine N-terminal (NTD) possédant une structure définie, de deux domaines de motifs de reconnaissance de l'ARN (RRM1 et RRM2) et d'un domaine C-terminal intrinsèquement désordonné (CTD). Le do

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31

Lu, Xiaojun. "STRUCTURE OF PRION PROTEIN AMYLOID FIBRILS AS DETERMINED BY HYDROGEN/DEUTERIUM EXCHANGE." Case Western Reserve University School of Graduate Studies / OhioLINK, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=case1205510131.

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32

Nassar, Roy. "The nanomechanical properties of amyloid fibrils using molecular dynamics simulations." Thesis, University of British Columbia, 2016. http://hdl.handle.net/2429/57685.

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Abstract (sommario):

Amyloid fibril formation, believed to be a generic property of polypeptides, plays major roles in neurodegenerative pathologies such as Alzheimer’s, Parkinson’s and prion diseases, as well as in functional biological processes in many organisms including humans. Revealing specifics of their molecular architecture, conformational stability, mechanisms of formation and physical properties holds clues to devising effective methods to fight their associated pathologies. An increasing requirement has been the development of a detailed understanding of the nanomechanics of amyloid core structures du

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33

Marginean, Denisse, та Ebba Hellstrand. "Fluorescent molecules as probes for characterization of amyloid β fibrils". Thesis, Linköpings universitet, Institutionen för fysik, kemi och biologi, 2021. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-178005.

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Abstract (sommario):

Alzheimer’s Disease (AD) is the leading cause of dementia in the world and the World Health Organization has recognized AD as a global public health priority. One of the pathological hallmarks of AD is amyloid plaques formed from amyloid β (Aβ) fibrils. Aβ is formed when amyloid precursor protein is cleaved by secretase enzymes. Cleavage by different secretases causes Aβ to occur in different forms, mainly as 40 and 42 residue long proteins, called Aβ1-40 and Aβ1-42, where Aβ1-42 is more likely to form amyloid fibrils and is therefore considered more harmful. Fluorescent probes are currently u

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34

Ndlovu, Hlengisizwe. "Mechanical response of amyloid fibrils probed by molecular dynamics simulation." Thesis, University of Leeds, 2013. http://etheses.whiterose.ac.uk/4592/.

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Abstract (sommario):

The presence of self-assembled protein aggregates known as Amyloid fibrils are associated with an increasing number of human conditions such as type-II Diabetes, Parkinson’s, Huntington’s and Alzheimer’s disease. A link has been made between the fragility of these normally robust structures and an enhancement of their toxic effects. This highlights a need for a firm understanding of the factors that govern their mechanical properties if effective therapeutic strategies are to be developed. The main aims of this thesis are to probe, at a molecular level, the key interactions that contribute to

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35

Mossuto, Maria Francesca. "Protein amyloidogenesis: characterization of aggregation prone conformations and fibrils structure." Doctoral thesis, Università degli studi di Padova, 2008. http://hdl.handle.net/11577/3425566.

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Abstract (sommario):

Current interest in studying amyloid fibrils arises from their involvement in different fields (Chiti and Dobson, 2006). First, they play a crucial role in disorders such as Alzheimer's and Parkinson's diseases. Second, since it has been demonstrated that all polypeptide chains form fibrils under appropriate conditions, the understanding of why and how this process happens has become central problem in protein knowledge. Last, the ordered ultrastructure characterizing amyloid fibrils may be thought as a basis for nanomaterials with possible technological applications. However, despite the abil

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36

Hagg, Rupert. "Macromolecules and their interactions of the surface of native cartilage fibrils /." Aachen : Shaker, 1997. http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&doc_number=007763733&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA.

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37

Yang, Lanti. "Mechanical properties of collagen fibrils and elastic fibers explored by AFM." Enschede : University of Twente [Host], 2008. http://doc.utwente.nl/58870.

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38

Smaoui, Mohamed. "A computational framework to create an ensemble of stable amyloid fibrils." Thesis, McGill University, 2011. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=104698.

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Abstract (sommario):

Amyloid proteins are known to have their implications on many neurodegenerative diseases such as Alzheimer's, Parkinson's, Huntington, and Type II Diabetes diseases. They come together and aggregate into very stable structures that the cell cannot easily eliminate. We developed a computational framework called CreateFibril to model the aggregation phenomena of amyloids, predict novel aggregation possibilities, and study the structural stability of amyloid aggregates under variable environment conditions.<br>Les protéines amyloïdes sont connues pour leurs implications sur de nombreuses maladies

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39

Caddy, G. L. "Dynamics, stability and formation of amyloid fibrils : insights from mass spectrometry." Thesis, University of Cambridge, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.597207.

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In this thesis I have used electrospray mass spectrometry (ESI-MS) to investigate various aspects of amyloid fibrils, including their mechanism of formation, their structure and dynamics, and approaches to inhibit fibril development. I have used hydrogen exchange methods coupled with ESI-MS to examine the differences in spontaneous protein unfolding between amyloidogenic and non-amyloidogenic variants of human lysozyme and thus determined a correlation between the ease with which the partially unfolded event occurs and the likelihood of amyloid deposition <i>in vivo</i>. I also used a similar

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40

Channon, Kevin. "Photophysical properties of fluorescent molecules organised onto self-assembled peptide fibrils." Thesis, University of Cambridge, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.613073.

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41

Mezache, Mathieu. "Oscillatory processes during the aggregation and the fragmentation of amyloid fibrils." Thesis, Sorbonne université, 2019. http://www.theses.fr/2019SORUS533.

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Cette thèse se focalise sur l'étude du processus d'agrégation et de fragmentation des protéines. Plus particulièrement, des phénomènes cinétiques oscillatoires sont identifiés lors d’expériences sur les maladies à prions, une sous-catégorie des maladies amyloïdes. Dans un premier temps, nous remarquons que des oscillations atténuées et localisées à des endroits spécifiques sur les signaux expérimentaux sont observables. Ces oscillations mettent en avant la présence de phénomènes cinétiques complexes, sous-jacents, lors des processus cinétiques de protéines. Nous définissons une caractérisation

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42

Biesecker, Steven. "THE ROLE OF BACTERIAL AMYLOID FIBRILS IN ESCHERICHIA COLI COMPLEMENT RESISTANCE." Master's thesis, Temple University Libraries, 2012. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/174200.

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Microbiology and Immunology<br>M.S.<br>Strains of Escherichia coli may exist as a beneficial human commensal or a pathogen capable of causing morbidity and mortality. Of the E. coli which causes human disease, many strains which cause bacteremia have been identified as possessing virulence factors which make them more resistant to the complement system. The bacterial amyloid fibril, curli, functions in bacterial adherence and the formation of biofilm. Curli-producing parental and curli-deficient mutant E. coli was compared in its survival to human complement, using in vitro serum sensitivity a

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43

Lam, Hoa Le Ko Frank K. "Electrospinning of single wall carbon nanotube reinforced aligned fibrils and yarns /." Philadelphia, Pa. : Drexel University, 2004. http://dspace.library.drexel.edu/handle/1860/368.

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44

Mantonico, Malisa. "Elucidation of structural Properties of amyloid-like Fibrils via Solid State NMR." Thesis, KTH, Skolan för kemi, bioteknologi och hälsa (CBH), 2018. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-227706.

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The invention of plastic has revolutionized people's life style not only by facilitating the storage and transportation of various goods but also by improving mechanical properties of mankind's technological advances. However, plastic is considered to be harmful, as it contains toxic chemical compounds which are accumulated due to its persistence. Therefore, plastic materials represent a threat to the wildlife, since its extensive use and disposal in landfills and natural habitats increased eminently. People's growing concern about the enviromental impact of pastic and its presence in the food

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45

Shen, Zhilei Liu. "Tensile Mechanical Properties of Isolated Collagen Fibrils Obtained by Microelectromechanical Systems Technology." Case Western Reserve University School of Graduate Studies / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=case1278977802.

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46

Liu, Yehe. "A NOVEL METHOD TO EXTRACT TYPE-I COLLAGEN FIBRILS FROM MAMMALIAN TENDONS." Case Western Reserve University School of Graduate Studies / OhioLINK, 2015. http://rave.ohiolink.edu/etdc/view?acc_num=case1433206202.

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47

Agnihotri, Mithila V. agnihotri. "Dynamics of biomolecules: Dielectric spectrum of DNA and assembly of peptide fibrils." The Ohio State University, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=osu1514831676642994.

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48

Mishra, Pamela Haradhan. "Unbinding of abeta peptides from amyloid fibrils explicit solvent molecular dynamics study /." Fairfax, VA : George Mason University, 2008. http://hdl.handle.net/1920/3419.

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Thesis (M.S.)--George Mason University, 2008.<br>Vita: p. 48. Thesis director: Dmitri Klimov. Submitted in partial fulfillment of the requirements for the degree of Master of Science in Bioinformatics and Computational Biology. Title from PDF t.p. (viewed Mar. 17, 2009). Includes bibliographical references (p. 45-47). Also issued in print.

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49

Ayutsede, Jonathan Eyitouyo Ko Frank K. "Regeneration of bombyx mori silk nanofibers and nanocomposite fibrils by the electrospinning process /." Philadelphia, Pa. : Drexel University, 2005. http://dspace.library.drexel.edu/handle/1860/546.

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Smith, Michael. "Nucleation and growth of insulin fibrils in bulk solution and at hydrophobic surfaces." Thesis, University of Nottingham, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.489699.

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Abstract (sommario):

The formation of amyloid fibrils and their associated aggregates has important. applications in the understanding of among others, Alzheimer's disease and Huntingdon's disease. In this study FTIR spectroscopy, together with complimentary techniques, was used to investigate the nucleation and growth of insulin fibrils in bulk solution and at a polystyrene interface. Fibril nucleation rates were fonnd to be significantly enhanced by the presence of a polystyrene surface when compared with the bulk. However, growth rates at a polystyrene surface were found to be significantly slower than those ob

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