Self-Assembly of Ovalbumin into Amyloid and Non-Amyloid Fibrils

Lara, Cécile; Gourdin-Bertin, S.; Adamčík, Jozef; Bolisetty, Sreenath; Mezzenga, Raffaele

doi:10.1021/bm301481v

Cited by 131 publications

(131 citation statements)

References 39 publications

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“…39 That study does not, however, investigate the molecular organization of the protolaments that assembles into the larger ribbon structures. Notably, no multistranded ribbons were observed in any of our samples.…”

Section: Molecular Mechanism For the Morphological Switchmentioning

confidence: 99%

On the role of peptide hydrolysis for fibrillation kinetics and amyloid fibril morphology

Hedenqvist

Langton

et al. 2018

RSC Adv.

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Self-assembly of proteins into amyloid-like nanofibrils is not only a key event in several diseases, but such fibrils are also associated with intriguing biological function and constitute promising components for new biobased materials. The bovine whey protein b-lactoglobulin has emerged as an important model protein for the development of such materials. We here report that peptide hydrolysis is the rate-determining step for fibrillation of b-lactoglobulin in whey protein isolate. We also explore the observation that blactoglobulin nanofibrils of distinct morphologies are obtained by simply changing the initial protein concentration. We find that the morphological switch is related to different nucleation mechanisms and that the two classes of nanofibrils are associated with variations of the peptide building blocks. Based on the results, we propose that the balance between protein concentration and the hydrolysis rate determines the structure of the formed nanofibrils.

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Section: Molecular Mechanism For the Morphological Switchmentioning

confidence: 99%

On the role of peptide hydrolysis for fibrillation kinetics and amyloid fibril morphology

Hedenqvist

Langton

et al. 2018

RSC Adv.

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“…Some form different fibril morphologies under different environmental conditions (such as in apo-C II (46), a-syn (43,44), b-2m (18), and OVA (47,48)). Alternatively some, like Ab, form flexible, wormlike fibrils early in the aggregation process before the appearance of rigid fibrils (9).…”

Section: Experimental Confirmation Of the Growth Pathwaymentioning

confidence: 99%

A Kinetic Study of Ovalbumin Fibril Formation: The Importance of Fragmentation and End-Joining

Kalapothakis

Morris

Szavits-Nossan

et al. 2015

Biophysical Journal

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The ability to control the morphologies of biomolecular aggregates is a central objective in the study of self-assembly processes. The development of predictive models offers the surest route for gaining such control. Under the right conditions, proteins will self-assemble into fibers that may rearrange themselves even further to form diverse structures, including the formation of closed loops. In this study, chicken egg white ovalbumin is used as a model for the study of fibril loops. By monitoring the kinetics of self-assembly, we demonstrate that loop formation is a consequence of end-to-end association between protein fibrils. A model of fibril formation kinetics, including end-joining, is developed and solved, showing that end-joining has a distinct effect on the growth of fibrillar mass density (which can be measured experimentally), establishing a link between self-assembly kinetics and the underlying growth mechanism. These results will enable experimentalists to infer fibrillar morphologies from an appropriate analysis of self-assembly kinetic data.

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“…The plateau phase of the aggregation reaction is an assortment of monomers, oligomers and fibrils with the morphology of the mature fibrils exhibiting appreciable heterogeneity [21,[23][24][25]. Morphological heterogeneity or structural polymorphism can be inherent as seen with proteins like Amyloid β [26], αSyn [21,27,28], Ig light chains [29], ovalbumin [30], β-lactoglobulin and lysozyme [31], which form morphologically distinct assemblies under the same solvent conditions. Also, specific solvent conditions may favor certain morphology.…”

Section: Introductionmentioning

confidence: 99%