The ecology of ditches : a modeling perspective

Mooij, Wolf M.; Klein, J.J.M. de; Gerven, L.P.A. van

doi:10.18174/390133

Cited by 2 publications

(2 citation statements)

References 130 publications

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“…The self-assembly of proteins into fibrils known as amyloid has become linked with both pathological and functional effects in biological systems. For example, amyloid formation from proteins like amyloid beta (Aβ), alpha synuclein, and amylin has been implicated in the progression of Alzheimer's disease, 1,2 Parkinson's disease, 3 and type II diabetes, 4 whereas amyloids derived from curli, rodlin, and β-endorphin aid in such processes as the growth of bacterial biofilms, 5,6 the branching of fungal spores, 7,8 and the storage of neuropeptides. 9 Consequently, extensive research has been focused on understanding and modulating the structure, formation, and stability of amyloid fibrils.…”

Section: Introductionmentioning

confidence: 99%

Polymer−Peptide Conjugates Convert Amyloid into Protein Nanobundles through Fragmentation and Lateral Association

Smith

Barclay

et al. 2019

ACS Appl. Nano Mater.

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The assembly of proteins into amyloid fibrils has become linked not only with the progression of myriad human diseases, but also important biological functions. Understanding and controlling the formation, structure, and stability of amyloid fibrils is therefore a major scientific goal. Here we utilize electron microscopy-based approaches combined with quantitative statistical analysis to show how recently developed kind of amyloid modulators-multivalent polymer-peptide conjugates (mPPCs)-can be applied to control the structure and stability of amyloid fibrils. In doing so, we demonstrate that mPPCs are able to convert 40-residue amyloid beta fibrils into ordered nanostructures through a combination of fragmentation and bundling. Fragmentation is shown to be consistent with a model where the rate constant of fibril breakage is independent of the fibril length, suggesting a local and specific interaction between fibrils and mPPCs. Subsequent bundling, which was previously not observed, leads to the formation of sheet-like nanostructures which are surprisingly much more uniform than the starting fibrils. These nanostructures have dimensions independent of the molecular weight of the mPPC and retain the molecular-level ordering of the starting amyloid fibrils. Collectively, we reveal quantitative and nanoscopic understanding of how mPPCs can be applied to control amyloid structure and stability, and demonstrate approaches to elucidate nanoscale amyloid phase behavior in the presence of functional macromolecules and other modulators.

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Section: Introductionmentioning

confidence: 99%

Polymer−Peptide Conjugates Convert Amyloid into Protein Nanobundles through Fragmentation and Lateral Association

Smith

Barclay

et al. 2019

ACS Appl. Nano Mater.

View full text Add to dashboard Cite

show abstract

“…This project became a collaboration between the Netherlands Institute of Ecology (NIOO-KNAW), Wageningen University & Research centre (WUR), the Netherlands Environmental Assessment Agency (PBL) and Witteveen+Bos, a private engineering company. The core of the research project consisted of a large number of case studies on Dutch lakes and two parallel running PhDstudies: one focussing on PCDitch (Van Gerven, 2016), and one focussing on PCLake (this thesis). Four objectives were identified as important pillars of the overarching project:…”

Section: The Assignmentmentioning

confidence: 99%

Making eco logic and models work : an integrative approach to lake ecosystem modelling

Kuiper¹

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The ecology of ditches : a modeling perspective

Cited by 2 publications

References 130 publications

Polymer−Peptide Conjugates Convert Amyloid into Protein Nanobundles through Fragmentation and Lateral Association

Polymer−Peptide Conjugates Convert Amyloid into Protein Nanobundles through Fragmentation and Lateral Association

Making eco logic and models work : an integrative approach to lake ecosystem modelling

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