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Abstract
Protein amyloid fibers are often found to have a β-pleated sheet structure regardless of their sequence, leading some to believe that it is the molecule's misfolding that leads to aggregation. In this article, an alternative model is introduced for the amyloid community to consider, that fiber formation is a surface-energy minimization process, starting with the generation of colloidal particles and their linear assembly, and ending with structural evolution of the aggregates into mature fibers. We propose that aggregation drives conformational change and that a conformational change is not essential to initiate the aggregation process.
| Abbreviations | ||
| AFM | = | atomic force microscopy |
| AD | = | Alzheimer's disease |
| NMR | = | nuclear magnetic resonance |
| MW | = | molecular weight |
| PrPC | = | cellular prion protein |
| PrPSc | = | scrapie prion protein |
| CPrPSc | = | concentration of PrPSc |
| CNucU | = | nucleation unit concentration |
| [PrPSc]Nuc | = | nucleation concentration for PrPSc |
| [PrPSc]Sat | = | saturation concentration for PrPSc |
| polyQ | = | polyglutamine |
| α-syn | = | α-synuclein |
| TEM | = | transmission electron microscopy |
| 2° and 3° | = | secondary and tertiary structure of protein |
| Abbreviations | ||
| AFM | = | atomic force microscopy |
| AD | = | Alzheimer's disease |
| NMR | = | nuclear magnetic resonance |
| MW | = | molecular weight |
| PrPC | = | cellular prion protein |
| PrPSc | = | scrapie prion protein |
| CPrPSc | = | concentration of PrPSc |
| CNucU | = | nucleation unit concentration |
| [PrPSc]Nuc | = | nucleation concentration for PrPSc |
| [PrPSc]Sat | = | saturation concentration for PrPSc |
| polyQ | = | polyglutamine |
| α-syn | = | α-synuclein |
| TEM | = | transmission electron microscopy |
| 2° and 3° | = | secondary and tertiary structure of protein |