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• W2285337112 endingPage "1382" @default.
• W2285337112 startingPage "1376" @default.
• W2285337112 abstract "Chain-length polydispersity is among the least understood factors governing the fibrillation propensity of homopolypeptides. For monodisperse poly-l-glutamic acid (PLGA), the tendency to form fibrils depends of the main-chain length. Long-chained PLGA, so-called (Glu)200, fibrillates more readily than short (Glu)5 fragments. Here we show that conversion of α-helical (Glu)200 into amyloid-like β-fibrils is dramatically accelerated in the presence of intrinsically disordered (Glu)5. While separately self-assembled fibrils of (Glu)200 and (Glu)5 reveal distinct morphological and infrared characteristics, accelerated fibrillation in mixed (Glu)200 and (Glu)5 leads to aggregates similar to neat (Glu)200 fibrils, even in excess of (Glu)5. According to molecular dynamics simulations and circular dichroism measurements, local events of “misfolding transfer” from (Glu)5 to (Glu)200 may play a key role in the initial stages of conformational dynamics underlying the observed phenomenon. Our results highlight chain-length polydispersity as a potent, although so-far unrecognized factor profoundly affecting the fibrillation propensity of homopolypeptides." @default.
• W2285337112 created "2016-06-24" @default.
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• W2285337112 date "2016-03-07" @default.
• W2285337112 modified "2023-09-23" @default.
• W2285337112 title "Beware of Cocktails: Chain-Length Bidispersity Triggers Explosive Self-Assembly of Poly-<scp>l</scp>-Glutamic Acid β₂-Fibrils" @default.
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• W2285337112 doi "https://doi.org/10.1021/acs.biomac.5b01770" @default.
• W2285337112 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26909651" @default.
• W2285337112 hasPublicationYear "2016" @default.
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