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- W2964674706 abstract "Many peptides aggregate into insoluble β-sheet rich amyloid fibrils. Some of these aggregation processes are linked to age-related diseases, such as Alzheimer's disease and type 2 diabetes. Here, we show that the secondary structure of the peptide uperin 3.5 directs the kinetics and mechanism of amyloid fibrillar aggregation. Uperin 3.5 variants were investigated using thioflavin T fluorescence assays, circular dichroism spectroscopy, and structure prediction methods. Our results suggest that those peptide variants with a strong propensity to form an α-helical secondary structure under physiological conditions are more likely to aggregate into amyloid fibrils than peptides in an unstructured or random coil conformation. This conclusion is in good agreement with the hypothesis that an α-helical transition state is required for peptide aggregation into amyloid fibrils. Specifically, uperin 3.5 variants in which charged amino acids were replaced by alanine were richer in α-helical content, leading to enhanced aggregation compared to that of wild type uperin 3.5. However, the addition of 2,2,2-trifluoroethanol as a major co-solute or membrane-mimicking phospholipid environments locked uperin 3.5 to the α-helical conformation preventing amyloid aggregation. Strategies for stabilizing peptides into their α-helical conformation could provide therapeutic approaches for overcoming peptide aggregation-related diseases. The impact of the physiological environment on peptide secondary structure could explain aggregation processes in a cellular environment." @default.
- W2964674706 created "2019-08-13" @default.
- W2964674706 creator A5005359088 @default.
- W2964674706 creator A5005620103 @default.
- W2964674706 creator A5021438817 @default.
- W2964674706 creator A5021728242 @default.
- W2964674706 creator A5022803092 @default.
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- W2964674706 creator A5055609359 @default.
- W2964674706 creator A5058121216 @default.
- W2964674706 creator A5063796389 @default.
- W2964674706 date "2019-08-06" @default.
- W2964674706 modified "2023-09-29" @default.
- W2964674706 title "The Kinetics of Amyloid Fibrillar Aggregation of Uperin 3.5 Is Directed by the Peptide’s Secondary Structure" @default.
- W2964674706 cites W1552345552 @default.
- W2964674706 cites W1568596575 @default.
- W2964674706 cites W1581858536 @default.
- W2964674706 cites W1588979652 @default.
- W2964674706 cites W1715632026 @default.
- W2964674706 cites W1745084828 @default.
- W2964674706 cites W1963834832 @default.
- W2964674706 cites W1970577444 @default.
- W2964674706 cites W1971356093 @default.
- W2964674706 cites W1971797738 @default.
- W2964674706 cites W1972535964 @default.
- W2964674706 cites W1974719543 @default.
- W2964674706 cites W1976201852 @default.
- W2964674706 cites W1976820443 @default.
- W2964674706 cites W1979509752 @default.
- W2964674706 cites W1981487040 @default.
- W2964674706 cites W1985818354 @default.
- W2964674706 cites W1985950310 @default.
- W2964674706 cites W1985992988 @default.
- W2964674706 cites W1988018861 @default.
- W2964674706 cites W1989270637 @default.
- W2964674706 cites W1989386714 @default.
- W2964674706 cites W1995272223 @default.
- W2964674706 cites W2002911779 @default.
- W2964674706 cites W2003496015 @default.
- W2964674706 cites W2004176946 @default.
- W2964674706 cites W2004242436 @default.
- W2964674706 cites W2004377868 @default.
- W2964674706 cites W2013136212 @default.
- W2964674706 cites W2020638348 @default.
- W2964674706 cites W2020854903 @default.
- W2964674706 cites W2025595434 @default.
- W2964674706 cites W2025938842 @default.
- W2964674706 cites W2026584052 @default.
- W2964674706 cites W2026727321 @default.
- W2964674706 cites W2029667189 @default.
- W2964674706 cites W2030106420 @default.
- W2964674706 cites W2030325989 @default.
- W2964674706 cites W2032487213 @default.
- W2964674706 cites W2038392139 @default.
- W2964674706 cites W2042214383 @default.
- W2964674706 cites W2042434150 @default.
- W2964674706 cites W2045994577 @default.
- W2964674706 cites W2050375429 @default.
- W2964674706 cites W2056816046 @default.
- W2964674706 cites W2057609017 @default.
- W2964674706 cites W2059259481 @default.
- W2964674706 cites W2061543974 @default.
- W2964674706 cites W2061657038 @default.
- W2964674706 cites W2064262345 @default.
- W2964674706 cites W2070905182 @default.
- W2964674706 cites W2071758457 @default.
- W2964674706 cites W2073775320 @default.
- W2964674706 cites W2075068625 @default.
- W2964674706 cites W2084845164 @default.
- W2964674706 cites W2090786642 @default.
- W2964674706 cites W2093720304 @default.
- W2964674706 cites W2094077114 @default.
- W2964674706 cites W2094881767 @default.
- W2964674706 cites W2096495474 @default.
- W2964674706 cites W2100361186 @default.
- W2964674706 cites W2104571730 @default.
- W2964674706 cites W2107677733 @default.
- W2964674706 cites W2110515879 @default.
- W2964674706 cites W2115537581 @default.
- W2964674706 cites W2119993590 @default.
- W2964674706 cites W2120717592 @default.
- W2964674706 cites W2121753059 @default.
- W2964674706 cites W2121963977 @default.
- W2964674706 cites W2131474431 @default.
- W2964674706 cites W2131617076 @default.
- W2964674706 cites W2131965976 @default.
- W2964674706 cites W2134057677 @default.
- W2964674706 cites W2137276641 @default.
- W2964674706 cites W2140260269 @default.
- W2964674706 cites W2143640196 @default.
- W2964674706 cites W2146516421 @default.
- W2964674706 cites W2148478260 @default.
- W2964674706 cites W2153187042 @default.
- W2964674706 cites W2154479185 @default.
- W2964674706 cites W2156069524 @default.
- W2964674706 cites W2156343873 @default.
- W2964674706 cites W2156798505 @default.
- W2964674706 cites W2158482458 @default.