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231224s2013 xx |||||o 00| ||eng c |
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|a 10.1021/la304374q
|2 doi
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|a eng
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| 100 |
1 |
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|a Dzwolak, Wojciech
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Conformational memory effect reverses chirality of vortex-induced insulin amyloid superstructures
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|c 2013
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|a Text
|b txt
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|a ƒaComputermedien
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|a ƒa Online-Ressource
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|a Date Completed 14.06.2013
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| 500 |
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|a Date Revised 08.01.2013
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Formation of amyloid fibrils is often associated with intriguing far-from-equilibrium phenomena such as conformational memory effects or flow-driven self-assembly. Insulin is a model amyloidogenic polypeptide forming distinct structural variants of fibrils, which self-propagate through seeding. According to infrared absorption, fibrils from bovine insulin ([BI]) and Lys(B31)-Arg(B32) human insulin analogue ([KR]) cross-seed each other and imprint distinct structural features in daughter fibrils. In the absence of preformed [KR] amyloid seeds, bovine insulin agitated at 60 °C converts into chiral amyloid superstructures exhibiting negative extrinsic Cotton effect in bound thioflavin T. However, when agitated bovine insulin is simultaneously cross-seeded with [KR] amyloid, daughter fibrils reveal a positive extrinsic Cotton effect. Our study indicates that dramatic changes in global properties of amyloid superstructures may emerge from subtle conformational-level variations in single fibrils (e.g., alignment and twist of β-strands) that are encoded by memory effects
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| 650 |
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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| 650 |
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|a Amyloid
|2 NLM
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| 650 |
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7 |
|a Insulin
|2 NLM
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| 700 |
1 |
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|a Surmacz-Chwedoruk, Weronika
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Babenko, Viktoria
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
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|g 29(2013), 1 vom: 08. Jan., Seite 365-70
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|g year:2013
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|g pages:365-70
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|u http://dx.doi.org/10.1021/la304374q
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