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231225s2020 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.0c01747
|2 doi
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|a pubmed24n1051.xml
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|a eng
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| 100 |
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|a Dec, Robert
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Extremely Amyloidogenic Single-Chain Analogues of Insulin's H-Fragment
|b Structural Adaptability of an Amyloid Stretch
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|c 2020
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|a ƒa Online-Ressource
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|a Date Completed 21.06.2021
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|a Date Revised 21.06.2021
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Relatively short amino acid sequences often play a pivotal role in triggering protein aggregation leading to the formation of amyloid fibrils. In the case of insulin, various regions of A- and B-chains have been implicated as the most relevant to the protein's amyloidogenicity. Here, we focus on the highly amyloidogenic H-fragment of insulin comprising the disulfide-bonded N-terminal parts of both chains. Analysis of the aggregation behavior of single-chain peptide derivatives of the H-fragment suggests that the A-chain's part initiates the aggregation process while the disulfide-tethered B-chain reluctantly adapts to amyloid structure. Merging of both A- and B-parts into single-chain continuous peptides (A-B and B-A) results in extreme amyloidogenicity exceeding that of the double-chain H-fragment as reflected by almost instantaneous de novo fibrillization. Amyloid fibrils of A-B and B-A present distinct morphological and infrared traits and do not cross-seed insulin. Our study suggests that the N-terminal part of insulin's A-chain containing the intact Cys6-Cys11 intrachain disulfide bond may constitute insulin's major amyloid stretch which, through its bent conformation, enforces a parallel in-register alignment of β-strands. Comparison of the self-association behavior of H, A-B, and B-A peptides suggests that A-chain's N-terminal amyloid stretch is very versatile and adaptive to various structural contexts
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Amyloid
|2 NLM
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| 650 |
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|a Amyloidogenic Proteins
|2 NLM
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| 650 |
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|a Disulfides
|2 NLM
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| 650 |
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|a Insulin
|2 NLM
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1 |
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|a Dzwolak, Wojciech
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1999
|g 36(2020), 41 vom: 20. Okt., Seite 12150-12159
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|x 1520-5827
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|g volume:36
|g year:2020
|g number:41
|g day:20
|g month:10
|g pages:12150-12159
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|u http://dx.doi.org/10.1021/acs.langmuir.0c01747
|3 Volltext
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