Halogenation of the N-Terminus Tyrosine 10 Promotes Supramolecular Stabilization of the Amyloid-β Sequence 7-12
© 2020 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA..
Here, we demonstrate that introduction of halogen atoms at the tyrosine 10 phenol ring of the DSGYEV sequence derived from the flexible amyloid-β N-terminus, promotes its self-assembly in the solid state. In particular, we report the crystal structures of two halogen-modified sequences, which we found to be stabilized in the solid state by halogen-mediated interactions. The structural study is corroborated by Non-Covalent Interaction (NCI) analysis. Our results prove that selective halogenation of an amino acid enhances the supramolecular organization of otherwise unstructured biologically-relevant sequences. This method may develop as a general strategy for stabilizing highly polymorphic peptide regions.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2020 |
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Erschienen: |
2020 |
Enthalten in: |
Zur Gesamtaufnahme - volume:9 |
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Enthalten in: |
ChemistryOpen - 9(2020), 2 vom: 13. Feb., Seite 253-260 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Maiolo, Daniele [VerfasserIn] |
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Links: |
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Themen: |
42HK56048U |
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Anmerkungen: |
Date Completed 21.06.2021 Date Revised 21.06.2021 published: Electronic-eCollection Citation Status MEDLINE |
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doi: |
10.1002/open.201900350 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM307027295 |
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520 | |a Here, we demonstrate that introduction of halogen atoms at the tyrosine 10 phenol ring of the DSGYEV sequence derived from the flexible amyloid-β N-terminus, promotes its self-assembly in the solid state. In particular, we report the crystal structures of two halogen-modified sequences, which we found to be stabilized in the solid state by halogen-mediated interactions. The structural study is corroborated by Non-Covalent Interaction (NCI) analysis. Our results prove that selective halogenation of an amino acid enhances the supramolecular organization of otherwise unstructured biologically-relevant sequences. This method may develop as a general strategy for stabilizing highly polymorphic peptide regions | ||
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700 | 1 | |a Gori, Alessandro |e verfasserin |4 aut | |
700 | 1 | |a Gazzera, Lara |e verfasserin |4 aut | |
700 | 1 | |a Demitri, Nicola |e verfasserin |4 aut | |
700 | 1 | |a Genoni, Alessandro |e verfasserin |4 aut | |
700 | 1 | |a Baggi, Fulvio |e verfasserin |4 aut | |
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700 | 1 | |a Resnati, Giuseppe |e verfasserin |4 aut | |
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