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Electrical characteristics of amyloid beta peptides in vertical junctions

DC Field Value Language
dc.contributor.authorSeo, Sohyeon-
dc.contributor.authorLee, Jinju-
dc.contributor.authorChoi, Jungsue-
dc.contributor.authorG. Hwan Park-
dc.contributor.authorYeseul Hong-
dc.contributor.authorHyoyoung Lee-
dc.date.accessioned2021-08-11T05:50:05Z-
dc.date.accessioned2021-08-11T05:50:05Z-
dc.date.available2021-08-11T05:50:05Z-
dc.date.available2021-08-11T05:50:05Z-
dc.date.created2021-08-09-
dc.date.issued2021-07-16-
dc.identifier.issn1884-4049-
dc.identifier.urihttps://pr.ibs.re.kr/handle/8788114/10074-
dc.description.abstract© 2021 Springer Nature Limited. Assembled amyloid beta (A beta) peptides have been considered pathological assemblies involved in human brain diseases, and the electron transfer or electron transport characteristics of A beta are important for the formation of structured assemblies. Here, we report the electrical characteristics of surface-assembled A beta peptides similar to those observed in Alzheimer's patients. These characteristics correlate to their electron transfer characteristics. Electrical current-voltage plots of A beta vertical junction devices show the A beta sequence dependence of the current densities at both A beta monomers (mono-A beta s) and A beta oligomers (oli-A beta s), while A beta sequence dependence is not clearly observed in the electrical characteristics of A beta planar field effect transistors (FETs). In particular, surface oligomerization of A beta peptides drastically decreases the activity of electron transfer, which presents a change in the electron transport pathway in the A beta vertical junctions. Electron transport at oli-A beta junctions is symmetric (tunneling/tunneling) due to the weak and voltage-independent coupling of the less redox-reactive oli-A beta to the contacts, while that at mono-A beta junctions is asymmetric (hopping/tunneling) due to redox levels of mono-A beta voltage-dependently coupled with contact electrodes. Consequently, through vertical junctions, the sequence- and conformation-dependent electrical characteristics of A beta s can reveal their electron transfer activities.-
dc.language영어-
dc.publisherNATURE RESEARCH-
dc.titleElectrical characteristics of amyloid beta peptides in vertical junctions-
dc.typeArticle-
dc.type.rimsART-
dc.identifier.wosid000674639200001-
dc.identifier.scopusid2-s2.0-85110558548-
dc.identifier.rimsid76156-
dc.contributor.affiliatedAuthorG. Hwan Park-
dc.contributor.affiliatedAuthorYeseul Hong-
dc.contributor.affiliatedAuthorHyoyoung Lee-
dc.identifier.doi10.1038/s41427-021-00321-z-
dc.identifier.bibliographicCitationNPG ASIA MATERIALS, v.13, no.1-
dc.relation.isPartOfNPG ASIA MATERIALS-
dc.citation.titleNPG ASIA MATERIALS-
dc.citation.volume13-
dc.citation.number1-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaMaterials Science-
dc.relation.journalWebOfScienceCategoryMaterials Science, Multidisciplinary-
dc.subject.keywordPlusCHARGE-TRANSPORT-
dc.subject.keywordPlusALZHEIMERS-
dc.subject.keywordPlusCONDUCTANCE-
dc.subject.keywordPlusMECHANISM-
dc.subject.keywordPlusOLIGOMERS-
dc.subject.keywordPlusTOXICITY-
Appears in Collections:
Center for Integrated Nanostructure Physics(나노구조물리 연구단) > 1. Journal Papers (저널논문)
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