About: Electrochemical sensing of 2D condensation in amyloid peptides

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An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://www.sciencedirect.com/science/article/pii/S0013468613009626
Description	The interfacial behavior of the model amyloid peptide octamer YYKLVFFC (peptide 1) and two otheramyloid peptides YEVHHQKLVFF (peptide 2) and KKLVFFA (peptide 3) at the metal\|aqueous solutioninterface was studied by voltammetric and constant current chronopotentiometric stripping (CPS). Allthree peptides are adsorbed in a wide potential range and exhibit different interfacial organizationsdepending on the electrode potential. At the least negative potentials, chemisorption of peptide 1 occursthrough the formation of a metal sulfur bond. This bond is broken close to -0.6 V. The peptide undergoesself-association at more negative potentials, leading to the formation of a %22pit%22 characteristic of a 2Dcondensed film. Under the same conditions the other peptides do not produce such a pit. Formation ofthe 2D condensed layer in peptide 1 is supported by the time, potential and temperature dependences ofthe interfacial capacity and it is shown that presence of the 2D layer is reflected by the peptide CPS signals due to the catalytic hydrogen evolution. The ability of peptide 1 to form the potential-dependent 2Dcondensed layer has been reported neither for any other peptide nor for any protein molecule. This abilitymight be related to the well-known oligomerization and aggregation of Alzheimer amyloid peptides. The interfacial behavior of the model amyloid peptide octamer YYKLVFFC (peptide 1) and two otheramyloid peptides YEVHHQKLVFF (peptide 2) and KKLVFFA (peptide 3) at the metal\|aqueous solutioninterface was studied by voltammetric and constant current chronopotentiometric stripping (CPS). Allthree peptides are adsorbed in a wide potential range and exhibit different interfacial organizationsdepending on the electrode potential. At the least negative potentials, chemisorption of peptide 1 occursthrough the formation of a metal sulfur bond. This bond is broken close to -0.6 V. The peptide undergoesself-association at more negative potentials, leading to the formation of a %22pit%22 characteristic of a 2Dcondensed film. Under the same conditions the other peptides do not produce such a pit. Formation ofthe 2D condensed layer in peptide 1 is supported by the time, potential and temperature dependences ofthe interfacial capacity and it is shown that presence of the 2D layer is reflected by the peptide CPS signals due to the catalytic hydrogen evolution. The ability of peptide 1 to form the potential-dependent 2Dcondensed layer has been reported neither for any other peptide nor for any protein molecule. This abilitymight be related to the well-known oligomerization and aggregation of Alzheimer amyloid peptides. (en)
Title	Electrochemical sensing of 2D condensation in amyloid peptides Electrochemical sensing of 2D condensation in amyloid peptides (en)
skos:prefLabel	Electrochemical sensing of 2D condensation in amyloid peptides Electrochemical sensing of 2D condensation in amyloid peptides (en)
skos:notation	RIV/00209805:_____/13:#0000416!RIV14-MSM-00209805
http://linked.open...avai/riv/aktivita	I P
http://linked.open...avai/riv/aktivity	I, P(ED2.1.00/03.0101), P(GAP301/11/2055)
http://linked.open...iv/cisloPeriodika	September
http://linked.open...vai/riv/dodaniDat	2014
http://linked.open...aciTvurceVysledku	Paleček, Emil
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Masarykův onkologický ústav
http://linked.open...dnocenehoVysledku	72363
http://linked.open...ai/riv/idVysledku	RIV/00209805:_____/13:#0000416
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	amyloid peptide sensing; 2D condensed layers; mercury-sulfur binding; voltammetric and chronopotentiometric stripping; catalytic hydrogen evolution (en)
http://linked.open.../riv/klicoveSlovo	2D condensed layers amyloid peptide sensing mercury-sulfur binding voltammetric and chronopotentiometric stripping catalytic hydrogen evolution
http://linked.open...odStatuVydavatele	GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV	[559FB892D7B5]
http://linked.open...i/riv/nazevZdroje	Electrochimica Acta
http://linked.open...in/vavai/riv/obor	CG
http://linked.open...ichTvurcuVysledku	1 (xsd:int)
http://linked.open...cetTvurcuVysledku	5 (xsd:int)
http://linked.open...vavai/riv/projekt	Regional Centre for Applied Molecular Oncology (RECAMO) New methods of analysis of proteins and their glycosylation in cancer - combination of electrochemistry, microfludic biosensors and mass spectrometry.
http://linked.open...UplatneniVysledku	2013
http://linked.open...v/svazekPeriodika	106
http://linked.open...iv/tvurceVysledku	Paleček, Emil
http://linked.open...ain/vavai/riv/wos	000323192400005
issn	0013-4686
number of pages	6 (xsd:int)
http://bibframe.org/vocab/doi	10.1016/j.electacta.2013.05.057

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