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Statements

Subject Item
n2:RIV%2F00209805%3A_____%2F13%3A%230000416%21RIV14-MSM-00209805
rdf:type
skos:Concept n3:Vysledek
rdfs:seeAlso
http://www.sciencedirect.com/science/article/pii/S0013468613009626
dcterms: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.
dcterms:title
Electrochemical sensing of 2D condensation in amyloid peptides Electrochemical sensing of 2D condensation in amyloid peptides
skos:prefLabel
Electrochemical sensing of 2D condensation in amyloid peptides Electrochemical sensing of 2D condensation in amyloid peptides
skos:notation
RIV/00209805:_____/13:#0000416!RIV14-MSM-00209805
n3:predkladatel
n4:ico%3A00209805
n5:aktivita
n6:P n6:I
n5:aktivity
I, P(ED2.1.00/03.0101), P(GAP301/11/2055)
n5:cisloPeriodika
September
n5:dodaniDat
n16:2014
n5:domaciTvurceVysledku
n19:9991646
n5:druhVysledku
n10:J
n5:duvernostUdaju
n13:S
n5:entitaPredkladatele
n12:predkladatel
n5:idSjednocenehoVysledku
72363
n5:idVysledku
RIV/00209805:_____/13:#0000416
n5:jazykVysledku
n18:eng
n5:klicovaSlova
amyloid peptide sensing; 2D condensed layers; mercury-sulfur binding; voltammetric and chronopotentiometric stripping; catalytic hydrogen evolution
n5:klicoveSlovo
n8:catalytic%20hydrogen%20evolution n8:mercury-sulfur%20binding n8:2D%20condensed%20layers n8:voltammetric%20and%20chronopotentiometric%20stripping n8:amyloid%20peptide%20sensing
n5:kodStatuVydavatele
GB - Spojené království Velké Británie a Severního Irska
n5:kontrolniKodProRIV
[559FB892D7B5]
n5:nazevZdroje
Electrochimica Acta
n5:obor
n9:CG
n5:pocetDomacichTvurcuVysledku
1
n5:pocetTvurcuVysledku
5
n5:projekt
n17:GAP301%2F11%2F2055 n17:ED2.1.00%2F03.0101
n5:rokUplatneniVysledku
n16:2013
n5:svazekPeriodika
106
n5:tvurceVysledku
Paleček, Emil
n5:wos
000323192400005
s:issn
0013-4686
s:numberOfPages
6
n20:doi
10.1016/j.electacta.2013.05.057