. . "http://www.sciencedirect.com/science/article/pii/S0013468613009626" . . . . "GB - Spojen\u00E9 kr\u00E1lovstv\u00ED Velk\u00E9 Brit\u00E1nie a Severn\u00EDho Irska" . "1"^^ . "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 . . "Electrochimica Acta" . "000323192400005" . "Electrochemical sensing of 2D condensation in amyloid peptides"@en . "RIV/00209805:_____/13:#0000416" . "amyloid peptide sensing; 2D condensed layers; mercury-sulfur binding; voltammetric and chronopotentiometric stripping; catalytic hydrogen evolution"@en . . "I, P(ED2.1.00/03.0101), P(GAP301/11/2055)" . "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." . "RIV/00209805:_____/13:#0000416!RIV14-MSM-00209805" . "0013-4686" . . "Electrochemical sensing of 2D condensation in amyloid peptides" . "[559FB892D7B5]" . . "72363" . . "Electrochemical sensing of 2D condensation in amyloid peptides" . . "Pale\u010Dek, Emil" . "September" . . . . "Electrochemical sensing of 2D condensation in amyloid peptides"@en . . "106" . . . "6"^^ . . . "10.1016/j.electacta.2013.05.057" . "5"^^ . .