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|a 10.1021/acs.langmuir.2c02682
|2 doi
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|a pubmed24n1173.xml
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|a (NLM)36688667
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|a DE-627
|b ger
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|e rakwb
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|a eng
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|a Clark, Rose A
|e verfasserin
|4 aut
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|a Tripeptide Self-Assembled Monolayers as Biocompatible Surfaces for Cytochrome c Electrochemistry
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|c 2023
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 01.02.2023
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|a Date Revised 27.02.2023
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Biocompatible tripeptide self-assembled monolayers (SAMs) are designed with a carboxylate group on the terminal amino acid (glutamate, aspartate, or amino adipate) to electrostatically attract the lysine groups around the heme crevice in horse heart cytochrome c (cyt c), creating an electroactive protein/tripeptide/Au interfacial structure. Exposing the peptide/Au electrode to cyt c resulted in an 11 ± 3 pmol/cm2 electroactive protein surface coverage. Topographical images of the interfacial structure are obtained down to single-protein resolution by atomic force microscopy. Uniform protein monolayer assemblies are formed on the Au electrode with no major surface roughness changes. The cyt c/peptide/Au electrode systems were examined electrochemically to probe surface charge effects on the redox thermodynamics and kinetics of cyt c. Neutralization of protein surface charge due to adsorption on anionic COOH-terminated SAMs was found to change the formal potential, as determined by cyclic voltammetry. The cyt c/peptide/Au electrodes exhibit formal potentials shifted to more positive values, have a surface carboxylic acid pKa of 6 or higher, and produce effective cyt c surface charges (Zox) of -6 to -14. The Marcus theory is utilized to determine the protein electron transfer rates, which are ∼5 times faster for cyt c/tripeptide/Au compared to cyt c/11-mercaptoundecanoic acid SAMs of similar chain lengths
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a Cytochromes c
|2 NLM
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|a 9007-43-6
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|a Proteins
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|a Peptides
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|a Gold
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|a 7440-57-5
|2 NLM
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|a Yawitz, Tanner
|e verfasserin
|4 aut
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|a Luchs, Logan
|e verfasserin
|4 aut
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|a Conrad, Tiffany
|e verfasserin
|4 aut
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|a Bartlebaugh, Owen
|e verfasserin
|4 aut
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|a Boyd, Hannah
|e verfasserin
|4 aut
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|a Hargittai, Balazs
|e verfasserin
|4 aut
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1999
|g 39(2023), 4 vom: 31. Jan., Seite 1414-1424
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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|g volume:39
|g year:2023
|g number:4
|g day:31
|g month:01
|g pages:1414-1424
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|u http://dx.doi.org/10.1021/acs.langmuir.2c02682
|3 Volltext
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|d 39
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