Tripeptide Self-Assembled Monolayers as Biocompatible Surfaces for Cytochrome c Electrochemistry

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 pr...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1999. - 39(2023), 4 vom: 31. Jan., Seite 1414-1424
1. Verfasser: Clark, Rose A (VerfasserIn)
Weitere Verfasser: Yawitz, Tanner, Luchs, Logan, Conrad, Tiffany, Bartlebaugh, Owen, Boyd, Hannah, Hargittai, Balazs
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2023
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Cytochromes c 9007-43-6 Proteins Peptides Gold 7440-57-5
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245 1 0 |a Tripeptide Self-Assembled Monolayers as Biocompatible Surfaces for Cytochrome c Electrochemistry 
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520 |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 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Research Support, U.S. Gov't, Non-P.H.S. 
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650 7 |a 9007-43-6  |2 NLM 
650 7 |a Proteins  |2 NLM 
650 7 |a Peptides  |2 NLM 
650 7 |a Gold  |2 NLM 
650 7 |a 7440-57-5  |2 NLM 
700 1 |a Yawitz, Tanner  |e verfasserin  |4 aut 
700 1 |a Luchs, Logan  |e verfasserin  |4 aut 
700 1 |a Conrad, Tiffany  |e verfasserin  |4 aut 
700 1 |a Bartlebaugh, Owen  |e verfasserin  |4 aut 
700 1 |a Boyd, Hannah  |e verfasserin  |4 aut 
700 1 |a Hargittai, Balazs  |e verfasserin  |4 aut 
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773 1 8 |g volume:39  |g year:2023  |g number:4  |g day:31  |g month:01  |g pages:1414-1424 
856 4 0 |u http://dx.doi.org/10.1021/acs.langmuir.2c02682  |3 Volltext 
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