| NSF Org: |
CHE Division Of Chemistry |
| Recipient: |
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| Initial Amendment Date: | July 30, 2019 |
| Latest Amendment Date: | July 30, 2019 |
| Award Number: | 1919589 |
| Award Instrument: | Standard Grant |
| Program Manager: |
Amanda Haes
CHE Division Of Chemistry MPS Directorate for Mathematical and Physical Sciences |
| Start Date: | September 1, 2019 |
| End Date: | August 31, 2022 (Estimated) |
| Total Intended Award Amount: | $83,181.00 |
| Total Awarded Amount to Date: | $83,181.00 |
| Funds Obligated to Date: |
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| History of Investigator: |
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| Recipient Sponsored Research Office: |
169 LAKEVIEW DR LORETTO PA US 15940-9705 (814)472-7000 |
| Sponsor Congressional District: |
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| Primary Place of Performance: |
PA US 15940-0600 |
| Primary Place of
Performance Congressional District: |
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| Unique Entity Identifier (UEI): |
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| Parent UEI: |
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| NSF Program(s): | Chemical Instrumentation |
| Primary Program Source: |
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| Program Reference Code(s): |
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| Program Element Code(s): |
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| Award Agency Code: | 4900 |
| Fund Agency Code: | 4900 |
| Assistance Listing Number(s): | 47.049 |
ABSTRACT
This award is funded by the Major Research Instrumentation (MRI) and Chemical Instrumentation (CRIF) programs. Professor Edward Zovinka from Saint Francis University and colleague Rose Clark are acquiring an atomic force microscope (AFM). The microscope is a powerful tool for studying the surface of a material. It uses a very small probe which scans across a surface to measure the forces between the probe and the surface. This produces an image of the surface with information on the structure of the surface, its properties and on materials adsorbed on the surface. The AFM data provides basic understanding of complicated surface phenomenon at the atomic level. The research projects supported by this award are interdisciplinary involving analytical chemistry (surface science), biophysical chemistry (protein electrochemistry), and inorganic/environmental analysis. The acquisition supports the educational goals of the faculty to train undergraduates to use major research instrumentation and to develop skills in data collection and interpretation. The instrument is also used in an outreach program to high school students to encourage them to pursue STEM fields.
Several collaborators are involved in the research projects using this atomic force microscope. One project involves the use of the microscope to characterize surfaces in acid mine drainage (AMD) processes. The goal is to better understand armoring of calcite and aluminum removal from AMD effluent. Another project uses the AFM to better understand new peptide self-assembled monolayers. In this project peptide self-assembled monolayers (SAMS) are employed to bind to cytochrome c. The researchers are working to develop new insights into the surface microenvironment and how it influences formal potential and kinetic mechanisms of proteins, paving the way for development of more advanced electrochemical biosensors.
This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.
PROJECT OUTCOMES REPORT
Disclaimer
This Project Outcomes Report for the General Public is displayed verbatim as submitted by the Principal Investigator (PI) for this award. Any opinions, findings, and conclusions or recommendations expressed in this Report are those of the PI and do not necessarily reflect the views of the National Science Foundation; NSF has not approved or endorsed its content.
Intellectual Merit
Project #1 Dr. Rose Clark PI Tripeptide Self-Assembled Monolayers as Biocompatible Surfaces for Cytochrome c (cytc) Electrochemistry1
Molecular scale tailoring of biocompatible surfaces to allow efficient electron transfer between the electrode and a redox protein is important to help direct protein interaction and adsorption. Our group is the first to make biocompatible tripeptide self-assembled monolayers (SAMs) designed with a carboxylate group on the terminal amino acid to electrostatically attract the lysine groups around the heme crevice of cytc. To better characterize the biocompatible surfaces, topographical images of the interfacial structure are obtained down to single-protein resolution by atomic force microscopy (AFM). Surface topographic images were obtained before and after protein addition. Addition of peptide SAM to the electrode caused the RMS roughness to decrease to 0.9 + 0.1 nm (n=10) average. Additional smoothing was observed, 0.7 + 0.1 nm (n=10) RMS, with the adsorption of the cytochrome c protein to peptide SAM/Au surface.
AFM images indicating a smoothing of the gold topography with adsorption of the cytc after monolayer coverage have been reported.2-4 AFM imaging shows cytc is distributed evenly over the surface, supporting a surface with a high density of carboxylic acid functional groups. In addition, AFM force studies were used to mimic the interaction forces between cytc and peptide modified Au surfaces. The amine modified AFM probe tip interacts with the -COOH modified electrode surface allowing the functional groups to electrostatically bind. With more detail for charge interactions, one will be able to predict the best surfaces for protein immobilization while maintaining the protein, or enzymes, desired activity and use protein/surface engineering to tailor the protein function for any application.
Project II: Dr. Edward P. Zovinka (PI) Analyzing the Topographical Effects of Synthetic Aluminum Acid Mine Drainage on the Surface of Calcite Via Liquid Cell Atomic Force Microscopy
Acid mine drainage (AMD) is a common pollutant of waterways worldwide, resulting from extensive mining and incomplete cleanup. Using atomic force microscopy (AFM), our group is tracking the reaction of synthetic aluminum AMD on the surface of calcite, a material used to passively treat AMD. In a solution capable AFM cell, a calcite sample is exposed to 5 ppm synthetic Al solution with a pH of 3.5 (Figure 1). Over time, the calcite is eaten away due to the acid base reaction and aluminum oxides deposit on the surface.
With a solution cell capable AFM, the calcite/aluminum solution can be scanned continuously over the course of the reaction (Figure 2).
Through the project, a number of undergraduates were trained on the Hitachi 5100 AFM, expanding their techonological background and preparation for the workforce. Additionally, other SFU faculty were trained to use the instrument, thereby expanding the educational and research reach of the AFM.
REFERENCES
1) Manuscript accepted to Langmuir: Clark, R.A.; Yawitz, T.; Luchs, L.; Conrad, T.; Bartlebaugh, O.; Boyd, H.; Hargittai, B., Jan 2023
2) Takeda, K; Uchihashi, T; Watanabe, H.; Ishida, T; Igarashi, K; Nakamura, N; Ohno, H. Real-Time Dynamic Adsorption Processes of Cytochrome c on an Electrode Observed through Electrochemical High-Speed Atomic Force Microscopy PLoS ONE, 2015 10: e0116685. https://doi.org/10.1371/journal.pone.0116685.
3) Nakano, Koji; Yoshitake, Tadateru; Yamashita, Yasunori; Bowden. Edmond F. Cytochrome c Self-Assembly on Alkanethiol Monolayer Electrodes as Characterized by AFM, IR, QCM, and Direct Electrochemistry. Langmuir 2007, 23, 6270–75. https://doi.org/10.1021/la063697w.
4) Hobara, Daisuke; Imabayashi, Shin-ichiro; Kakiuchi, Takashi. Preferential Adsorption of Horse Heart Cytochrome c on Nanometer-Scale Domains of a Phase-Separated Binary Self-Assembled Monolayer of 3-Mercaptopropionic Acid and 1-Hexadecanethiol on Au(111). Nano Lett. 2002, 2, 1021–25. https://doi.org/10.1021/nl0256863.
Last Modified: 01/02/2023
Modified by: Edward P Zovinka
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