Intended and Unintended Consequences and Applications of Unnatural Interfaces: Oligo <i>p</i>-Phenylene Ethynylene Electrolytes, Biological Cells and Biomacromolecules

This short review focuses on an extended study of synthetic oligomericphenyleneethynylene (OPE) electrolytes that have been investigated for both their antimicrobial activity and their fluorescence sensing properties. In both cases, interfaces between these synthetic electrolytes and naturally occurring materials such as proteins, lipids, nucleic acids and cells are critical to their function or activity. The review contains a general overview with a focus at the end on three recent examples including biological and chemical sensing, induction of spore germination and fluorescent detection of amyloid protein aggregates.

Keywords:
conjugated polyelectrolyte; phenylene ethynylene; oligomer; biosensing; biocide; bactéria

Authorship

Harry C. Pappas

Department of Nanoscience and Microsystems Engineering, University of New Mexico, 87131-1341 Albuquerque-New Mexico, United States of AmericaUniversity of New MexicoUSAAlbuquerque, New Mexico, USADepartment of Nanoscience and Microsystems Engineering, University of New Mexico, 87131-1341 Albuquerque-New Mexico, United States of America

Center for Biomedical Engineering, Department of Chemical and Biological Engineering, University of New Mexico, 87131-1341 Albuquerque-New Mexico, United States of AmericaUniversity of New MexicoUSAAlbuquerque, New Mexico, USACenter for Biomedical Engineering, Department of Chemical and Biological Engineering, University of New Mexico, 87131-1341 Albuquerque-New Mexico, United States of America

Patrick L. Donabedian

Kirk S. Schanze ^**e-mail: kschanze@chem.ufl.edu,whitten@unm.edu

Department of Chemistry, University of Florida, 32611-7200 Gainesville-Florida, United States of AmericaUniversity of FloridaUSAGainesville, Florida, USADepartment of Chemistry, University of Florida, 32611-7200 Gainesville-Florida, United States of America

David G. Whitten ^**e-mail: kschanze@chem.ufl.edu,whitten@unm.edu

*e-mail: kschanze@chem.ufl.edu,whitten@unm.edu

Harry C. Pappas obtained his bachelor's degree from the College of Engineering, University of Massachusetts Amherst in 2010. He is currently a PhD student under the supervision of Prof David G. Whitten at the University of New Mexico. His research is focused on evaluating the biocidal activity of phenylene ethynylene-based compounds, and in particular, the mechanisms by which they induce stress responses in bacteria.

Patrick L. Donabedian received his BSc in Liberal Arts from St. John's College in 2012, and is currently a PhD student in Nanoscience Engineering in the labs of Prof David Whitten and Prof Eva Chi at the University of New Mexico, Albuquerque, New Mexico, USA.

Kirk Schanze earned his BSc in Chemistry from Florida State University in 1979 and his PhD in Chemistry from the University of North Carolina at Chapel Hill in 1983. He was appointed a Miller Postdoctoral Fellow at the University of California, Berkeley, from 1984-1986 and began his independent faculty career at the University of Florida in 1986. Schanze is currently University Distinguished Professor and Prominski Professor of Chemistry at the University of Florida. He has authored or co-authored more than 275 peer-reviewed articles on basic and applied research topics, with a primary focus on organic and organometallic materials chemistry.

David G. Whitten earned a PhD degree at Johns Hopkins University in 1963. After 2 years as an Army officer and a postdoctoral at Caltech, he joined the University of North Carolina in 1966 and rose to become Smith Professor. He joined the University of Rochester in 1983 as C. E. Kenneth Mees Professor of Chemistry. In 1997 he moved to Los Alamos and studied conjugated polyelectrolytes. In 2000 he co-founded QTL Biosystems, a company developing biosensing technology for drug discovery and defense. He moved to the University of New Mexico in 2005 where he is Professor of Chemical Engineering.

SCIMAGO INSTITUTIONS RANKINGS

Figures

Figures (16)

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Figure 1
Structure of PPE-1.

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Figure 2
Structures and names for representative OPEs discussed in this paper.

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Figure 3
Enzyme cleavage sites in a phospholipid.

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Figure 4
S-OPE-1 (n = 1) (cationic and anionic), (n = 2) (cationic) and lipid substrates DLPG and lauroyl choline chloride. Cationic OPE used with DLPG, anionic OPE used with lauroyl choline chloride. Reprinted with permission from Ref. 27. Copyright 2015 American Chemical Society.

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Figure 5
(a) Cationic OPE-2 fluorescence vs. time for PLA1; (b) PLA2. Fluorescence measured at a temperature of 25 °C, and a pH of 7.5. Reprinted with permission from Ref. 27. Copyright 2015 American Chemical Society.

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Figure 6
(a) Absorbance; (b) fluorescence of S-OPE-1^- (COOEt) and LaCh at 0.2, 0.4 and 0.6 U of AChE. Reprinted with permission from Ref. 27. Copyright 2015 American Chemical Society.

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Figure 7
S-OPE-1 (COOEt)/LaCh complex (5 µmol L^-1 OPE, 32 µmol L^-1 LaCh) showing fluorescence change after addition of 0.6 U of AChE in the presence of AChE inhibitor (a) itopride HCl; (b) meptazinol HCl; (c) TAE-1. Traces with inhibitor are denoted with +I and the inhibitor. Reprinted with permission from Ref. 27. Copyright 2015 American Chemical Society.

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Figure 8
Structure of EO-OPE (Th,C2).

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Figure 9
Bacillus atrophaeus spores visualized via SEM. (a) Spores suspended in physiological saline solution for 5 h in the dark; (b) spores exposed to 20 µg mL^-1 OPE for 5 h in the dark; (c) spores suspended in physiological saline solution for 5 h in UVA light; (d) and (e) spores exposed to 20 µg mL^-1 OPE for 5 h in UVA light. Scale bars spanning 3 µm are included. Arrows indicate spore coat remnants. Reprinted with permission from Ref. 42. Copyright 2015 American Chemical Society.

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Figure 10
B. anthracis Sterne spore and germinated vegetative cell viability as a function of starting concentration. (a) OPE exposed to varying spore concentrations for 90 min durations in the absence of UVA light; (b) presence of UVA light. Viability was inferred based on the spore's capacity to grow colonies on TSA before and after heat treatment. Reprinted with permission from Ref. 42. Copyright 2015 American Chemical Society.

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Figure 11
(a) TEM (top) and AFM (bottom) images of hen egg white lysozyme amyloids incubated for 4 hours, showing short bunched fibrils. Scale bars 200 nm. Inset: isolated fibril showing double-braid morphology, scale bar 50 nm; (b) structure of example OPE investigated (-1C); (c) spectroscopic changes observed upon amyloid binding: left, excitation spectrum of OPE alone (black dashed line), OPE (500 nmol L^-1) with monomeric HEWL (5 µmol L^-1) (red dotted line) and OPE with HEWL amyloid (5 µmol L^-1 monomerper 250 µg mL^-1) (blue solid line); middle, emission spectrum of OPE alone (black dashed line), OPE with monomeric HEWL (red dotted line) and OPE with HEWL amyloid (blue solid line); right, circular dichroism of OPE (10 µmol L^-1) with HEWL monomer (500 µg mL^-1) (black trace) and OPE with HEWL amyloid (500 µg mL^-1) (red trace). OPE alone has no CD signal. Partially reprinted with permission from Ref. 43. Copyright 2015 American Chemical Society.

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Figure 12
Emission spectra at λ_ex = 280 nm, showing decrease of HEWL intrinsic fluorescence due to solvent exposure of aromatic residues during refolding and aggregation process and appearance of HEWL

Figure 1 Structure of PPE-1.

Figure 2 Structures and names for representative OPEs discussed in this paper.

Figure 3 Enzyme cleavage sites in a phospholipid.

Figure 4 S-OPE-1 (n = 1) (cationic and anionic), (n = 2) (cationic) and lipid substrates DLPG and lauroyl choline chloride. Cationic OPE used with DLPG, anionic OPE used with lauroyl choline chloride. Reprinted with permission from Ref. 27. Copyright 2015 American Chemical Society.

Figure 5 (a) Cationic OPE-2 fluorescence vs. time for PLA1; (b) PLA2. Fluorescence measured at a temperature of 25 °C, and a pH of 7.5. Reprinted with permission from Ref. 27. Copyright 2015 American Chemical Society.

Figure 6 (a) Absorbance; (b) fluorescence of S-OPE-1^- (COOEt) and LaCh at 0.2, 0.4 and 0.6 U of AChE. Reprinted with permission from Ref. 27. Copyright 2015 American Chemical Society.

Figure 7 S-OPE-1 (COOEt)/LaCh complex (5 µmol L^-1 OPE, 32 µmol L^-1 LaCh) showing fluorescence change after addition of 0.6 U of AChE in the presence of AChE inhibitor (a) itopride HCl; (b) meptazinol HCl; (c) TAE-1. Traces with inhibitor are denoted with +I and the inhibitor. Reprinted with permission from Ref. 27. Copyright 2015 American Chemical Society.

Figure 8 Structure of EO-OPE (Th,C2).

Figure 9 Bacillus atrophaeus spores visualized via SEM. (a) Spores suspended in physiological saline solution for 5 h in the dark; (b) spores exposed to 20 µg mL^-1 OPE for 5 h in the dark; (c) spores suspended in physiological saline solution for 5 h in UVA light; (d) and (e) spores exposed to 20 µg mL^-1 OPE for 5 h in UVA light. Scale bars spanning 3 µm are included. Arrows indicate spore coat remnants. Reprinted with permission from Ref. 42. Copyright 2015 American Chemical Society.

Figure 10 B. anthracis Sterne spore and germinated vegetative cell viability as a function of starting concentration. (a) OPE exposed to varying spore concentrations for 90 min durations in the absence of UVA light; (b) presence of UVA light. Viability was inferred based on the spore's capacity to grow colonies on TSA before and after heat treatment. Reprinted with permission from Ref. 42. Copyright 2015 American Chemical Society.

Figure 11 (a) TEM (top) and AFM (bottom) images of hen egg white lysozyme amyloids incubated for 4 hours, showing short bunched fibrils. Scale bars 200 nm. Inset: isolated fibril showing double-braid morphology, scale bar 50 nm; (b) structure of example OPE investigated (-1C); (c) spectroscopic changes observed upon amyloid binding: left, excitation spectrum of OPE alone (black dashed line), OPE (500 nmol L^-1) with monomeric HEWL (5 µmol L^-1) (red dotted line) and OPE with HEWL amyloid (5 µmol L^-1 monomerper 250 µg mL^-1) (blue solid line); middle, emission spectrum of OPE alone (black dashed line), OPE with monomeric HEWL (red dotted line) and OPE with HEWL amyloid (blue solid line); right, circular dichroism of OPE (10 µmol L^-1) with HEWL monomer (500 µg mL^-1) (black trace) and OPE with HEWL amyloid (500 µg mL^-1) (red trace). OPE alone has no CD signal. Partially reprinted with permission from Ref. 43. Copyright 2015 American Chemical Society.

Figure 12 Emission spectra at λ_ex = 280 nm, showing decrease of HEWL intrinsic fluorescence due to solvent exposure of aromatic residues during refolding and aggregation process and appearance of HEWL OPE FRET signal in OPE/amyloid mixture. Partially reprinted with permission from Ref. 43. Copyright 2015 American Chemical Society.

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Intended and Unintended Consequences and Applications of Unnatural Interfaces: Oligo <i>p</i>-Phenylene Ethynylene Electrolytes, Biological Cells and Biomacromolecules

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[1] *e-mail: kschanze@chem.ufl.edu,whitten@unm.edu