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Identification of Porphyrin-Silica Composite Nanoparticles using Atmospheric Solids Analysis Probe Mass Spectrometry

MRS Advances

Karler, Casey; Parchert, Kylea J.; Ricken, James B.; Carson, Bryan C.; Mowry, Curtis D.; Fan, Hongyou F.; Ye, Dongmei Y.

Porphyrins are vital pigments involved in biological energy transduction processes. Their abilities to absorb light, then convert it to energy, have raised the interest of using porphyrin nanoparticles as photosensitizers in photodynamic therapy. A recent study showed that self- assembled porphyrin-silica composite nanoparticles can selectively destroy tumor cells, but detection of the cellular uptake of porphyrin-silica composite nanoparticles was limited to imaging microscopy. Here we developed a novel method to rapidly identify porphyrin-silica composite nanoparticles using Atmospheric Solids Analysis Probe-Mass Spectrometry (ASAP-MS). ASAP-MS can directly analyze complex mixtures without the need for sample preparation. Porphyrin-silica composite nanoparticles were vaporized using heated nitrogen desolvation gas, and their thermo-profiles were examined to identify distinct mass- to-charge (M/Z) signatures. HeLa cells were incubated in growth media containing the nanoparticles, and after sufficient washing to remove residual nanoparticles, the cell suspension was loaded onto the end of ASAP glass capillary probe. Upon heating, HeLa cells were degraded and porphyrin-silica composite nanoparticles were released. Vaporized nanoparticles were ionized and detected by MS. The cellular uptake of porphyrin-silica composite nanoparticles was identified using this ASAP-MS method.

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TYPE Journal Article YEAR 2019
ScopusOSTIDOI

Posters for AA/CE Reception

Kuether, Robert J.; Allensworth, Brooke M.; Backer, Adam B.; Chen, Elton Y.; Dingreville, Remi P.; Forrest, Eric C.; Knepper, Robert; Tappan, Alexander S.; Marquez, Michael P.; Vasiliauskas, Jonathan G.; Rupper, Stephen G.; Grant, Michael J.; Atencio, Lauren C.; Hipple, Tyler J.; Maes, Danae M.; Timlin, Jerilyn A.; Ma, Tian J.; Garcia, Rudy J.; Danford, Forest L.; Patrizi, Laura P.; Galasso, Jennifer G.; Draelos, Timothy J.; Gunda, Thushara G.; Venezuela, Otoniel V.; Brooks, Wesley A.; Anthony, Stephen M.; Carson, Bryan C.; Reeves, Michael J.; Roach, Matthew R.; Maines, Erin M.; Lavin, Judith M.; Whetten, Shaun R.; Swiler, Laura P.

Abstract not provided.

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TYPE Presentation YEAR 2018
OSTI

Method for measuring the unbinding energy of strongly-bound membrane-associated proteins

Biochimica et Biophysica Acta - Biomembranes

La Bauve, Elisa; Vernon, Briana C.; Ye, Dongmei Y.; Rogers, David M.; Siegrist, Cathryn M.; Carson, Bryan C.; Rempe, Susan R.; Zheng, Aihua; Kielian, Margaret; Shreve, Andrew P.; Kent, Michael S.

We describe a new method to measure the activation energy for unbinding (enthalpy ΔH*u and free energy ΔG*u) of a strongly-bound membrane-associated protein from a lipid membrane. It is based on measuring the rate of release of a liposome-bound protein during centrifugation on a sucrose gradient as a function of time and temperature. The method is used to determine ΔH*u and ΔG*u for the soluble dengue virus envelope protein (sE) strongly bound to 80:20 POPC:POPG liposomes at pH 5.5. ΔH*u is determined from the Arrhenius equation whereas ΔG*u is determined by fitting the data to a model based on mean first passage time for escape from a potential well. The binding free energy ΔGb of sE was also measured at the same pH for the initial, predominantly reversible, phase of binding to a 70:30 PC:PG lipid bilayer. The unbinding free energy (20 ± 3 kcal/mol, 20% PG) was found to be roughly three times the binding energy per monomer, (7.8 ± 0.3 kcal/mol for 30% PG, or est. 7.0 kcal/mol for 20% PG). This is consistent with data showing that free sE is a monomer at pH 5.5, but assembles into trimers after associating with membranes. This new method to determine unbinding energies should be useful to understand better the complex interactions of integral monotopic proteins and strongly-bound peripheral membrane proteins with lipid membranes.

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TYPE Journal Article YEAR 2016
ScopusOSTIDOI

New Method for Measuring the Anchoring Energy of Strongly-Bound Membrane-Associated Proteins [Method for measuring the anchoring energy of strongly-bound membrane-associated proteins]

Biophysical Journal

Kent, Michael S.; La Bauve, Elisa L.; Vernon, Briana C.; Ye, Dongmei Y.; Rogers, David M.; Mayes, Cathryn M.; Carson, Bryan C.; Rempe, Susan R.; Zheng, Aihua Z.; Kielian, Margaret K.; Shreve, Andrew S.; Kent, Michael S.

Here, we describe a new method to measure the activation energy required to remove a strongly-bound membrane-associated protein from a lipid membrane (anchoring energy). It is based on measuring the rate of release of a liposome-bound protein during centrifugation on a sucrose gradient as a function of time and temperature. The method was used to determine anchoring energy for the soluble dengue virus envelope protein (sE) strongly bound to 80:20 POPC:POPG liposomes at pH 5.5. We also measured the binding energy of sE at the same pH for the initial, predominantly reversible, phase of binding to a 70:30 PC:PG lipid bilayer. The anchoring energy (37 +/- 1.7 kcal/mol, 20% PG) was found to be much larger than the binding energy (7.8 +/- 0.3 kcal/mol for 30% PG, or est. 7.0 kcal/mol for 20% PG). This is consistent with data showing that free sE is a monomer at pH 5.5, but assembles into trimers after associating with membranes. But, trimerization alone is insufficient to account for the observed difference in energies, and we conclude that some energy dissipation occurs during the release process. This new method to determine anchoring energy should be useful to understand the complex interactions of integral monotopic proteins and strongly-bound peripheral membrane proteins with lipid membranes.

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TYPE Journal Article YEAR 2016
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Laser Machined Plastic Laminates: Towards Portable Diagnostic Devices for Use in Low Resource Environments

Electroanalysis

Harper, Jason C.; Carson, Bryan C.; Bachand, George B.; Arndt, William A.; Finley, Melissa F.; Brinker, C.J.; Edwards, Thayne L.

Despite significant progress in development of bioanalytical devices cost, complexity, access to reagents and lack of infrastructure have prevented use of these technologies in resource-limited regions. To provide a sustainable tool in the global effort to combat infectious diseases the diagnostic device must be low cost, simple to operate and read, robust, and have sensitivity and specificity comparable to laboratory analysis. In this mini-review we describe recent work using laser machined plastic laminates to produce diagnostic devices that are capable of a wide variety of bioanalytical measurements and show great promise towards future use in low-resource environments.

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TYPE Journal Article YEAR 2015
ScopusOSTIDOI
Results 1–25 of 65
Results 1–25 of 65