Nethaniah Dorh
Michigan Technological University, Chemistry, Graduate Student
Mapping surface hydrophobic interactions in proteins is key to understanding molecular recognition, biological functions, and is central to many protein misfolding diseases. Herein, we report synthesis and application of new BODIPY-based... more
Mapping surface hydrophobic interactions in proteins is key to understanding molecular recognition, biological functions, and is central to many protein misfolding diseases. Herein, we report synthesis and application of new BODIPY-based hydrophobic sensors (HPsensors) that are stable and highly fluorescent for pH values ranging from 7.0 to 9.0. Surface hydrophobic measurements of proteins (BSA, apomyoglobin, and myoglobin) by these HPsensors display much stronger signal compared to 8-anilino-1-naphthalene sulfonic acid (ANS), a commonly used hydrophobic probe; HPsensors show a 10- to 60-fold increase in signal strength for the BSA protein with affinity in the nanomolar range. This suggests that these HPsensors can be used as a sensitive indicator of protein surface hydrophobicity. A first principle approach is used to identify the molecular level mechanism for the substantial increase in the fluorescence signal strength. Our results show that conformational change and increased mol...
Research Interests:
Neuroscience, Chemistry, Surface Science, Quantum Theory, Fluorescence, and 14 moreNeurodegenerative Diseases, Protein Chemistry, Animals, Cattle, Myoglobin, Food Protein Chemistry, Bovine Serum Albumin, Protein Binding, BODIPY, Hydrogen-Ion Concentration, Boron Compounds, Apoproteins, Surface hydrophobicity, and fluorescent dyes
We report five fluorescent probes based on coumarin-hybridized fluorescent dyes with spirolactam ring structures (A-E) to detect pH changes in live cell by monitoring visible and near-infrared fluorescence changes. Under physiological or... more
We report five fluorescent probes based on coumarin-hybridized fluorescent dyes with spirolactam ring structures (A-E) to detect pH changes in live cell by monitoring visible and near-infrared fluorescence changes. Under physiological or basic conditions, the fluorescent probes A, B, C, D and E preserve their spirolactam ring-closed forms and only display fluorescent peaks in the visible region corresponding to coumarin moieties at 497, 483, 498, 497 and 482 nm, respectively. However, at acidic pH, the rings of the spirolactam forms of the fluorescent probes A, B, C, D and E open up, generating new near-infrared fluorescence peaks at 711, 696, 707, 715, and 697 nm, respectively, through significantly extended π-conjugation to coumarin moieties of the fluorophores. The fluorescent probes B and E can be applied to visualize pH changes by monitoring visible as well as near-infrared fluorescence changes. This helps avoid fluorescence imaging blind spots at neutral or basic pH, which typ...
Research Interests:
Research Interests:
Research Interests:
Research Interests:
The development of synthesis processes to make high quality Single-Walled Carbon Nanotubes have been the focus of many researchers in different fields since this type of carbon material was discovered in 1991. Despite all these efforts,... more
The development of synthesis processes to make high quality Single-Walled Carbon Nanotubes have been the focus of many researchers in different fields since this type of carbon material was discovered in 1991. Despite all these efforts, only a few methods succeeded to produce high quality SWNT with minimal amounts of other carbon species. Among them, the CoMoCAT process, developed at the University of Oklahoma, has differentiated itself from the others since it does not only show great selectivity towards SWNT but it is also capable of producing nanotubes with narrow diameter and chirality distributions. Moreover, the CoMoCat process can be tuned to produce different types of nanotubes by changing operating conditions such us reaction temperature and feedstock composition. The different (n,m) species produced under different set of conditions have been determined by optical absorption. Interestingly it was found that although the nanotubes produced at different temperatures show a b...
Mapping surface hydrophobic interactions in proteins is key to understanding molecular recognition, biological functions, and is central to many protein misfolding diseases. Herein, we report synthesis and application of new BODIPY-based... more
Mapping surface hydrophobic interactions in proteins is key to understanding molecular recognition,
biological functions, and is central to many protein misfolding diseases. Herein, we report synthesis
and application of new BODIPY-based hydrophobic sensors (HPsensors) that are stable and highly
fluorescent for pH values ranging from 7.0 to 9.0. Surface hydrophobic measurements of proteins
(BSA, apomyoglobin, and myoglobin) by these HPsensors display much stronger signal compared to
8-anilino-1-naphthalene sulfonic acid (ANS), a commonly used hydrophobic probe; HPsensors show a
10- to 60-fold increase in signal strength for the BSA protein with affinity in the nanomolar range. This
suggests that these HPsensors can be used as a sensitive indicator of protein surface hydrophobicity. A
first principle approach is used to identify the molecular level mechanism for the substantial increase in
the fluorescence signal strength. Our results show that conformational change and increased molecular
rigidity of the dye due to its hydrophobic interaction with protein lead to fluorescence enhancement.
biological functions, and is central to many protein misfolding diseases. Herein, we report synthesis
and application of new BODIPY-based hydrophobic sensors (HPsensors) that are stable and highly
fluorescent for pH values ranging from 7.0 to 9.0. Surface hydrophobic measurements of proteins
(BSA, apomyoglobin, and myoglobin) by these HPsensors display much stronger signal compared to
8-anilino-1-naphthalene sulfonic acid (ANS), a commonly used hydrophobic probe; HPsensors show a
10- to 60-fold increase in signal strength for the BSA protein with affinity in the nanomolar range. This
suggests that these HPsensors can be used as a sensitive indicator of protein surface hydrophobicity. A
first principle approach is used to identify the molecular level mechanism for the substantial increase in
the fluorescence signal strength. Our results show that conformational change and increased molecular
rigidity of the dye due to its hydrophobic interaction with protein lead to fluorescence enhancement.