Publications by authors named "P Butko"

The S4 transmembrane segment in voltage-gated ion channels, a highly basic alpha helix, responds to changes in membrane potential and induces channel opening. Earlier work by others indicates that the S4 segment interacts with lipids in plasma membrane, but its mechanism is unclear. Working with synthetic tryptophan-labeled S4 peptides, we characterized binding of autonomous S4 to lipid membranes.

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We used fluorescence spectroscopy and surface tensiometry to study the interaction between low-generation (G1 and G4) poly(amidoamine) (PAMAM) dendrimers, potential vehicles for intracellular drug delivery, and model lipid bilayers. Membrane association of fluorescently labeled dendrimers, measured by fluorescence anisotropy, increased with increasing size of the dendrimer and with increasing negative charge density in the membrane, indicating the electrostatic nature of the interaction. When the membrane was doped with pyrene-labeled phosphatidyl glycerol (pyrene-PG), pyrene excimer fluorescence demonstrated a dendrimer-induced selective aggregation of negatively charged lipids when the membrane was in the liquid crystalline state.

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Objectives: To compare student academic performance and the student experience in the first-year doctor of pharmacy (PharmD) program between the main and newly opened satellite campuses of the University of Maryland.

Methods: Student performance indicators including graded assessments, course averages, cumulative first-year grade point average (GPA), and introductory pharmacy practice experience (IPPE) evaluations were analyzed retrospectively. Student experience indicators were obtained via an online survey instrument and included involvement in student organizations; time-budgeting practices; and stress levels and their perceived effect on performance.

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Cyt1A is a cytolytic toxin from Bacillus thuringiensis var. israelensis. A computer model of the toxin in solution was generated and validated by resonance energy transfer (RET).

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Protein-transduction domains (PTDs) have been shown to translocate into and through the living cells in a rapid manner by an as yet unknown mechanism. Regardless of the mechanism of translocation, the first necessary step must be binding of the PTD peptide to the surface of the lipid membrane. We used fluorescence spectroscopy to study the interaction between PTD of the HIV-1 Tat protein (TAT-PTD; residues 47-60 of Tat, fluorescently labeled with tryptophan) and the lipid bilayer labeled with various fluorescence membrane probes.

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