A set of diagnostic methods to obtain the plasma parameters including power dissipation, gas temperature and electron density is evaluated for an atmospheric pressure helium or argon radio frequency (RF) plasma needle for biomedical applications operated in open air. The power density of the plasma is more or less constant and equal to 1.3 × 10 9 W m −3 . Different methods are investigated and evaluated to obtain the gas temperature. In this paper the gas temperatures obtained by rotational spectra of OH(A-X) and N + 2 (B-X) are compared with Rayleigh scattering measurements and measurements of the line broadening of hydrogen and helium emission lines. The obtained gas temperature ranges from 300 to 650 K, depending on the gas. The electron densities are estimated from the Stark broadening of the hydrogen α and β lines which yield values between 10 19 and 10 20 m −3 . In the case of helium, this is an overestimate as is shown by a power balance from the measured power density in the plasma jet. The obtained plasma parameters enable us to explain the radial contraction of the argon plasma compared with the more diffuse helium plasma. The accuracy of all considered diagnostics is discussed in detail.
Proline-rich antimicrobial peptides (PrAMPs) internalize into susceptible bacteria using specific transporters and interfere with protein synthesis and folding. To date, mammalian PrAMPs have so far been identified only in artiodactyls. Since cetaceans are co-phyletic with artiodactyls, we mined the genome of the bottlenose dolphin Tursiops truncatus, leading to the identification of two PrAMPs, Tur1A and Tur1B. Tur1A, which is orthologous to the bovine PrAMP Bac7, is internalized into Escherichia coli, without damaging the membranes, using the inner membrane transporters SbmA and YjiL/MdM. Furthermore, like Bac7, Tur1A also inhibits bacterial protein synthesis by binding to the ribosome and blocking the transition from the initiation to the elongation phase. By contrast, Tur1B is a poor inhibitor of protein synthesis and may utilize another mechanism of action. An X-ray structure of Tur1A bound within the ribosomal exit tunnel provides a basis to develop these peptides as novel antimicrobial agents.
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