The Mass of Kepler-93b and The Composition of Terrestrial Planets

Kepler-93b is a 1.478 ± 0.019 R ⊕ planet with a4.7 day period around a bright (V = 10.2), astroseismicallycharacterized host star with a mass of 0.911 ± 0.033 M⊙ and a radius of 0.919 ± 0.011 R⊙. Based on 86 radial velocity observations obtainedwith the HARPS-N spectrograph on the Telescopio Nazionale Galileo and 32archival Keck/HIRES observations, we present a precise mass estimate of4.02 ± 0.68 M ⊕. The corresponding high densityof 6.88 ± 1.18 g cm-3 is consistent with a rockycomposition of primarily iron and magnesium silicate. We compareKepler-93b to other dense planets with well-constrained parameters andfind that between 1 and 6 M ⊕, all dense planetsincluding the Earth and Venus are well-described by the same fixed ratioof iron to magnesium silicate. There are as of yet no examples of suchplanets with masses >6 M ⊕. All known planets inthis mass regime have lower densities requiring significant fractions ofvolatiles or H/He gas. We also constrain the mass and period of theouter companion in the Kepler-93 system from the long-term radialvelocity trend and archival adaptive optics images. As the sample ofdense planets with well-constrained masses and radii continues to grow,we will be able to test whether the fixed compositional model found forthe seven dense planets considered in this paper extends to the fullpopulation of 1-6 M ⊕ planets.Based on observations made with the Italian Telescopio Nazionale Galileo(TNG) operated on the island of La Palma by the Fundación GalileoGalilei of the INAF (Istituto Nazionale di Astrofisica) at the SpanishObservatorio del Roque de los Muchachos of the Instituto de Astrofisicade Canarias.

A Combined Molecular Cloning and Mass Spectrometric Method to Identify, Characterize, and Design Frenatin Peptides from the Skin Secretion of Litoria infrafrenata

Amphibian skin secretions are unique sources of bioactive molecules, particularly bioactive peptides. In this study, the skin secretion of the white-lipped tree frog (Litoria infrafrenata) was obtained to identify peptides with putative therapeutic potential. By utilizing skin secretion-derived mRNA, a cDNA library was constructed, a frenatin gene was cloned and its encoded peptides were deduced and confirmed using RP-HPLC, MALDI-TOF and MS/MS. The deduced peptides were identified as frenatin 4.1 (GFLEKLKTGAKDFASAFVNSIKGT) and a post-translationally modified peptide, frenatin 4.2 (GFLEKLKTGAKDFASAFVNSIK.NH2). Antimicrobial activity of the peptides was assessed by determining their minimal inhibitory concentrations (MICs) using standard model microorganisms. Through studying structure–activity relationships, analogues of the two peptides were designed, resulting in synthesis of frenatin 4.1a (GFLEKLKKGAKDFASALVNSIKGT) and frenatin 4.2a (GFLLKLKLGAKLFASAFVNSIK.NH2). Both analogues exhibited improved antimicrobial activities, especially frenatin 4.2a, which displayed significant enhancement of broad spectrum antimicrobial efficiency. The peptide modifications applied in this study, may provide new ideas for the generation of leads for the design of antimicrobial peptides with therapeutic applications.