| 1. |
- Currie, Thayne, et al.
(författare)
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Subaru/SCExAO First-light Direct Imaging of a Young Debris Disk around HD 36546
- 2017
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Ingår i: Astrophysical Journal Letters. - 2041-8205 .- 2041-8213. ; 836:1
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Tidskriftsartikel (refereegranskat)abstract
- We present H-band scattered light imaging of a bright debris disk around the A0 star HD 36546 obtained from the Subaru Coronagraphic Extreme Adaptive Optics (SCExAO) system with data recorded by the HiCIAO camera using the vector vortex coronagraph. SCExAO traces the disk from r similar to 0.3 to r similar to 1 (34-114 au). The disk is oriented in a near east-west direction (PA similar to 75 degrees), is inclined by i similar to 70 degrees-75 degrees, and is strongly forward-scattering (g > 0.5). It is an extended disk rather than a sharp ring; a second, diffuse dust population extends from the disk's eastern side. While HD 36546 intrinsic properties are consistent with a wide age range (t similar to 1-250 Myr), its kinematics and analysis of coeval stars suggest a young age (3-10 Myr) and a possible connection to Taurus-Auriga's star formation history. SCExAO's planet-to-star contrast ratios are comparable to the first-light Gemini Planet Imager contrasts; for an age of 10 Myr, we rule out planets with masses comparable to HR 8799 b beyond a projected separation of 23 au. A massive icy planetesimal disk or an unseen super-Jovian planet at r > 20 au may explain the disk's visibility. The HD 36546 debris disk may be the youngest debris disk yet imaged, is the first newly identified object from the now-operational SCExAO extreme AO system, is ideally suited for spectroscopic follow-up with SCExAO/CHARIS in 2017, and may be a key probe of icy planet formation and planet-disk interactions.
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| 2. |
- Mann, Anita, et al.
(författare)
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Differences in DNA Condensation and Release by Lysine and Arginine Homopeptides Govern Their DNA Delivery Efficiencies
- 2011
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Ingår i: Molecular Pharmaceutics. - : American Chemical Society (ACS). - 1543-8384 .- 1543-8392. ; 8:5, s. 1729-1741
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Tidskriftsartikel (refereegranskat)abstract
- Designing of nanocarriers that can efficiently deliver therapeutic DNA payload and allow its smooth intracellular release for transgene expression is still a major constraint. The optimization of DNA nanocarriers requires thorough understanding of the chemical and structural characteristics of the vector-nucleic acid complexes and its correlation with the cellular entry, intracellular state and transfection efficiency. L-Lysine and L-arginine based cationic peptides alone or in conjugation with other vectors are known to be putative DNA delivery agents. Here we have used L-lysine and L-arginine homopeptides of three different lengths and probed their DNA condensation and release properties by using a multitude of biophysical techniques including fluorescence spectroscopy, gel electrophoresis and atomic force microscopy. Our results clearly showed that although both lysine and arginine based homopeptides condense DNA via electrostatic interactions, they follow different pattern of DNA condensation and release in vitro. While lysine homopeptides condense DNA to form both monomolecular and multimolecular complexes and show differential release of DNA in vitro depending on the peptide length, arginine homopeptides predominantly form multimolecular complexes and show complete DNA release for all peptide lengths. The cellular uptake of the complexes and their intracellular state (as observed through flow cytometry and fluorescence microscopy) seem to be controlled by the peptide chemistry. The difference in the transfection efficiency of lysine and arginine homopeptides has been rationalized in light of these observations.
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