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Jung, Younghun,Yang, Gwangseok,Chun, Seungju,Kim, Donghwan,Kim, Jihyun Optical Society of America 2014 Optics express Vol.22 No.suppl3
<P>We investigated the morphological, structural and optical properties of CdCl2-treated cadmium telluride (CdTe) thin films deposited on defective graphene using a close-spaced sublimation (CSS) system. Heat treatment in the presence of CdCl2 caused recrystallization of CSS-grown CdTe over the as-deposited structures. The preferential (111) orientation of as-deposited CdTe films was randomized after post-growth CdCl2 treatment. New small grains (bumps) on the surface of CdCl2-treated CdTe films were ascribed to nucleation of the CdTe grains during the CdCl2 treatment. The properties of as-deposited and CdCl2-treated CdTe films were characterized by room temperature micro-photoluminescence, micro-Raman spectroscopy, scanning electron microscopy, and X-ray diffraction analysis. Our results are useful to demonstrate a substrate configuration CdTe thin film solar cells.</P>
Envelope-deforming antiviral peptide derived from influenza virus M2 protein
Jung, Younghun,Kong, Byoungjae,Moon, Seokoh,Yu, Seok-Hyeon,Chung, Jinhyo,Ban, Choongjin,Chung, Woo-Jae,Kim, Sung-Gun,Kweon, Dae-Hyuk Elsevier 2019 Biochemical and biophysical research communication Vol.517 No.3
<P><B>Abstract</B></P> <P>Molecules interfering with lipid bilayer function exhibit strong antiviral activity against a broad range of enveloped viruses, with a lower risk of resistance development than that for viral protein-targeting drugs. Amphipathic peptides are rich sources of such membrane-interacting antivirals. Here, we report that influenza viruses were effectively inactivated by M2 AH, an amphipathic peptide derived from the M2 protein of the influenza virus. Although overall hydrophobicity (<H>) of M2 AH was not related to antiviral activity, modification of the hydrophobic moment (<μH>) of M2 AH dramatically altered the antiviral activity of this peptide. M2 MH, a derivative of M2 AH with a <μH> of 0.874, showed a half maximal inhibitory concentration (IC<SUB>50</SUB>) of 53.3 nM against the A/PR/8/34 strain (H1N1), which is 16-times lower than that of M2 AH. The selectivity index (IC<SUB>50</SUB>/CC<SUB>50</SUB>), where CC<SUB>50</SUB> is the half maximal cytotoxic concentration, was 360 for M2 MH and 81 for M2 AH. Dynamic light scattering spectroscopy and electron microscopy revealed that M2 AH-derived peptides did not disrupt liposomes but altered the shape of viruses. This result suggests that the shape of virus envelope was closely related to its activity. Thus, we propose that deforming without rupturing the membranes may achieve a high selectivity index for peptide antivirals.</P> <P><B>Highlights</B></P> <P> <UL> <LI> M2 AH is an amphipathic peptide derived from influenza virus M2 protein. </LI> <LI> M2 MH with elevated hydrophobic moment was a strong antiviral with low toxicity. </LI> <LI> M2 AH and MH did not disrupt membrane but simply deformed the shape of virus. </LI> <LI> Deformation of viral envelope may achieve a high selectivity index for peptide antivirals. </LI> </UL> </P>