Observation of B0→D*-(5π)+, B+→D*-(4π)++ and B+→D̅*0 (5π)+

journal articl

Capitol Building-Constitution P.1

Front: Utah State Constitution Case. Lorenzo S. Young, Architect, November 14, 1939. Back: Utah Constitution, Lorenzo S. Young, October, 1940. Salt Lake Tribune #14573

SDS polyacrylamide gel showing synthetic pleurocidin (Ple) band at appx 3000 kd

<p><b>Copyright information:</b></p><p>Taken from "Recombinant Expression of Pleurocidin cDNA Using the Expression System"</p><p>Journal of Biomedicine and Biotechnology 2005;2005(4):374-384.</p><p>Published online Jan 2005</p><p>PMCID:PMC1361485.</p><p>Olive-Jean Burrowes et al</p

PCR analysis of transformed cells showing inserted pleurocidin cDNA at 590 bp

<p><b>Copyright information:</b></p><p>Taken from "Recombinant Expression of Pleurocidin cDNA Using the Expression System"</p><p>Journal of Biomedicine and Biotechnology 2005;2005(4):374-384.</p><p>Published online Jan 2005</p><p>PMCID:PMC1361485.</p><p>Olive-Jean Burrowes et al</p> M represents 500 bp marker. Lanes 2–5 represent transformed DNA ( KM71H and X-33). Lanes 6–7 represent control DNA (untransformed cells in lanes) indicated by parrallel arrows. Lanes 8–9 represent vector DNA (vector with and without insert). Lane 10 represents vector with transformed DNA. Lane 11 represents PCR control (no DNA) indicated by single arrow. Lanes 13–15 represent yeast DNA

Transcribed pleurocidin cDNA bands at 590 b from transformed KMH 71cells at days 5 and 6 (+RT) and gel containing transformed KMH 71 cells (−RT); positive control shown in lane 48

<p><b>Copyright information:</b></p><p>Taken from "Recombinant Expression of Pleurocidin cDNA Using the Expression System"</p><p>Journal of Biomedicine and Biotechnology 2005;2005(4):374-384.</p><p>Published online Jan 2005</p><p>PMCID:PMC1361485.</p><p>Olive-Jean Burrowes et al</p

Peptidomimetic Oligomers Targeting Membrane Phosphatidylserine Exhibit Broad Antiviral Activity

The development of durable new antiviral therapies is challenging, as viruses can evolve rapidly to establish resistance and attenuate therapeutic efficacy. New compounds that selectively target conserved viral features are attractive therapeutic candidates, particularly for combating newly emergent viral threats. The innate immune system features a sustained capability to combat pathogens through production of antimicrobial peptides (AMPs); however, these AMPs have shortcomings that can preclude clinical use. The essential functional features of AMPs have been recapitulated by peptidomimetic oligomers, yielding effective antibacterial and antifungal agents. Here, we show that a family of AMP mimetics, called peptoids, exhibit direct antiviral activity against an array of enveloped viruses, including the key human pathogens Zika, Rift Valley fever, and chikungunya viruses. These data suggest that the activities of peptoids include engagement and disruption of viral membrane constituents. To investigate how these peptoids target lipid membranes, we used liposome leakage assays to measure membrane disruption. We found that liposomes containing phosphatidylserine (PS) were markedly sensitive to peptoid treatment; in contrast, liposomes formed exclusively with phosphatidylcholine (PC) showed no sensitivity. In addition, chikungunya virus containing elevated envelope PS was more susceptible to peptoid-mediated inactivation. These results indicate that peptoids mimicking the physicochemical characteristics of AMPs act through a membrane-specific mechanism, most likely through preferential interactions with PS. We provide the first evidence for the engagement of distinct viral envelope lipid constituents, establishing an avenue for specificity that may enable the development of a new family of therapeutics capable of averting the rapid development of resistance

伝送路の状態を考慮したマルチキャリヤ伝送用回線制御方式

マルチキャリヤ信号のサブキャリヤから伝送路の状態を比較的容易に推定できることに着目し、これを利用して伝送品質を向上させるマルチキャリヤ伝送用の回線制御方式を提案する。提案方式では、受信電力が小さく伝送品質が劣化していると予想されるサブキャリヤにはデータを割り当てずにダミーキャリヤとして送信し、受信電力が大きく伝送品質が良好であると予想されるサブキャリヤのみにデータを割り当てて伝送する。移動通信環境を想定した性能評価の結果、すべてのサブキャリヤにデータを割り当てる通常のマルチキャリヤ伝送方式に比べ、受信レベルの低いサブキャリヤをダミーキャリヤとしてデータを割り当てない提案方式のほうが、伝送効率が向上することを示す。更に提案方式における誤り訂正符号の効果を明らかにする。journal articl

Self-Assembly of Antimicrobial Peptoids Impacts Their Biological Effects on <i>ESKAPE</i> Bacterial Pathogens

Antimicrobial peptides (AMPs) are promising pharmaceutical candidates for the prevention and treatment of infections caused by multidrug-resistant ESKAPE pathogens, which are responsible for the majority of hospital-acquired infections. Clinical translation of AMPs has been limited, in part by apparent toxicity on systemic dosing and by instability arising from susceptibility to proteolysis. Peptoids (sequence-specific oligo-N-substituted glycines) resist proteolytic digestion and thus are of value as AMP mimics. Only a few natural AMPs such as LL-37 and polymyxin self-assemble in solution; whether antimicrobial peptoids mimic these properties has been unknown. Here, we examine the antibacterial efficacy and dynamic self-assembly in aqueous media of eight peptoid mimics of cationic AMPs designed to self-assemble and two nonassembling controls. These amphipathic peptoids self-assembled in different ways, as determined by small-angle X-ray scattering; some adopt helical bundles, while others form core–shell ellipsoidal or worm-like micelles. Interestingly, many of these peptoid assemblies show promising antibacterial, antibiofilm activity in vitro in media, under host-mimicking conditions and antiabscess activity in vivo. While self-assembly correlated overall with antibacterial efficacy, this correlation was imperfect. Certain self-assembled morphologies seem better-suited for antibacterial activity. In particular, a peptoid exhibiting a high fraction of long, worm-like micelles showed reduced antibacterial, antibiofilm, and antiabscess activity against ESKAPE pathogens compared with peptoids that form ellipsoidal or bundled assemblies. This is the first report of self-assembling peptoid antibacterials with activity against in vivo biofilm-like infections relevant to clinical medicine