130985-36-3Relevant academic research and scientific papers
Nanoscale ionic diodes with tunable and switchable rectifying behavior
Macrae, Michael X.,Blake, Steven,Mayer, Michael,Yang, Jerry
, p. 1766 - 1767 (2010)
(Figure Presented) Nanoscale ionic diodes have attracted interest as circuit elements for development of nanofluidic devices for a variety of applications, including biosensing, constructing artificial cells, and engineering biological batteries. This paper presents a bottom-up, self-assembly approach for constructing nanopores with rectified conductance behavior in a membrane using semisynthetic derivatives of the ion-channel-forming peptide gramicidin A. The capability to individually access each half of a dimeric gramicidin channel makes it possible to generate asymmetric channels in a membrane that exhibit diodelike conductance properties. The modular nature of these self-assembled channels affords the possibility of tuning their rectifying conductance properties by simple replacement of one peptide derivative with another in the membrane. Additionally, introduction of an external stimulus (here, an enzyme) to change the functional group attached to one side of the gramicidin pore induces diodelike conductance behavior in previously nonrectified channels, demonstrating the possibility of switching the conductance properties of these nanopores in situ in a controlled manner. Copyright
PRODRUG MODULATORS OF THE INTEGRATED STRESS PATHWAY
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Paragraph 00272, (2020/05/19)
Provided herein are compounds, compositions, and methods useful for modulating the integrated stress response (ISR) and for treating related diseases, disorders and conditions.
ANTIMICROBIAL OXAZOLIDINONE PRODRUGS
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, (2010/11/29)
This invention includes oxazolidinone prodrug compounds of Formula (I) and Formula (II) as defined herein. The prodrugs are convertible by natural biological processes into an active ingredient possessed of antimicrobial properties useful in treating bact
Renin inhibitory peptides. Incorporation of polar, hydrophilic end groups into an active renin inhibitory peptide template and their evaluation in a human renin infused rat model and in conscious sodium-depleted monkeys
Thaisrivongs,Pals,DuCharme,Turner,DeGraaf,Lawson,Couch,Williams
, p. 633 - 642 (2007/10/02)
We previously reported that Boc-Pro-Phe-N-MeHis-Leuψ[CHOHCH2]-Ile-Amp (1) is a potent and specific inhibitor of human renin in vitro. It was shown to resist degradation by selected proteases and a rat liver homogenate. It was shown to inhibit p
