Laying Bare: Agamben, Chandler, and The Responsibility to Protect

This paper demonstrates the hidden similarities between Raymond Chandler’s prototypical noir The Big Sleep, and the United Nations Responsibility to Protect (R2P) document. By taking up the work of philosopher Giorgio Agamben, this paper shows that the bare life produces the form of protection embodied by Philip Marlowe in Chandler’s novel and by the United Nations Security Council in R2P. Agamben’s theorizing of the extra-legal status of the sovereign pertains to both texts, in which the protector exists outside of the law. Philip Marlowe, tasked with preventing the distribution of pornographic images, commits breaking-and-entering, withholding evidence, and murder. Analogously, R2P advocates for the Security Council’s ability to trespass laws that safeguard national sovereignty in order to prevent “bare” atrocities against human life. As Agamben demonstrates, the extra-legal position of the protector is made possible by “stripping bare” human life. This paper also gestures towards limitations of Agamben’s thought by indicating, through a comparison of these two texts, that bare life produces states of exception as the object of protection rather than punishment

Quantification of cytotoxicity in weight concentration (mg/mL).

<p>(a) Histogram, (b) dot plot, (c) box plot, and (d) normal Q-Q plot of cytotoxicity data set expressed in mg/mL. While the histogram, dot plot and box plot imply a narrow distribution of cytotoxicity in mg/mL, Q-Q plot also shows considerable deviation from normal distribution.</p

Plasmonic Thermal Decomposition/Digestion of Proteins: A Rapid On-Surface Protein Digestion Technique for Mass Spectrometry Imaging

A method based on plasmon surface resonance absorption and heating was developed to perform a rapid on-surface protein thermal decomposition and digestion suitable for imaging mass spectrometry (MS) and/or profiling. This photothermal process or plasmonic thermal decomposition/digestion (plasmonic-TDD) method incorporates a continuous wave (CW) laser excitation and gold nanoparticles (Au-NPs) to induce known thermal decomposition reactions that cleave peptides and proteins specifically at the C-terminus of aspartic acid and at the N-terminus of cysteine. These thermal decomposition reactions are induced by heating a solid protein sample to temperatures between 200 and 270 °C for a short period of time (10–50 s per 200 μm segment) and are reagentless and solventless, and thus are devoid of sample product delocalization. In the plasmonic-TDD setup the sample is coated with Au-NPs and irradiated with 532 nm laser radiation to induce thermoplasmonic heating and bring about site-specific thermal decomposition on solid peptide/protein samples. In this manner the Au-NPs act as nanoheaters that result in a highly localized thermal decomposition and digestion of the protein sample that is independent of the absorption properties of the protein, making the method universally applicable to all types of proteinaceous samples (e.g., tissues or protein arrays). Several experimental variables were optimized to maximize product yield, and they include heating time, laser intensity, size of Au-NPs, and surface coverage of Au-NPs. Using optimized parameters, proof-of-principle experiments confirmed the ability of the plasmonic-TDD method to induce both C-cleavage and D-cleavage on several peptide standards and the protein lysozyme by detecting their thermal decomposition products with matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). The high spatial specificity of the plasmonic-TDD method was demonstrated by using a mask to digest designated sections of the sample surface with the heating laser and MALDI-MS imaging to map the resulting products. The solventless nature of the plasmonic-TDD method enabled the nonenzymatic on-surface digestion of proteins to proceed with undetectable delocalization of the resulting products from their precursor protein location. The advantages of this novel plasmonic-TDD method include short reaction times (<30 s/200 μm), compatibility with MALDI, universal sample compatibility, high spatial specificity, and localization of the digestion products. These advantages point to potential applications of this method for on-tissue protein digestion and MS-imaging/profiling for the identification of proteins, high-fidelity MS imaging of high molecular weight (>30 kDa) proteins, and the rapid analysis of formalin-fixed paraffin-embedded (FFPE) tissue samples

Statistic data of two data sets in mole concentration and mass concentration.

<p>Statistic data of two data sets in mole concentration and mass concentration.</p

Quantification of cytotoxicity in mole concentration (µM).

<p>(a) Histogram, (b) dot plot, (c) box plot and (d) normal Q-Q plot of cytotoxicity data set expressed in µM. While histogram shows how cytotoxicity data spread out in certain concentration range, dot plot gives the global dispersion picture in full concentration range, and box plot brings the mean value as reference. Q-Q plot demonstrates that cytotoxicity in µM as the sample set used in the test, deviates significantly from the normal distribution.</p

Illustration of the aggregates constrained in a fixed volume and are expressed in different units of concentration.

<p>(a) Mole concentration only represents the amounts of individual units in a certain volume. (b) Mass concentration is able to reflect the solid-like properties such as density, which indicates the interaction and accommodates inhomogeneous distribution of the aggregates.</p

Flow chart of study identification, inclusion, exclusion.

<p>Flow chart of study identification, inclusion, exclusion.</p

Down-regulation of D2R leads to the shift of synaptic plasticity from LTD to LTP in PD 30 EtOH rats.

<p>‘↑’ indicates the time point of HFS application. The hollow line represents the period of drug occurrence in ASCF. <b>A & B:</b> L-sulpiride completely blocked HFS induced LTD in control rats, but had no effect on HFS induced LTP in EtOH rats. <b>C:</b> the D2R agonist quinpirole recovered the induction of LTD in EtOH rats. <b>D & E:</b> SCH23390 completely blocked either the induction of LTD in control rats or quinpirole-recovered LTD in EtOH rats.</p

Facile synthesis of bisphosphine monoxides from Morita–Baylis–Hillman carbonates

<p>A facile two-step synthesis of bisphosphine monoxides (BPMOs, with both the phosphine and phosphine oxide moieties within one molecule) from readily available Morita–Baylis–Hillman (MBH) carbonates was realized. Under the catalysis of DABCO, the MBH carbonates undergo allylic phosphorylation reaction with diphenylphosphine oxide or diethyl phosphonate to give monophosphine oxides bearing an activated alkene moiety; subsequent base-catalyzed hydrophosphination of the prepared monophosphine oxide with HPPh₂ readily affords the BPMOs.</p

mGluR activation mediates the quinpirole-recovered LTD in EtOH rats.

<p>‘↑’ indicates the time point of HFS application. The hollow line represents the period of drug occurrence in ASCF. <b>A & B:</b> the LTD in control rats was sensitive to MPEP, but not AP5. <b>C & D:</b> The quinpirole-recovered LTD in EtOH rats was inhibited by MPEP, but not AP5.</p