Theoretical study and analysis of o-nitrophenol adsorption using layered double hydroxides containing Ca-Al, Ni-Al and Zn-Al.

A theoretical assessment of the o-nitrophenol adsorption on layered double hydroxides containing different metallic species (Ca-Al, Ni-Al and Zn-Al) was performed. Experimental o-nitrophenol adsorption isotherms obtained at different adsorption temperatures with these layered double hydroxides were analyzed using a statistical physics monolayer model. Model calculations showed that the o-nitrophenol aggregation could occur with a high degree. It was estimated that the o-nitrophenol adsorption implied a non-flat orientation on all adsorbent surfaces and this process was multi-molecular. It was also demonstrated that there was no significant difference on the o-nitrophenol adsorption capacities of tested adsorbents, which varied from 77 to 135, 95 to 122 and 74 and 130 mg/g for Ca-Al, Ni-Al and Zn-Al layered double hydroxides, respectively. This finding suggested that the incorporation of Ca-Al, Ni-Al and Zn-Al in the layered double hydroxide structure played a similar role to adsorb o-nitrophenol molecules from aqueous solution. Calculated adsorption energies and thermodynamic functions confirmed an exothermic adsorption with the presence of physical-based interaction forces. This paper highlights the importance of reliable theoretical calculations based on statistical physics theory to contribute in the understanding of the adsorption mechanisms of a relevant water pollutant using layered double hydroxides as promising adsorbents for industrial applications.

Theoretical interpretation of the adsorption of amoxicillin on activated carbon via physical model.

The paper describes a theoretical analysis of the adsorption of amoxicillin (AMX) onto two activated carbons pyrolysed at either 600 or 700 °C (PAC-600 and PAC-700). Series of experimental data are carried out at different temperatures ranging from 10 to 45 °C, as this is the first key factor to explain the adsorption mechanism of this pollutant. AMX adsorption capacity varied from 275 to 450 mg/g and between 276 and 454 mg/g for PAC-600 and PAC-700, respectively. It can be deduced that the pyrolysis temperature does not play a crucial role in AMX removal capacity of the adsorbents. A comparison with literature data shows that the retrieved adsorption capacities of both the adsorbents are very competitive for an effective water treatment. Physical models are applied to the two experimental data sets showing that a monolayer model with single energy is the best option to explain the AMX adsorption mechanism on both PAC-600 and PAC-700 adsorbents. The interpretation of the theoretical results points out that the AMX was not aggregated during the adsorption process. Under these experimental working conditions, it is noted that AMX is adsorbed almost via a parallel orientation on PAC-600 and PAC-700 adsorbents, reflecting that the adsorption is a multi-interaction mechanism. The model provides an estimation of the adsorption energy that allows the quantification of the interactions between the AMX and both PAC-600 and PAC-700 adsorbent surfaces; in both the cases, physical bindings are involved in AMX adsorption.

A "Drug Sweeping" State of the TriABC Triclosan Efflux Pump from Pseudomonas aeruginosa.

The structure of the TriABC inner membrane component of the triclosan/SDS-specific efflux pump from Pseudomonas aeruginosa was determined by cryoelectron microscopy to 4.5 Å resolution. The complete structure of the inner membrane transporter TriC of the resistance-nodulation-division (RND) superfamily was solved, including a partial structure of the fused periplasmic membrane fusion subunits, TriA and TriB. The substrate-free conformation of TriABC represents an intermediate step in efflux complex assembly before the engagement of the outer membrane channel. Structural analysis identified a tunnel network whose constriction impedes substrate efflux, indicating inhibition of TriABC in the unengaged state. Blind docking studies revealed binding to TriC at the same loci by substrates and bulkier non-substrates. Together with functional analyses, we propose that selective substrate translocation involves conformational gating at the tunnel narrowing that, together with conformational ordering of TriA and TriB, creates an engaged state capable of mediating substrate efflux.

Ternary adsorption of cobalt, nickel and methylene blue on a modified chitin: Phenomenological modeling and physical interpretation of the adsorption mechanism.

The simultaneous adsorption of three pollutants cobalt (Co), methylene blue (MB) and nickel (Ni) on a modified chitin surface from ternary systems was investigated. Multicomponent experimental adsorption data were determined at 298-328 K and pH 6. These experimental studies indicated that Ni adsorption was higher than those obtained for Co and MB. The multicomponent adsorption mechanism of this ternary system was analyzed with statistical physics theory where a set of new models with different hypotheses was developed and tested. Results showed that an adsorption model assuming that the pollutants Co, MB and Ni were adsorbed on three different types of modified chitin receptor sites was the most appropriate. This model was also utilized to calculate the corresponding adsorption energies to describe the possible interactions between these adsorbates and the surface of modified chitin. A general analysis of trends and magnitude of the model parameters provided a deeper understanding of the ternary adsorption mechanism at molecular level. Macroscopically, the ternary adsorption mechanism was interpreted via a calculation of three thermodynamic functions.

MmpL3 as a Target for the Treatment of Drug-Resistant Nontuberculous Mycobacterial Infections.

Nontuberculous mycobacterial (NTM) pulmonary infections are emerging as a global health problem and pose a threat to susceptible individuals with structural or functional lung conditions such as cystic fibrosis, chronic obstructive pulmonary disease and bronchiectasis. Mycobacterium avium complex (MAC) and Mycobacterium abscessus complex (MABSC) species account for 70-95% of the pulmonary NTM infections worldwide. Treatment options for these pathogens are limited, involve lengthy multidrug regimens of 12-18 months with parenteral and oral drugs, and their outcome is often suboptimal. Development of new drugs and improved regimens to treat NTM infections are thus greatly needed. In the last 2 years, the screening of compound libraries against M. abscessus in culture has led to the discovery of a number of different chemotypes that target MmpL3, an essential inner membrane transporter involved in the export of the building blocks of the outer membrane of all mycobacteria known as the mycolic acids. This perspective reflects on the therapeutic potential of MmpL3 in Mycobacterium tuberculosis and NTM and the possible reasons underlying the outstanding promiscuity of this target. It further analyzes the physiological and structural factors that may account for the apparent looser structure-activity relationship of some of these compound series against M. tuberculosis compared to NTM.

Structure-Function Profile of MmpL3, the Essential Mycolic Acid Transporter from Mycobacterium tuberculosis.

The MmpL family of proteins translocates complex (glyco)lipids and siderophores across the cell envelope of mycobacteria and closely related Corynebacteriaceae and plays important roles in the biogenesis of the outer membrane of these organisms. Despite their significance in the physiology and virulence of Mycobacterium tuberculosis, and from the perspective of developing novel antituberculosis agents, little is known about their structure and mechanism of translocation. In this study, the essential mycobacterial mycolic acid transporter, MmpL3, and its orthologue in Corynebacterium glutamicum, CmpL1, were investigated as prototypical MmpL proteins to gain insight into the transmembrane topology, tertiary and quaternary structures, and functional regions of this transporter family. The combined genetic, biochemical, and biophysical studies indicate that MmpL3 and CmpL1 are structurally similar to Gram-negative resistance-nodulation and division efflux pumps. They harbor 12 transmembrane segments interrupted by two large soluble periplasmic domains and function as homotrimers to export long-chain (C22-C90) mycolic acids, possibly in their acetylated form, esterified to trehalose. The mapping of a number of functional residues within the middle region of the transmembrane domain of MmpL3 shows a striking overlap with mutations associated with resistance to MmpL3 inhibitors. The results suggest that structurally diverse inhibitors of MmpL3 all target the proton translocation path of the transporter and that multiresistance to these inhibitors is enabled by conformational changes in MmpL3.