A comprehensive review on current technologies for removal of endocrine disrupting chemicals from wastewaters.

In the recent years, endocrine disrupting compounds (EDCs) has received increasing attention due to their significant toxic effects on human beings and wildlife by affecting their endocrine systems. As an important group of emerging pollutant, EDCs have been detected in various aquatic environments, including surface waters, groundwater, wastewater, runoff, and landfill leachates. Their removal from water resources has also been an emerging concern considering growing population as well as reducing access to fresh water resources. EDC removal from wastewaters is highly dependent on physicochemical properties of the given EDCs present in each wastewater types as well as various aquatic environments. Due to chemical, physical and physicochemical diversities in these parameters, variety of technologies consisting of physical, biological, electrochemical, and chemical processes have been developed for their removal. This review highlights that the effectiveness of EDC removal is highly dependent of selecting the appropriate technology; which decision is made upon a full wastewater chemical characterization. This review aims to provide a comprehensive perspective about all the current technologies used for EDCs removal from various aquatic matrices along with rising challenges such as the antimicrobial resistance gene transfer during EDC treatment.

Major Ampullate Spider Silk with Indistinguishable Spidroin Dope Conformations Leads to Different Fiber Molecular Structures.

To plentifully benefit from its properties (mechanical, optical, biological) and its potential to manufacture green materials, the structure of spider silk has to be known accurately. To this aim, the major ampullate (MA) silk of Araneus diadematus (AD) and Nephila clavipes (NC) has been compared quantitatively in the liquid and fiber states using Raman spectromicroscopy. The data show that the spidroin conformations of the two dopes are indistinguishable despite their specific amino acid composition. This result suggests that GlyGlyX and GlyProGlyXX amino acid motifs (X = Leu, Glu, Tyr, Ser, etc.) are conformationally equivalent due to the chain flexibility in the aqueous environment. Species-related sequence specificity is expressed more extensively in the fiber: the ß-sheet content is lower and width of the orientation distribution of the carbonyl groups is broader for AD (29% and 58°, respectively) as compared to NC (37% and 51°, respectively). ß-Sheet content values are close to the proportion of polyalanine segments, suggesting that ß-sheet formation is mainly dictated by the spidroin sequence. The extent of molecular alignment seems to be related to the presence of proline (Pro) that may decrease conformational flexibility and inhibit chain extension and alignment upon drawing. It appears that besides the presence of Pro, secondary structure and molecular orientation contribute to the different mechanical properties of MA threads.

Mimicking and Understanding the Agglutination Effect of the Antimicrobial Peptide Thanatin Using Model Phospholipid Vesicles.

Thanatin is a cationic 21-residue antimicrobial and antifongical peptide found in the spined soldier bug Podisus maculiventris. It is believed that it does not permeabilize membranes but rather induces the agglutination of bacteria and inhibits cellular respiration. To clarify its mode of action, lipid vesicle organization and aggregation propensity as well as peptide secondary structure have been studied using different membrane models. Dynamic light scattering and turbidimetry results show that specific mixtures of negatively charged and zwitterionic phospholipid vesicles are able to mimic the agglutination effect of thanatin observed on Gram-negative and Gram-positive bacterial cells, while monoconstituent ("conventional") models cannot reproduce this phenomenon. The model of eukaryotic cell reveals no particular interaction with thanatin, which is consistent with the literature. Infrared spectroscopy shows that under the conditions under which vesicle agglutination occurs, thanatin exhibits a particular spectral pattern in the amide I' region and in the region associated with Arg side chains. The data suggest that thanatin mainly retains its hairpin structure, Arg residues being involved in strong interactions with anionic groups of phospholipids. In the absence of vesicle agglutination, the peptide conformation and Arg side-chain environment are similar to those observed in solution. The data show that a negatively charged membrane is required for thanatin to be active, but this condition is insufficient. The activity of thanatin seems to be modulated by the charge surface density of membranes and thanatin concentration.