Preparation of a selective flocculant for treatment of oily wastewater produced from polymer flooding and its flocculant mechanism

There are residual polymers in the oily wastewater produced from polymer flooding (OWPF); keeping the residual polymer in the water during the flocculation is meaningful and challenging. In this paper, a selective flocculant (denoted as PDC10) which can remove the oil while keeping partially hydrolyzed polyacrylamide (HPAM) in water was prepared by copolymerization of decyl two methyl vinylbenzyl ammonium chloride (C10MVBA) and dimethyl aminopropyl methacryamide (DMAPMA). By using oil removal and HPAM retention as evaluation indexes, the synthesis condition of PDC10 was optimized. The optimum PDC10 exhibited oil removal of 98.0% and HPAM retention of 80.5%. Its HPAM retention is much higher than that of a regular cationic flocculant. Measurements of zeta potential, interfacial tension, interfacial dilational modulus and a dual polarization interferometry (DPI) test were carried out for investigating the flocculation mechanism of PDC10. The mechanism of PDC10 was that it can bridge and flocculate oil droplets by electrostatic interaction and hydrophobic interaction. It also preferred to distribute at the interface, and its interaction with HPAM in bulk water was weak, which confirms its selective flocculation properties.

Modern Biophysical Approaches to Study Protein–Ligand Interactions

Protein–ligand interactions act as a pivot to the understanding of most of the biological interactions. The study of interactions between proteins and cellular molecules has led to the establishment and identification of various important pathways that control biological systems. Investigators working in different fields of biological sciences have an intrinsic interest in this field and complement their findings by the application of different biophysical approaches and tools to quantify protein–ligand interactions that include protein–small molecules, protein–DNA, protein–RNA, protein–protein both in vitro and in vivo. In this paper, the various biophysical techniques that can be employed to study such interactions will be discussed. In addition to native gel electrophoresis and fluorescence-based methods, more details will be discussed, on the broad range of modern day biophysical tools such as Circular Dichroism, Fourier Transform Infrared (FTIR) Spectroscopy, Isothermal Titration Calorimetry, Analytical Ultracentrifugation, Surface Plasmon Resonance, Fluorescence Correlation Spectroscopy, Differential Scanning Fluorimetry, Nuclear Magnetic Resonance, Mass Spectroscopy, Single Molecule Spectroscopy, Dual Polarization Interferometry, Micro Scale Thermophoresis and Electro–switchable Biosensors that can be used to study the different aspects of protein–ligand interactions.

The influence of truncating the carboxy-terminal amino acid residues of Streptococcal enolase on its ability to interact with canine plasminogen

The native octameric structure of streptococcal enolase from Streptococcus pyogenes increasingly dissociates as amino acid residues are removed one by one from the carboxy-terminus. These truncations gradually convert native octameric enolase into monomers and oligomers. In this work, we investigated how these truncations influence the interaction between Streptococcal enolase and canine plasminogen. We used dual polarization interferometry (DPI), localized surface plasmon resonance (LSPR), and sedimentation velocity analytical ultracentrifugation (AUC) to study the interaction. The DPI was our first technique, was performed on all the truncations and used one exclusive kind of chip. The LSRP was used to show that the DPI results were not dependent on the type of chip used. The AUC was required to show that our surface results were not the result of selecting a minority population in any given sample; the majority of the protein was responsible for the binding phenomenon we observed. By comparing results from these techniques we identified one detail that is essential for streptococcal enolase to bind plasminogen: In our hands the individual monomers bind plasminogen; dimers, trimers, tetramers may or may not bind, the fully intact, native, octamer does not bind plasminogen. We also evaluated the contribution to the equilibrium constant made by surface binding as well as in solution. On a surface, the association coefficient is about twice that in solution. The difference is probably not significant. Finally, the fully octameric form of the protein that does not contain a hexahis N-terminal peptide does not bind to a silicon oxynitride surface, does not bind to a Au-nanoparticle surface, does not bind to a surface coated with Ni-NTA nor does it bind to a surface coated with DPgn. The likelihood is great that the enolase species on the surface of Streptococcus pyogenes is an x-mer of the native octamer.