Scavenging of copper(II) ions, phosphate(V) ions, and diuron from aqueous media by goethite modified with chitosan or poly(acrylic acid).

Goethite was modified by chitosan (CS) or poly(acrylic acid) (PAA) to improve its adsorptive abilities toward components of agrochemicals, i.e., copper ions (Cu), phosphate ions (P), and diuron. The pristine goethite effectively bound Cu (7.68 mg/g, 63.71%) and P (6.31 mg/g, 50.46%) only in their mixed systems. In the one adsorbate solutions, the adsorption levels accounted for 3.82 mg/g (30.57%) for Cu, 3.22 mg/g (25.74%) for P, and 0.15 mg/g (12.15%) for diuron. Goethite modification with CS or PAA did not yield spectacular results in adsorption. The maximum increase in adsorbed amount was noted for Cu ions (8.28%) after PAA modification as well as for P (6.02%) and diuron (24.04%) after CS modification. Both goethite modifications contributed to clear reduction in desorption of pollutants (even by 20.26% for Cu after PAA coating), which was mainly dictated by electrostatic attractive forces and hydrogen bonds formation occurring between macromolecules and impurities. The only exception in this phenomenon was Cu desorption from CS-modified solid-the polymer made it higher (to 95.00%). The Cu adsorption on PAA-modified goethite enhanced solid aggregation and thus facilitated metal cation separation from aqueous media. Consequently, the goethite modification with PAA was considered more promising for environmental remediation.

Antifungal Activity of Anionic Defense Peptides: Insight into the Action of Galleria mellonella Anionic Peptide 2.

Anionic antimicrobial peptides constitute an integral component of animal innate immunity, however the mechanisms of their antifungal activity are still poorly understood. The action of a unique Galleria mellonella anionic peptide 2 (AP2) against fungal pathogen Candida albicans was examined using different microscopic techniques and Fourier transform infrared (FTIR) spectroscopy. Although the exposure to AP2 decreased the survival rate of C. albicans cells, the viability of protoplasts was not affected, suggesting an important role of the fungal cell wall in the peptide action. Atomic force microscopy showed that the AP2-treated cells became decorated with numerous small clods and exhibited increased adhesion forces. Intensified lomasome formation, vacuolization, and partial distortion of the cell wall was also observed. FTIR spectroscopy suggested AP2 interactions with the cell surface proteins, leading to destabilization of protein secondary structures. Regardless of the anionic character of the whole AP2 molecule, bioinformatics analyses revealed the presence of amphipathic α-helices with exposed positively charged lysine residues. High content of the α-helical structure was confirmed after deconvolution of the IR absorption spectrum and during circular dichroism measurements. Our results indicated that the antimicrobial properties of G. mellonella AP2 rely on the same general characteristics found in cationic defense peptides.