BSA Adsorption and Antibiofilm Properties of (N-Cyclohexylacrylamide-co-Acrylamide/AMPSNa) Hydrogels

The hydrogels poly (N-cyclohexylacrylamide-co-acrylamide/2-acrylamido-2-methyl-1-propanesodiumsulfonate) i.e.poly(NCA-co-AM/AMPSNa) (HG41,HG42,HG43&HG44) were synthesised via free-radical copolymerization of NCA and (AM) in a fixed proportion (50:50), but varying the ionic monomer-AMPSNa (0.1g,0.3g,0.5 d 0.7g) in a medium of mixture of water and methanol at 60°C in an oil bath, Potassium persulfate (KPS) was used as an initiator, while N,N'-methylene-bisacrylamide (MBA) was used as a cross-linker. FT-IR spectral data, SEM, XRD, and TGA techniques were used to characterise the synthesised hydrogel (HG43). On changing pH(3.0, 5.0, 7.0 & 9.0), the amount of Bovine Serum Albumin (BSA) adsorption efficiency by these hydrogels was evaluated. At pH 5.0, which is near to BSA's isoelectric point (4.7)., the maximum adsorption was found. BSA adsorption increased as the amount of AMPSNa increased. SEM and XRD were used to examine the BSA-adsorbed hydrogel (HG43). The antibiofilm abilities of the hydrogel (HG43) by Microtiter plate Assay(MTP), Fluorescence microscopy and SEMl against Staphylococcus aureus and Pseudomonas aureginosa displayed outstanding efficacy.

Influence of bovine serum albumin on corrosion behaviour of pure Zn in phosphate buffered saline

Zinc (Zn) and its alloys have received increasing attention as new alternative biodegradable metals. However, consensus has not been reached on the corrosion behaviour of Zn. As cardiovascular artery stent material, Zn is supposed to contact with plasma that contains inorganic salts and organic components. Protein is one of the most important constitute in the plasma and could adsorb on the material surface. In this paper, bovine serum albumin (BSA) was used as a typical protein. Influences of BSA on pure Zn corrosion in phosphate buffered saline is investigated as a function of BSA concentrations and immersion durations by electrochemical techniques and surface analysis. Results showed that pure Zn corrosion was progressively accelerated with BSA concentrations (ranging from 0.05 to 5 g L−1) at 0.5 h. With time evolves, formation of phosphates as corrosion product was delayed by BSA adsorption, especially at concentration of 2 g L−1. Within 48 h, the corrosion of pure Zn was alleviated by BSA at concentration of 0.1 g L−1, whereas the corrosion was enhanced after 168 h. Addition of 2 g L−1 BSA has opposite influence on the pure Zn corrosion. Furthermore, schematic corrosion behaviour at protein/Zn interfaces was proposed. This work encourages us to think more about the influence of protein on the material corrosion and helps us to better understand the corrosion behaviour of pure Zn.

Polysaccharides-Based Complex Particles’ Protective Role on the Stability and Bioactivity of Immobilized Curcumin

The curcumin degradation represents a significant limitation for its applications. The stability of free curcumin (FC) and immobilized curcumin in complex particles (ComPs) based on different polysaccharides was studied under the action of several factors. Ultraviolet-visible (UV-VIS) and Fourier-transform infrared (FTIR) spectroscopy proved the FC photodegradation and its role as a metal chelator: 82% of FC and between 26% and 39.79% of curcumin within the ComPs degraded after exposure for 28 days to natural light. The degradation half-life (t1/2) decreases for FC when the pH increases, from 6.8 h at pH = 3 to 2.1 h at pH = 9. For curcumin extracted from ComPs, t1/2 was constant (between 10 and 13 h) and depended on the sample’s composition. The total phenol (TPC) and total flavonoids (TFC) content values increased by 16% and 13%, respectively, for FC exposed to ultraviolet light at λ = 365 nm (UVA), whereas no significant change was observed for immobilized curcumin. Antioxidant activity expressed by IC50 (µmoles/mL) for FC exposed to UVA decreased by 29%, but curcumin within ComPs was not affected by the UVA. The bovine serum albumin (BSA) adsorption efficiency on the ComPs surface depends on the pH value and the cross-linking degree. ComPs have a protective role for the immobilized curcumin.