The influence of pH and ionic strength on the interactions between human serum albumin and magnetic iron oxide nanoparticles

Nanoparticle protein corona: from structure and function to therapeutic targeting

“…Recently, the stability of HSA-coated magnetic iron oxide nanoparticles (MNPs) was evaluated in phosphate buffer at pH 6.0, 6.6, and 7.5, and ionic strengths of 0.15 and 0.30 M NaCl. 89 At pH 6 and 0.05 M phosphate buffer, HSA coating on MNPs had the highest stability and the least exchangeability. However, increasing the ionic strength, as well as pH, decreased the stability of adsorbed HSA.…”

“…Due to the widespread use of human serum in biomedical applications, determining the effect of pH on HSA and BSA structural changes on the surface of NPs is critical. 89 Although BSA is not found in the human body, it is widely used in basic research studies to understand the fundamentals of the PC rather than translating it into clinical studies. The reason for this is that, when compared to HSA, BSA is less expensive, easier to obtain, and has similar physiochemical properties.…”

An overview on the exploring the interaction of inorganic nanoparticles with microtubules for the advancement of cancer therapeutics

“…For example, it has been shown that the smaller sized AgNPs have a stronger interaction with BSA relative to that of larger-sized NPs [110], and the rod-like AuNPs induce more structural changes in albumin in comparison with spherical-shaped counterparts due to higher surface energy [111]. In another study, it was shown that the interaction of albumin with magnetic NPs (MNPs) reduced as the pH of the medium increased from 6 to 7.5 due to possible variation in the charge distribution of the system [112]. Zaheer and co-workers also indicated that the binding affinity of NPs with proteins is lower than that of ions due to the different coordination affinities of NPs with their ionic counterparts [113].…”

Interactions of Common Biological Buffers with Iron Oxide Nanoparticles

“…The preparation and application of IONPs for biomedical applications is, therefore, generally carried out under controlled pH conditions in biological buffers, whose effective pH ranges cover the most likely physiological conditions (pH 6−8). 12 Buffers are used to regulate the pH of IONP suspensions for various purposes, such as surface charge stabilization, which can impact protein immobilization; 13,14 coupling chemistries, such as carbodiimide coupling, which requires different pH conditions for the carboxylate activation and amine coupling steps; 15 and catalysis, where proton transfers may be crucial to the catalytic process. 16 The surfaces of IONPs have been demonstrated to display a rich chemistry for the binding of organic ligands.…”