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Investigation of the influence of lead compounds with particles of different dispersity on human blood plasma proteins as an express method for evaluation of their safety

ISSN 2223-6775 Ukrainian journal of occupational health Vol.16, No 3, 2020

Investigation of the influence of lead compounds with particles of different dispersity on human blood plasma proteins as an express method for evaluation of their safety

Dmytrukha N. M., Lahutina O. S., Gromovoy T. Yu.

1State Institution «Kundiiev Institute of Occupational Health of the National Academy of Medical Sciences of Ukraine», Kyiv

2Chuiko Institute of Surface Chemistry of the National Academy of Sciences of Ukraine, Kyiv


Full article (PDF), UKR

Introduction. The production of lead and its use in various industries cause its entering the human body in the form of an aerosol with particles of different dispersion, including nanosized. Specific physicochemical properties of nanoparticles (NPs), the ability of lead to bioaccumulation and the polytropic toxicity necessitate studying its toxicity and hazard in the nanoscale state.

The purpose of the study investigate the effect of lead compounds with different particle sizes on human plasma proteins (NPs with the size of 30 nm and 65 nm, human blood plasma (OA, R +), albumin and human immunoglobulin G (IgG) (Sigma. The effect of lead compounds on protein structure was determined using an Autoflex II mass spectrometer (Bruker, Germany) and a Mefan spectrophotometer (Ukraine).

Results. The obtained mass spectra of human plasma proteins after incubation with lead nitrate and PbS NPs differed by the availability and intensity of peaks, which is a consequence of different types of interaction of ions and NPs with proteins. Also, the indices of optical density of the studied protein solutions indicate different types of interaction of lead with proteins in the form of ions and NPs. It is shown that the degree of conformation changes of albumin and IgG depends on both the chemical form of lead compounds and the size of nanoparticles, as well as on their concentration in the incubation medium. The largest changes in the protein structure were caused by PbS with NPs of 26-34 nm, and the smallest by lead nitrate (ionic form). Human IgG was more sensitive to lead compounds than albumin.

Conclusions. The established selective interaction of PbS ions and NPs with blood proteins can lead to changes in the structure of proteins, in their functional activity as well as in properties and behavior of nanoparticles, as it can affect their size, transport, accumulation and elimination.

A model "nanoparticles blood plasma proteins" can be used for express assessment of the biocompatibility of metal NPs and their toxicity.

Key words: lead ions and nanoparticles, human blood plasma, albumin, immunoglobulin G, denaturation, toxicity.



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