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Synergistic effects of metal-induced aggregation of human serum albumin
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Surface and Corrosion Science.ORCID iD: 0000-0003-2145-3650
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Surface and Corrosion Science.
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Applied Physical Chemistry.
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Surface and Corrosion Science.ORCID iD: 0000-0002-6042-9752
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2019 (English)In: Colloids and Surfaces B: Biointerfaces, ISSN 0927-7765, E-ISSN 1873-4367, Vol. 173, p. 751-758Article in journal (Refereed) Published
Abstract [en]

Exposure to cobalt (Co), chromium (Cr), and nickel (Ni) occurs often via skin contact and from different dental and orthopedic implants. The metal ions bind to proteins, which may induce structural changes and aggregation, with different medical consequences. We investigated human serum albumin (HSA) aggregation in the presence of Co-II, Cr-III, and/or Ni-II ions and/or their nanoparticle precipitates by using scattering, spectroscopic, and imaging techniques, at simulated physiological conditions (phosphate buffered saline - PBS, pH 7.3) using metal salts that did not affect the pH, and at HSA:metal molar ratios of up to 1:8. Co ions formed some solid nano particles in PBS at the investigated conditions, as determined by nanoparticle tracking analysis, but the Cr-III anions and Ni-II ions remained fully soluble. It was found that all metal ions induced HSA aggregation, and this effect was significantly enhanced when a mixture of all three metal ions was present instead of any single type of ion. Thus, the metal ions induce aggregation synergistically. HSA aggregates formed linear structures on a mica surface in the presence of Cr-III ions. A clear tendency of aggregation and linearly aligned aggregates was seen in the presence of all three metal ions. Spectroscopic investigations indicated that the majority of the HSA molecules maintained their alpha helical secondary structure and conformation. This study highlights the importance of synergistic effects of metal ions and/or their precipitates on protein aggregation, which are highly relevant for implant materials and common exposures to metals.

Place, publisher, year, edition, pages
ELSEVIER SCIENCE BV , 2019. Vol. 173, p. 751-758
Keywords [en]
Cobalt, Chromium, Nickel, Binding, Albumin, Aggregation
National Category
Physical Chemistry
Identifiers
URN: urn:nbn:se:kth:diva-241193DOI: 10.1016/j.colsurfb.2018.10.061ISI: 000454377300089PubMedID: 30384272Scopus ID: 2-s2.0-85055579350OAI: oai:DiVA.org:kth-241193DiVA, id: diva2:1280901
Note

QC 20190121

Available from: 2019-01-21 Created: 2019-01-21 Last updated: 2019-01-21Bibliographically approved

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Hedberg, YolandaDobryden, IlliaChaudhary, HimanshuWei, ZhengClaesson, Per M.Lendel, Christofer

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Hedberg, YolandaDobryden, IlliaChaudhary, HimanshuWei, ZhengClaesson, Per M.Lendel, Christofer
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