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Proteins enriched in charged amino acids control the formation and stabilization of selenium nanoparticles in Comamonas testosteroni S44
- Source :
- Scientific Reports, Scientific Reports, Vol 8, Iss 1, Pp 1-11 (2018)
- Publication Year :
- 2018
- Publisher :
- Springer Science and Business Media LLC, 2018.
-
Abstract
- Elemental selenium nanoparticles (SeNPs) are useful in medicine, environmental remediation and in material science. Biosynthesized SeNPs (BioSeNPs) by bacteria are cheap, eco-friendly and have a lower cytotoxicity in comparison with chemically synthesized ones. Organic matters were found to cap on the surface of BioSeNPs, but the functions were still not entirely clear. The purified BioSeNPs were coated in a thick layer of organic substrates observed by transmission electron microscopy (TEM). Fourier Transform Infrared (FT-IR) and quantitative detection of the coating agents showed that one gram of purified BioSeNPs bound 1069 mg proteins, 23 mg carbohydrates and only very limited amounts of lipids. Proteomics of BioSeNPs showed more than 800 proteins bound to BioSeNPs. Proteins enriched in charged amino acids are the major factor thought to govern the formation process and stabilization of BioSeNPs in bacteria. In view of the results reported here, a schematic model for the molecular mechanism of BioSeNPs formation in bacteria is proposed. These findings are helpful for the artificial green synthesis of stable SeNPs under specific condition and guiding the surface modification of SeNPs for medicine application.
- Subjects :
- Proteomics
0301 basic medicine
lcsh:Medicine
chemistry.chemical_element
Nanoparticle
010501 environmental sciences
01 natural sciences
Article
Selenium
03 medical and health sciences
Drug Stability
Comamonas testosteroni
Amino Acids
lcsh:Science
Cytotoxicity
0105 earth and related environmental sciences
chemistry.chemical_classification
Multidisciplinary
biology
lcsh:R
Proteins
biology.organism_classification
Combinatorial chemistry
Amino acid
030104 developmental biology
chemistry
Molecular mechanism
Nanoparticles
Surface modification
lcsh:Q
Bacteria
Subjects
Details
- ISSN :
- 20452322
- Volume :
- 8
- Database :
- OpenAIRE
- Journal :
- Scientific Reports
- Accession number :
- edsair.doi.dedup.....90c3b7e3e2f62a53a2319d9dfa35fa71