4.8 Article

Role of Protein in Fungal Biomineralization of Copper Carbonate Nanoparticles

Journal

CURRENT BIOLOGY
Volume 31, Issue 2, Pages 358-+

Publisher

CELL PRESS
DOI: 10.1016/j.cub.2020.10.044

Keywords

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Funding

  1. China Scholarship Council (CSC) through a CSC-School of Life Sciences PhD scholarship [201609110150]
  2. Natural Environment Research Council [NE/M010910/1, NE/M011275/1]
  3. NERC [NE/M010910/1, NE/M011275/1] Funding Source: UKRI

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Biomineralization processes play a crucial role in the biogeochemical cycling of metals by microorganisms, with potential applications in nanoparticle synthesis. This study elucidated the association of fungal proteins in the formation of biogenic copper carbonate nanoparticles, particularly identifying triosephosphate isomerase (TPI) as a key protein involved in shaping nanomaterial morphology. The research also highlighted the unfolding of proteins and increased beta sheets within protein structures during biomineralization, providing insights into the mechanisms involved in the formation of complex protein/inorganic systems for nanomaterial synthesis.
Biomineralization processes are of key importance in the biogeochemical cycling of metals and other elements by microorganisms, and several studies have highlighted the potential applications of nanoparticle synthesis via biomineralization. The roles played by proteins in the transformation and biologically induced biomineralization of metals by microorganisms is not well understood, despite the interactions of protein and nanoparticles at mineral interfaces attracting much interest in various emerging fields for novel biomaterial synthesis. Here, we have elucidated the association and involvement of fungal proteins in the formation of biogenic copper carbonate nanoparticles (CuNPs) using a carbonate-enriched biomass-free ureolytic fungal culture supernatant. Proteomic analysis was conducted that identified the major proteins present in the culture supernatant. Of the proteins identified, triosephosphate isomerase (TPI) exhibited a strong affinity to the CuNPs, and the impact of purified TPI on CuNP formation was studied in detail. The combined use of scanning electron microscopy (SEM) and confocal laser scanning microscopy (CLSM) confirmed that TPI played an important role in controlling the morphology and structure of the nanomaterials. Fourier transform infrared spectroscopy (FTIR) was applied to examine conformational changes of the proteins to further clarity the interaction mechanisms with CuNPs during biomineralization. Such analyses revealed unfolding of proteins on the mineral surface and an increase in beta sheets within the protein structure. These results extend understanding of how microbial systems can influence biomineral formation through protein secretion, the mechanisms involved in formation of complex protein/inorganic systems, and provide useful guidelines for the synthesis of inorganic-protein based nanomaterials.

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