Dataset Information

Investigation on the Adsorption-Interaction Mechanism of Pb(II) at Surface of Silk Fibroin Protein-Derived Hybrid Nanoflower Adsorbent.

ABSTRACT: For further the understanding of the adsorption mechanism of heavy metal ions on the surface of protein-inorganic hybrid nanoflowers, a novel protein-derived hybrid nanoflower was prepared to investigate the adsorption behavior and reveal the function of organic and inorganic parts on the surface of nanoflowers in the adsorption process in this study. Silk fibroin (SF)-derived and copper-based protein-inorganic hybrid nanoflowers of SF@Cu-NFs were prepared through self-assembly. The product was characterized and applied to adsorption of heavy metal ion of Pb(II). With Chinese peony flower-like morphology, the prepared SF@Cu-NFs showed ordered three-dimensional structure and exhibited excellent efficiency for Pb(II) removal. On one hand, the adsorption performance of SF@Cu-HNFs for Pb(II) removal was evaluated through systematical thermodynamic and adsorption kinetics investigation. The good fittings of Langmuir and pseudo-second-order models indicated the monolayer adsorption and high capacity of about 2000 mg g-1 of Pb(II) on SF@Cu-NFs. Meanwhile, the negative values of ? r G m ( T ) ? and ? r H m ? proved the spontaneous and exothermic process of Pb(II) adsorption. On the other hand, the adsorption mechanism of SF@Cu-HNFs for Pb(II) removal was revealed with respect to its individual organic and inorganic component. Organic SF protein was designated as responsible 'stamen' adsorption site for fast adsorption of Pb(II), which was originated from multiple coordinative interaction by numerous amide groups; inorganic Cu3(PO4)2 crystal was designated as responsible 'petal' adsorption site for slow adsorption of Pb(II), which was restricted from weak coordinative interaction by strong ion bond of Cu(II). With only about 10% weight content, SF protein was proven to play a key factor for SF@Cu-HNFs formation and have a significant effect on Pb(II) treatment. By fabricating SF@Cu-HNFs hybrid nanoflowers derived from SF protein, this work not only successfully provides insights on its adsorption performance and interaction mechanism for Pb(II) removal, but also provides a new idea for the preparation of adsorption materials for heavy metal ions in environmental sewage in the future.

SUBMITTER: Li X

PROVIDER: S-EPMC7085063 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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Investigation on the Adsorption-Interaction Mechanism of Pb(II) at Surface of Silk Fibroin Protein-Derived Hybrid Nanoflower Adsorbent.

Li Xiang X Xiong Yan Y Duan Ming M Wan Haiqin H Li Jun J Zhang Can C Qin Sha S Fang Shenwen S Zhang Run R

Materials (Basel, Switzerland) 20200309 5

For further the understanding of the adsorption mechanism of heavy metal ions on the surface of protein-inorganic hybrid nanoflowers, a novel protein-derived hybrid nanoflower was prepared to investigate the adsorption behavior and reveal the function of organic and inorganic parts on the surface of nanoflowers in the adsorption process in this study. Silk fibroin (SF)-derived and copper-based protein-inorganic hybrid nanoflowers of SF@Cu-NFs were prepared through self-assembly. The product was ...[more]

PMID: 32182957

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Project description:The dissolution of Bombyx mori silk fibroin (SF) films in formic acid (FA) for the preparation of electrospinning dopes is widely exploited to produce electrospun SF scaffolds. The SILKBridge® nerve conduit is an example of medical device having in its wall structure an electrospun component produced from an FA spinning dope. Though highly volatile, residual FA remains trapped into the bulk of the SF nanofibers. The purpose of this work is to investigate the type and strength of the interaction between FA and SF in electrospun mats, to quantify its amount and to evaluate its possible toxicological impact on human health. The presence of residual FA in SF mats was detected by FTIR and Raman spectroscopy (new carbonyl peak at about 1,725 cm-1) and by solid state NMR, which revealed a new carbonyl signal at about 164.3 ppm, attributed to FA by isotopic 13C substitution. Changes occurred also in the spectral ranges of hydroxylated amino acids (Ser and Thr), demonstrating that FA interacted with SF by forming formyl esters. The total amount of FA was determined by HS-GC/MS analysis and accounted for 247 ± 20 μmol/g. The greatest part was present as formyl ester, a small part (about 3%) as free FA. Approximately 17% of the 1,500 μmol/g of hydroxy amino acids (Ser and Thr) theoretically available were involved in the formation of formyl esters. Treatment with alkali (Na2CO3) succeeded to remove the greatest part of FA, but not all. Alkali-treated electrospun SF mats underwent morphological, physical, and mechanical changes. The average diameter of the fibers increased from about 440 nm to about 480 nm, the mat shrunk, became stiffer (the modulus increased from about 5.5 MPa to about 7 MPa), and lost elasticity (the strain decreased from about 1 mm/mm to about 0.8 mm/mm). Biocompatibility studies with human adult dermal fibroblasts did not show significant difference in cell proliferation (313 ± 18 and 309 ± 23 cells/mm2 for untreated and alkali-treated SF mat, respectively) and metabolic activity. An in-depth evaluation of the possible toxicological impact of residual FA was made using the SILKBridge® nerve conduit as case study, following the provisions of the ISO 10993-1 standard. The Potential Patient Daily Intake, calculated from the total amount of FA determined by HS-GC/MS, was 2.4 mg/day and the Tolerable Exposure level was set to 35.4 mg/day. This allowed to obtain a value of the Margin of Safety of 15, indicating that the amount of FA left on SF mats after electrospinning does not raise concerns for human health.

Dataset Information

Investigation on the Adsorption-Interaction Mechanism of Pb(II) at Surface of Silk Fibroin Protein-Derived Hybrid Nanoflower Adsorbent.

Publications

Investigation on the Adsorption-Interaction Mechanism of Pb(II) at Surface of Silk Fibroin Protein-Derived Hybrid Nanoflower Adsorbent.

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