Probing the interaction of carbonaceous dots with transferrin and albumin: Impact on the protein structure and non-synergetic metal release

Abstract Carbon quantum dots (CQD) have been emerging as an essential material for biological applications due to their relevant properties. Here, we synthesized and characterized low toxic anionic carbon dots and examined the interaction of the nanoparticles with human transferrin (hTf) and bovine serum albumin (BSA) by using multi-spectroscopic techniques. CQD showed low cytotoxic effect against HBMEC, A549, and HTC116 cells. Temperature variable fluorescence experiments reveal that CQD quench the BSA and hTf intrinsic fluorescence following a dynamical and static mechanisms, respectively. Both proteins attach tightly to the nanoparticle (Ka ≈ 104–105 M−1), and hydrophobic forces drive the binding. Additionally, hTf-CQD interaction is also guided by electrostatic interaction. Furthermore, protein CD spectra reveal that both proteins experience structural changes during nanoparticle interaction, which differs from previously reported anionic carbon dots from other sources. Experiments corroborate the observed structural modifications and unveil that the nanoparticle interaction induces iron release from hTf lobes. The mechanism of hTf iron release induced by CQD can be understood based on anionic non-synergetic effects.

• Publication year

  2019

• Venue

  Journal of Molecular Liquids

• Publication date

  2019-10-15

• Fields of study

  Materials Science, Chemistry

• Identifiers
  DOI 10.1016/J.MOLLIQ.2019.111460
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

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