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

Garcia, Yarima Sanchez; Barros, Marcela Rodrigues; Queiroz, Rafaela Muniz de; Todeschini, Adriane R.; Neves, Jorge Luiz

doi:10.1016/j.molliq.2019.111460

Cited by 14 publications

(5 citation statements)

References 44 publications

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“…The ease of preparation and modification of CQDs offers advantages not only in fine-tuning of their electronic and optical properties but also mediation of the interaction between CQDs and analytes leading to fluorescence quenching or enhancement. Due to the diverse surface structure of CQDs, they are known to be able to interact with many compounds and biomolecules via a variety of intermolecular interactions [8][9][10][11]. Examples include oligonucleotides (electrostatic, hydrogen bonding, and p-p stacking interaction), proteins (electrostatic, hydrogen bonding, and hydrophobic interaction), and metal ions (hard-soft acid-base (HSAB) interactions).…”

Section: Introductionmentioning

confidence: 99%

Carbon quantum dots for the detection of antibiotics and pesticides

Chu¹,

Unnikrishnan²,

Anand³

et al. 2020

Journal of Food and Drug Analysis

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Section: Introductionmentioning

confidence: 99%

Carbon quantum dots for the detection of antibiotics and pesticides

Chu¹,

Unnikrishnan²,

Anand³

et al. 2020

Journal of Food and Drug Analysis

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“…Alternatively, some studies investigate albumin fragments to the task 45 Moreover, protein structural modification on the HTF-MnCQD complex is corroborated by λ max shifts observed on the fluorescence quenching experiments. Our previous investigation 46 with small anionic non-metallic CQDs from the same source revealed that the HTF also underwent secondary structure modification through NP interaction, and it was followed by subtle iron release from HTF. Despite these relevant observations, it was still not possible to identify the modified protein region by complex formation with CQDs and also with MnCQDs.…”

Section: Discussionmentioning

confidence: 99%

Non-passivated manganese-based carbonaceous nanoparticles selectively target kidney outer medulla, exhibiting renal clearance, high T1-weighted MRI contrast, subtle citotoxicity and low opsonization level.

Garcia¹,

Menezes

Barros

et al. 2021

Preprint

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Nanoparticle passivation by molecular recognition moieties (small molecules, aptamers, antibodies) imputes unique characteristics to nanoparticles (NPs) and unlocks their fascinating selectivity to targeting disease sites. Although non-passivated nanomaterials may archive selective targeting by exploring NP features and their interaction with biofluids proteins, such studies are scarce in the literature. Here, we report spherical manganese-based carbonaceous NPs (MnCQD), which specifically target mice kidneys after intravenous injection, even without direct surface chemical modification. Also, the NPs provide high image contrast in T1 magnetic resonance imaging (MRI) with subtle toxicological effects. The unexpected selectivity of MnCQD to the kidney has been examined based on their determined intrinsic properties and their interaction with two blood proteins: Bovine Serum Albumin (BSA), and Human Transferrin (HTF). More particularly, aspects such as size, composition, superficial charge, spectroscopic features, interaction mechanism, affinities, thermodynamic, and protein structural changes have been investigated. All these results highlight the excellent potential of MnCQD as a low toxic T1-MRI contrast agent and open the prospect of using non-functionalized NPs as a selective agent to target specific organs.

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“…CDs tightly bind to human Tf (hTf) via hydrophobic forces and electrostatic interactions, inducing structural changes in hTf. 217 The conformational changes of hTf cause iron release from the hTf lobes, highlighting the subtle toxicological effect of CDs at the molecular level. The conformational changes in hTf could be due to the non-synergetic anion function of CDs, which bind allosterically to the hTf site and alter its structure.…”

Section: Role Of Nanoparticles In Protein Corona Conformationmentioning

confidence: 99%