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Nano-bio interaction between human immunoglobulin G and nontoxic, near-infrared emitting water-borne silicon quantum dot micelles. | LitMetric

AI Article Synopsis

  • The field of nanomaterials is rapidly growing, particularly in biological applications, but their clinical use is hindered by a lack of understanding of how they interact with biological environments.
  • This study investigates how human immunoglobulin G (IgG) changes shape when interacting with specially designed silicon quantum dots (SiQDs), utilizing various advanced techniques to assess these interactions.
  • Findings reveal that these engineered SiQDs have a strong binding affinity for IgG and show minimal toxicity while improving uptake in biological models, indicating potential for effective therapeutic applications without adverse protein changes.

Article Abstract

In recent years, the field of nanomaterials has exponentially expanded with versatile biological applications. However, one of the roadblocks to their clinical translation is the critical knowledge gap about how the nanomaterials interact with the biological microenvironment (nano-bio interactions). When nanomaterials are used as drug carriers or contrast agents for biological imaging, the nano-bio interaction-mediated protein conformational changes and misfolding could lead to disease-related molecular alterations and/or cell death. Here, we studied the conformation changes of human immunoglobulin G (IgG) upon interaction with silicon quantum dots functionalized with 1-decene, Pluronic-F127 (SiQD-De/F127 micelles) using UV-visible, fluorescence steady state and excited state kinetics, circular dichroism, and molecular modeling. Decene monolayer terminated SiQDs are accumulated inside the Pluronic F127 shells to form SiQD-De/F127 micelles and were shown to bind strongly with IgG. In addition, biological evaluation studies in cell lines (HeLa, Fibroblast) and medaka fish (eggs and larvae) showed enhanced uptake and minimal cytotoxicity. Our results substantiate that engineered QDs obviating the protein conformational changes could have adept bioefficacy.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9939978PMC
http://dx.doi.org/10.1039/d3ra00552fDOI Listing

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