4.8 Article

BSA modification to reduce CTAB induced nonspecificity and cytotoxicity of aptamer-conjugated gold nanorods

Journal

NANOSCALE
Volume 7, Issue 22, Pages 10240-10248

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/c5nr01704a

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Funding

  1. National Institutes of Health [GM079359, CA133086]
  2. NATIONAL CANCER INSTITUTE [R01CA133086] Funding Source: NIH RePORTER
  3. NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM079359] Funding Source: NIH RePORTER

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Aptamer-conjugated gold nanorods (AuNRs) are excellent candidates for targeted hyperthermia therapy of cancer cells. However, in high concentrations of AuNRs, aptamer conjugation alone fails to result in highly cell-specific AuNRs due to the presence of positively charged cetyltrimethylammonium bromide (CTAB) as a templating surfactant. Besides causing nonspecific electrostatic interactions with the cell surfaces, CTAB can also be cytotoxic, leading to uncontrolled cell death. To avoid the nonspecific interactions and cytotoxicity triggered by CTAB, we report the further biologically inspired modification of aptamer-conjugated AuNRs with bovine serum albumin (BSA) protein. Following this modification, interaction between CTAB and the cell surface was efficiently blocked, thereby dramatically reducing the side effects of CTAB. This approach may provide a general and simple method to avoid one of the most serious issues in biomedical applications of nanomaterials: nonspecific binding of the nanomaterials with biological cells.

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