Site-specific protein conjugation onto fluorescent single-walled carbon nanotubes

Zubkovs, V ; Sharif University of Technology | 2020

417 Viewed
  1. Type of Document: Article
  2. DOI: 10.1021/acs.chemmater.0c02051
  3. Publisher: American Chemical Society , 2020
  4. Abstract:
  5. Semiconducting single-walled carbon nanotubes (SWCNTs) are among the few photostable optical emitters that are ideal for sensing, imaging, drug delivery, and monitoring of protein activity. These applications often require strategies for immobilizing proteins onto the nanotube while preserving the optical properties of the SWCNTs. Site-specific and oriented immobilization strategies, in particular, offer advantages for improving sensor and optical signaling responses. In this study, we demonstrate site-specific protein immobilization of a model of enhanced yellow fluorescent protein with a single engineered cysteine residue, using either single-stranded DNA or a pyrene-containing linker to interact with the SWCNT surface. Protein expression and bioconjugation were characterized using a combination of gel electrophoresis, absorbance, fluorescence, mass spectrometry, and circular dichroism measurements. The results confirm successful protein immobilization onto SWCNTs, which retain their near-infrared fluorescence following conjugation. The successful demonstration of these bioconjugation strategies serves as a basis for more cost-effective, site-specific immobilization strategies that can help preserve protein folding and functionality. © 2020 American Chemical Society
  6. Keywords:
  7. Amino acids ; Cost effectiveness ; Dichroism ; DNA ; Drug delivery ; Electrophoresis ; Fluorescence ; Infrared devices ; Mass spectrometry ; Nanotubes ; Proteins ; Circular dichroism measurements ; Enhanced yellow fluorescent proteins ; Near-infrared fluorescence ; Oriented immobilizations ; Protein conjugations ; Protein expressions ; Protein immobilization ; Single-walled carbon nanotube (SWCNTs)
  8. Source: Chemistry of Materials ; Volume 32, Issue 20 , 2020 , Pages 8798-8807
  9. URL: https://pubs.acs.org/doi/10.1021/acs.chemmater.0c02051