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Molecular biosensing system based on intrinsically disordered proteins.

Kyle A Cissell1, Suresh Shrestha, Jennifer Purdie

  • 1Department of Chemistry and Chemical Biology, Indiana University Purdue University Indianapolis, 402 N. Blackford Street, Room LD 326, Indianapolis, IN, 46217, USA.

Analytical and Bioanalytical Chemistry
|January 15, 2008
PubMed
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Intrinsically disordered proteins (IDPs) like BRCA1 can detect tumor suppressor p53 by changing structure upon binding. This study demonstrates IDPs as novel biological recognition elements for sensitive protein detection using fluorescence.

Area of Science:

  • Biochemistry and Molecular Biology
  • Biotechnology and Biosensing
  • Protein Science

Background:

  • Intrinsically disordered proteins (IDPs) exhibit dynamic structures and specific binding interactions.
  • IDPs are increasingly recognized for their potential as biological recognition elements in sensing applications.
  • The BRCA1/p53 interaction involves a conformational change in BRCA1, offering a basis for detection.

Purpose of the Study:

  • To demonstrate the utility of intrinsically disordered proteins (IDPs) as biological recognition elements for sensing.
  • To establish a proof-of-concept for detecting tumor suppressor protein p53 using BRCA1.
  • To investigate the use of both intrinsic and extrinsic fluorescence for detecting p53 via BRCA1 binding.

Main Methods:

  • Utilized BRCA1 (residues 219-498) as the recognition element for detecting p53 (residues 311-393).

Related Experiment Videos

  • Employed circular dichroism (CD) spectroscopy to observe BRCA1's disorder-to-order conformational transition upon p53 binding.
  • Applied intrinsic tryptophan fluorescence and extrinsic fluorescent probes (TMR, dansyl-X, SE) conjugated to BRCA1 for p53 detection.

    • Main Results:

    • BRCA1's conformational change upon p53 binding was confirmed by CD measurements.
    • Intrinsic BRCA1 fluorescence detected p53 with a limit of detection (LOD) of 0.559 nM.
    • Extrinsic probes (TMR, dansyl-X, SE) conjugated to BRCA1 showed enhanced sensitivity for p53 detection, with LODs of 1.50 nM for dansyl-X, SE-conjugated BRCA1.
    • Conjugation of fluorophores did not disrupt the p53/BRCA1 binding interaction.

    Conclusions:

    • Intrinsically disordered proteins, exemplified by BRCA1, can function as effective biological recognition elements for protein detection.
    • The conformational change induced by p53 binding to BRCA1 provides a reliable signal for sensing.
    • Environmentally sensitive fluorophores conjugated to IDPs offer a sensitive and validated approach for detecting target molecules that induce structural changes.