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Structural modification of protease inducible preprogrammed nanofiber precursor.

Benedict Law1, Ching-Hsuan Tung

  • 1Center for Molecular Imaging Research, Massachusetts General Hospital, Harvard Medical School, Charlestown, Massachusetts 02129, USA. Shek.law@ndsu.edu

Biomacromolecules
|January 8, 2008
PubMed
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New peptide-based nanofibers detect urokinase plasminogen activator (uPA) by fluorescence. Upon protease degradation, they form hydrogels, enabling diagnostic sensors and drug delivery for protease-associated diseases.

Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Biomedical Engineering

Background:

  • Proteases like urokinase plasminogen activator (uPA) are overexpressed in tumors.
  • Previous work introduced uPA-degradable peptide-based hydrogels for drug delivery.
  • Fluorescent nanofibers were developed for uPA activity detection via optical imaging.

Purpose of the Study:

  • To investigate the structural and optical responses of nanofiber precursors (NFPs) to protease activity.
  • To explore the potential of these responsive nanomaterials as diagnostic sensors and drug delivery platforms.

Main Methods:

  • Design and synthesis of fluorescent nanofibers incorporating methoxyl polyethylene glycol (MPEG) and a FITC-labeled peptide core.
  • Exposure of nanofiber precursors (NFPs) to a model protease.

Related Experiment Videos

  • Analysis of morphological changes and fluorescence properties using optical imaging.

    • Main Results:

    • Protease degradation released FITC-containing hydrophilic fragments, amplifying fluorescence.
    • Remaining self-assembling residues transformed into micrometer-sized hydrogel networks.
    • Observed unique morphological and optical changes in response to protease activity.

    Conclusions:

    • The developed NFPs exhibit significant structural and optical responses to protease activity.
    • These responsive nanomaterials show promise as diagnostic sensors for specific proteases.
    • Potential applications include dual systemic and functional nanoplatforms for protease-associated diseases.