Biologically-Based Self-Assembling Hydrogels

Abstract

We have developed polymers, which borrowing from biology, assemble into networks. The self-assembly regions of fibrinogen were cloned to form a scaffolding that either interacts with fibrin or assembles independently. Peptides consisting of a binding pocket (BP), ligand (L), and/or a Factor XIIIa substrate were synthesized and conjugated to methacroylated dextran or acrylated poly(ethylene glycol). Peptide-conjugated dextran was added to polymerizing fibrin, and the resulting hydrogels were evaluated rheologically. These conjugates significantly affected the mechanical properties of fibrin while the addition of unconjugated dextran did not. The BP and L peptides were conjugated to PEG star polymer. Mixtures of conjugated PEG-BP and PEG-L were found to assemble. This work shows that peptides directing assembly can be designed using motifs found in proteins. The peptides in this study not only alter the mechanical properties of fibrin, but also allow a mechanism for creating a self-assembling network.

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Document Details

Document Type
Technical Report
Publication Date
Apr 01, 2002
Accession Number
ADP014396

Entities

People

  • Alyssa Panitch
  • Brandon L. Seal

Organizations

  • Arizona State University

Tags

DTIC Thesaurus Topics

  • Alkenes
  • Amino Acids
  • Assembly
  • Chemical Synthesis
  • Chemistry
  • Crystal Structure
  • Essential Amino Acids
  • Hydrogels
  • Materials
  • Mechanical Properties
  • Mixtures
  • Molecules
  • Organic Chemistry
  • Polymers
  • Self Assembly
  • Synthetic Polymers

Readers

  • Molecular and Cellular Biochemistry
  • Nanocomposite Materials Science
  • Polymer Science and Technology