Self-assembling peptide-polymer hydrogels designed from the coiled coil region of fibrin

Peng Jing, Jai S. Rudra, Andrew B. Herr, Joel H. Collier

Research output: Contribution to journalArticle

73 Citations (Scopus)

Abstract

Biomaterials constructed from self-assembling peptides, peptide derivatives, and peptide - polymer conjugates are receiving increasing attention as defined matrices for tissue engineering, controlled therapeutic release, and in vitro cell expansion, but many are constructed from peptide structures not typically found in the human extracellular matrix. Here we report a self-assembling biomaterial constructed from a designed peptide inspired by the coiled coil domain of human fibrin, the major protein constituent of blood clots and the provisional scaffold of wound healing. Targeted substitutions were made in the residues forming the interface between coiled coil strands for a 37-amino acid peptide from human fibrinogen to stabilize the coiled coil peptide bundle, while the solvent-exposed residues were left unchanged to provide a surface similar to that of the native protein. This peptide, which self-assembled into coiled coil dimers and tetramers, was then used to produce triblock peptide-PEG-peptide bioconjugates that self-assembled into viscoelastic hydrogel biomaterials.

Original languageEnglish (US)
Pages (from-to)2438-2446
Number of pages9
JournalBiomacromolecules
Volume9
Issue number9
DOIs
StatePublished - Sep 2008
Externally publishedYes

Fingerprint

Hydrogels
Fibrin
Peptides
Polymers
Biocompatible Materials
Biomaterials
Proteins
Hydrogel
Scaffolds (biology)
Tissue engineering
Scaffolds
Dimers
Fibrinogen
Polyethylene glycols
Amino acids
Blood
Substitution reactions
Derivatives
Amino Acids

ASJC Scopus subject areas

  • Bioengineering
  • Materials Chemistry
  • Polymers and Plastics
  • Biomaterials

Cite this

Self-assembling peptide-polymer hydrogels designed from the coiled coil region of fibrin. / Jing, Peng; Rudra, Jai S.; Herr, Andrew B.; Collier, Joel H.

In: Biomacromolecules, Vol. 9, No. 9, 09.2008, p. 2438-2446.

Research output: Contribution to journalArticle

Jing, Peng ; Rudra, Jai S. ; Herr, Andrew B. ; Collier, Joel H. / Self-assembling peptide-polymer hydrogels designed from the coiled coil region of fibrin. In: Biomacromolecules. 2008 ; Vol. 9, No. 9. pp. 2438-2446.
@article{1264d229071b4aad8c02e1d37c6ff67e,
title = "Self-assembling peptide-polymer hydrogels designed from the coiled coil region of fibrin",
abstract = "Biomaterials constructed from self-assembling peptides, peptide derivatives, and peptide - polymer conjugates are receiving increasing attention as defined matrices for tissue engineering, controlled therapeutic release, and in vitro cell expansion, but many are constructed from peptide structures not typically found in the human extracellular matrix. Here we report a self-assembling biomaterial constructed from a designed peptide inspired by the coiled coil domain of human fibrin, the major protein constituent of blood clots and the provisional scaffold of wound healing. Targeted substitutions were made in the residues forming the interface between coiled coil strands for a 37-amino acid peptide from human fibrinogen to stabilize the coiled coil peptide bundle, while the solvent-exposed residues were left unchanged to provide a surface similar to that of the native protein. This peptide, which self-assembled into coiled coil dimers and tetramers, was then used to produce triblock peptide-PEG-peptide bioconjugates that self-assembled into viscoelastic hydrogel biomaterials.",
author = "Peng Jing and Rudra, {Jai S.} and Herr, {Andrew B.} and Collier, {Joel H.}",
year = "2008",
month = "9",
doi = "10.1021/bm800459v",
language = "English (US)",
volume = "9",
pages = "2438--2446",
journal = "Biomacromolecules",
issn = "1525-7797",
publisher = "American Chemical Society",
number = "9",

}

TY - JOUR

T1 - Self-assembling peptide-polymer hydrogels designed from the coiled coil region of fibrin

AU - Jing, Peng

AU - Rudra, Jai S.

AU - Herr, Andrew B.

AU - Collier, Joel H.

PY - 2008/9

Y1 - 2008/9

N2 - Biomaterials constructed from self-assembling peptides, peptide derivatives, and peptide - polymer conjugates are receiving increasing attention as defined matrices for tissue engineering, controlled therapeutic release, and in vitro cell expansion, but many are constructed from peptide structures not typically found in the human extracellular matrix. Here we report a self-assembling biomaterial constructed from a designed peptide inspired by the coiled coil domain of human fibrin, the major protein constituent of blood clots and the provisional scaffold of wound healing. Targeted substitutions were made in the residues forming the interface between coiled coil strands for a 37-amino acid peptide from human fibrinogen to stabilize the coiled coil peptide bundle, while the solvent-exposed residues were left unchanged to provide a surface similar to that of the native protein. This peptide, which self-assembled into coiled coil dimers and tetramers, was then used to produce triblock peptide-PEG-peptide bioconjugates that self-assembled into viscoelastic hydrogel biomaterials.

AB - Biomaterials constructed from self-assembling peptides, peptide derivatives, and peptide - polymer conjugates are receiving increasing attention as defined matrices for tissue engineering, controlled therapeutic release, and in vitro cell expansion, but many are constructed from peptide structures not typically found in the human extracellular matrix. Here we report a self-assembling biomaterial constructed from a designed peptide inspired by the coiled coil domain of human fibrin, the major protein constituent of blood clots and the provisional scaffold of wound healing. Targeted substitutions were made in the residues forming the interface between coiled coil strands for a 37-amino acid peptide from human fibrinogen to stabilize the coiled coil peptide bundle, while the solvent-exposed residues were left unchanged to provide a surface similar to that of the native protein. This peptide, which self-assembled into coiled coil dimers and tetramers, was then used to produce triblock peptide-PEG-peptide bioconjugates that self-assembled into viscoelastic hydrogel biomaterials.

UR - http://www.scopus.com/inward/record.url?scp=52649118132&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=52649118132&partnerID=8YFLogxK

U2 - 10.1021/bm800459v

DO - 10.1021/bm800459v

M3 - Article

VL - 9

SP - 2438

EP - 2446

JO - Biomacromolecules

JF - Biomacromolecules

SN - 1525-7797

IS - 9

ER -