Branched peptide-amphiphiles as self-assembling coatings for tissue engineering scaffolds

Daniel A. Harrington, Earl Y. Cheng, Mustafa O. Guler, Leslie K. Lee, Jena L. Donovan, Randal C. Claussen, Samuel I Stupp

Research output: Contribution to journalArticle

136 Citations (Scopus)

Abstract

An important challenge in regenerative medicine is the design of suitable bioactive scaffold materials that can act as artificial extracellular matrices. We reported previously on a family of peptide-amphiphile (PA) molecules that self-assemble into high-aspect ratio nanofibers under physiological conditions, and can display bioactive peptide epitopes along each nanofiber's periphery. One type of PA displays its epitope at a branched site using a lysine dendron, a molecular feature that improves epitope availability on the nanofiber surface. In this work, we describe the application of these branched PA (b-PA) systems as self-assembling coatings for fiber-bonded poly(glycolic acid) scaffolds. b-PAs bearing variations of the RGDS adhesion epitope from fibronectin were shown by elemental analysis to coat repeatably onto fiber scaffolds. The retention of supramolecular organization after coating on the scaffold was demonstrated through spectroscopic identification of β-sheet structures and the close association of hydrophobic tails in a model pyrene-containing PA system. Primary human bladder smooth muscle cells demonstrated greater initial adhesion to b-PA-functionalized scaffolds than to bare scaffolds or to those coated with linear PAs. This strategy of molecular design and coating may have potential application in bladder tissue regeneration.

Original languageEnglish
Pages (from-to)157-167
Number of pages11
JournalJournal of Biomedical Materials Research - Part A
Volume78
Issue number1
DOIs
Publication statusPublished - Jul 2006

Fingerprint

Tissue Scaffolds
Amphiphiles
Scaffolds (biology)
Tissue engineering
Scaffolds
Peptides
Epitopes
Coatings
Nanofibers
glycolic acid
Bearings (structural)
Adhesion
Tissue regeneration
Fibers
Pyrene
Fibronectins
Lysine
Muscle
Aspect ratio
Cells

Keywords

  • Bladder
  • Regenerative medicine
  • Self-assembly
  • Supramolecular
  • Tissue engineering

ASJC Scopus subject areas

  • Biomedical Engineering
  • Biomaterials

Cite this

Branched peptide-amphiphiles as self-assembling coatings for tissue engineering scaffolds. / Harrington, Daniel A.; Cheng, Earl Y.; Guler, Mustafa O.; Lee, Leslie K.; Donovan, Jena L.; Claussen, Randal C.; Stupp, Samuel I.

In: Journal of Biomedical Materials Research - Part A, Vol. 78, No. 1, 07.2006, p. 157-167.

Research output: Contribution to journalArticle

Harrington, Daniel A. ; Cheng, Earl Y. ; Guler, Mustafa O. ; Lee, Leslie K. ; Donovan, Jena L. ; Claussen, Randal C. ; Stupp, Samuel I. / Branched peptide-amphiphiles as self-assembling coatings for tissue engineering scaffolds. In: Journal of Biomedical Materials Research - Part A. 2006 ; Vol. 78, No. 1. pp. 157-167.
@article{e06b3195d6d24754a081ec45aff743aa,
title = "Branched peptide-amphiphiles as self-assembling coatings for tissue engineering scaffolds",
abstract = "An important challenge in regenerative medicine is the design of suitable bioactive scaffold materials that can act as artificial extracellular matrices. We reported previously on a family of peptide-amphiphile (PA) molecules that self-assemble into high-aspect ratio nanofibers under physiological conditions, and can display bioactive peptide epitopes along each nanofiber's periphery. One type of PA displays its epitope at a branched site using a lysine dendron, a molecular feature that improves epitope availability on the nanofiber surface. In this work, we describe the application of these branched PA (b-PA) systems as self-assembling coatings for fiber-bonded poly(glycolic acid) scaffolds. b-PAs bearing variations of the RGDS adhesion epitope from fibronectin were shown by elemental analysis to coat repeatably onto fiber scaffolds. The retention of supramolecular organization after coating on the scaffold was demonstrated through spectroscopic identification of β-sheet structures and the close association of hydrophobic tails in a model pyrene-containing PA system. Primary human bladder smooth muscle cells demonstrated greater initial adhesion to b-PA-functionalized scaffolds than to bare scaffolds or to those coated with linear PAs. This strategy of molecular design and coating may have potential application in bladder tissue regeneration.",
keywords = "Bladder, Regenerative medicine, Self-assembly, Supramolecular, Tissue engineering",
author = "Harrington, {Daniel A.} and Cheng, {Earl Y.} and Guler, {Mustafa O.} and Lee, {Leslie K.} and Donovan, {Jena L.} and Claussen, {Randal C.} and Stupp, {Samuel I}",
year = "2006",
month = "7",
doi = "10.1002/jbm.a.30718",
language = "English",
volume = "78",
pages = "157--167",
journal = "Journal of Biomedical Materials Research - Part A",
issn = "0021-9304",
publisher = "John Wiley and Sons Inc.",
number = "1",

}

TY - JOUR

T1 - Branched peptide-amphiphiles as self-assembling coatings for tissue engineering scaffolds

AU - Harrington, Daniel A.

AU - Cheng, Earl Y.

AU - Guler, Mustafa O.

AU - Lee, Leslie K.

AU - Donovan, Jena L.

AU - Claussen, Randal C.

AU - Stupp, Samuel I

PY - 2006/7

Y1 - 2006/7

N2 - An important challenge in regenerative medicine is the design of suitable bioactive scaffold materials that can act as artificial extracellular matrices. We reported previously on a family of peptide-amphiphile (PA) molecules that self-assemble into high-aspect ratio nanofibers under physiological conditions, and can display bioactive peptide epitopes along each nanofiber's periphery. One type of PA displays its epitope at a branched site using a lysine dendron, a molecular feature that improves epitope availability on the nanofiber surface. In this work, we describe the application of these branched PA (b-PA) systems as self-assembling coatings for fiber-bonded poly(glycolic acid) scaffolds. b-PAs bearing variations of the RGDS adhesion epitope from fibronectin were shown by elemental analysis to coat repeatably onto fiber scaffolds. The retention of supramolecular organization after coating on the scaffold was demonstrated through spectroscopic identification of β-sheet structures and the close association of hydrophobic tails in a model pyrene-containing PA system. Primary human bladder smooth muscle cells demonstrated greater initial adhesion to b-PA-functionalized scaffolds than to bare scaffolds or to those coated with linear PAs. This strategy of molecular design and coating may have potential application in bladder tissue regeneration.

AB - An important challenge in regenerative medicine is the design of suitable bioactive scaffold materials that can act as artificial extracellular matrices. We reported previously on a family of peptide-amphiphile (PA) molecules that self-assemble into high-aspect ratio nanofibers under physiological conditions, and can display bioactive peptide epitopes along each nanofiber's periphery. One type of PA displays its epitope at a branched site using a lysine dendron, a molecular feature that improves epitope availability on the nanofiber surface. In this work, we describe the application of these branched PA (b-PA) systems as self-assembling coatings for fiber-bonded poly(glycolic acid) scaffolds. b-PAs bearing variations of the RGDS adhesion epitope from fibronectin were shown by elemental analysis to coat repeatably onto fiber scaffolds. The retention of supramolecular organization after coating on the scaffold was demonstrated through spectroscopic identification of β-sheet structures and the close association of hydrophobic tails in a model pyrene-containing PA system. Primary human bladder smooth muscle cells demonstrated greater initial adhesion to b-PA-functionalized scaffolds than to bare scaffolds or to those coated with linear PAs. This strategy of molecular design and coating may have potential application in bladder tissue regeneration.

KW - Bladder

KW - Regenerative medicine

KW - Self-assembly

KW - Supramolecular

KW - Tissue engineering

UR - http://www.scopus.com/inward/record.url?scp=33745612238&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33745612238&partnerID=8YFLogxK

U2 - 10.1002/jbm.a.30718

DO - 10.1002/jbm.a.30718

M3 - Article

C2 - 16619254

AN - SCOPUS:33745612238

VL - 78

SP - 157

EP - 167

JO - Journal of Biomedical Materials Research - Part A

JF - Journal of Biomedical Materials Research - Part A

SN - 0021-9304

IS - 1

ER -