Supramolecular assembly of multifunctional maspin-mimetic nanostructures as a potent peptide-based angiogenesis inhibitor

R. Helen Zha, Shantanu Sur, Job Boekhoven, Heidi Y. Shi, Ming Zhang, Samuel I Stupp

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Aberrant angiogenesis plays a large role in pathologies ranging from tumor growth to macular degeneration. Anti-angiogenic proteins have thus come under scrutiny as versatile, potent therapeutics but face problems with purification and tissue retention. We report here on the synthesis of supramolecular nanostructures that mimic the anti-angiogenic activity of maspin, a class II tumor suppressor protein. These maspin-mimetic nanostructures are formed via self-assembly of small peptide amphiphiles containing the g-helix motif of maspin. Using tubulogenesis assays with human umbilical vein endothelial cells, we demonstrate that maspin-mimetic nanostructures show anti-angiogenic activity at concentrations that are significantly lower than those necessary for the g-helix peptide. Furthermore, in vivo assays in the chick chorioallantoic membrane show maspin-mimetic nanostructures to be effective over controls at inhibiting angiogenesis. Thus, the nanostructures investigated here offer an attractive alternative to the use of anti-angiogenic recombinant proteins in the treatment of cancer or other diseases involving abnormal blood vessel formation.

Original languageEnglish
Pages (from-to)1-10
Number of pages10
JournalActa Biomaterialia
Volume12
Issue numberC
DOIs
Publication statusPublished - 2015

Fingerprint

Angiogenesis Inhibitors
Nanostructures
Peptides
Angiogenic Proteins
Tumors
Assays
Proteins
Tumor Suppressor Proteins
Chorioallantoic Membrane
Recombinant proteins
Amphiphiles
Endothelial cells
Human Umbilical Vein Endothelial Cells
Blood vessels
Macular Degeneration
Pathology
Recombinant Proteins
Self assembly
Purification
Blood Vessels

Keywords

  • Anti-angiogenic
  • g-Helix
  • Maspin
  • Peptide amphiphile
  • Self-assembly

ASJC Scopus subject areas

  • Biomaterials
  • Biomedical Engineering
  • Biotechnology
  • Biochemistry
  • Molecular Biology

Cite this

Supramolecular assembly of multifunctional maspin-mimetic nanostructures as a potent peptide-based angiogenesis inhibitor. / Zha, R. Helen; Sur, Shantanu; Boekhoven, Job; Shi, Heidi Y.; Zhang, Ming; Stupp, Samuel I.

In: Acta Biomaterialia, Vol. 12, No. C, 2015, p. 1-10.

Research output: Contribution to journalArticle

Zha, R. Helen ; Sur, Shantanu ; Boekhoven, Job ; Shi, Heidi Y. ; Zhang, Ming ; Stupp, Samuel I. / Supramolecular assembly of multifunctional maspin-mimetic nanostructures as a potent peptide-based angiogenesis inhibitor. In: Acta Biomaterialia. 2015 ; Vol. 12, No. C. pp. 1-10.
@article{f72e0e662f944a0cb396903c697ae4e8,
title = "Supramolecular assembly of multifunctional maspin-mimetic nanostructures as a potent peptide-based angiogenesis inhibitor",
abstract = "Aberrant angiogenesis plays a large role in pathologies ranging from tumor growth to macular degeneration. Anti-angiogenic proteins have thus come under scrutiny as versatile, potent therapeutics but face problems with purification and tissue retention. We report here on the synthesis of supramolecular nanostructures that mimic the anti-angiogenic activity of maspin, a class II tumor suppressor protein. These maspin-mimetic nanostructures are formed via self-assembly of small peptide amphiphiles containing the g-helix motif of maspin. Using tubulogenesis assays with human umbilical vein endothelial cells, we demonstrate that maspin-mimetic nanostructures show anti-angiogenic activity at concentrations that are significantly lower than those necessary for the g-helix peptide. Furthermore, in vivo assays in the chick chorioallantoic membrane show maspin-mimetic nanostructures to be effective over controls at inhibiting angiogenesis. Thus, the nanostructures investigated here offer an attractive alternative to the use of anti-angiogenic recombinant proteins in the treatment of cancer or other diseases involving abnormal blood vessel formation.",
keywords = "Anti-angiogenic, g-Helix, Maspin, Peptide amphiphile, Self-assembly",
author = "Zha, {R. Helen} and Shantanu Sur and Job Boekhoven and Shi, {Heidi Y.} and Ming Zhang and Stupp, {Samuel I}",
year = "2015",
doi = "10.1016/j.actbio.2014.11.001",
language = "English",
volume = "12",
pages = "1--10",
journal = "Acta Biomaterialia",
issn = "1742-7061",
publisher = "Elsevier BV",
number = "C",

}

TY - JOUR

T1 - Supramolecular assembly of multifunctional maspin-mimetic nanostructures as a potent peptide-based angiogenesis inhibitor

AU - Zha, R. Helen

AU - Sur, Shantanu

AU - Boekhoven, Job

AU - Shi, Heidi Y.

AU - Zhang, Ming

AU - Stupp, Samuel I

PY - 2015

Y1 - 2015

N2 - Aberrant angiogenesis plays a large role in pathologies ranging from tumor growth to macular degeneration. Anti-angiogenic proteins have thus come under scrutiny as versatile, potent therapeutics but face problems with purification and tissue retention. We report here on the synthesis of supramolecular nanostructures that mimic the anti-angiogenic activity of maspin, a class II tumor suppressor protein. These maspin-mimetic nanostructures are formed via self-assembly of small peptide amphiphiles containing the g-helix motif of maspin. Using tubulogenesis assays with human umbilical vein endothelial cells, we demonstrate that maspin-mimetic nanostructures show anti-angiogenic activity at concentrations that are significantly lower than those necessary for the g-helix peptide. Furthermore, in vivo assays in the chick chorioallantoic membrane show maspin-mimetic nanostructures to be effective over controls at inhibiting angiogenesis. Thus, the nanostructures investigated here offer an attractive alternative to the use of anti-angiogenic recombinant proteins in the treatment of cancer or other diseases involving abnormal blood vessel formation.

AB - Aberrant angiogenesis plays a large role in pathologies ranging from tumor growth to macular degeneration. Anti-angiogenic proteins have thus come under scrutiny as versatile, potent therapeutics but face problems with purification and tissue retention. We report here on the synthesis of supramolecular nanostructures that mimic the anti-angiogenic activity of maspin, a class II tumor suppressor protein. These maspin-mimetic nanostructures are formed via self-assembly of small peptide amphiphiles containing the g-helix motif of maspin. Using tubulogenesis assays with human umbilical vein endothelial cells, we demonstrate that maspin-mimetic nanostructures show anti-angiogenic activity at concentrations that are significantly lower than those necessary for the g-helix peptide. Furthermore, in vivo assays in the chick chorioallantoic membrane show maspin-mimetic nanostructures to be effective over controls at inhibiting angiogenesis. Thus, the nanostructures investigated here offer an attractive alternative to the use of anti-angiogenic recombinant proteins in the treatment of cancer or other diseases involving abnormal blood vessel formation.

KW - Anti-angiogenic

KW - g-Helix

KW - Maspin

KW - Peptide amphiphile

KW - Self-assembly

UR - http://www.scopus.com/inward/record.url?scp=84927709679&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84927709679&partnerID=8YFLogxK

U2 - 10.1016/j.actbio.2014.11.001

DO - 10.1016/j.actbio.2014.11.001

M3 - Article

VL - 12

SP - 1

EP - 10

JO - Acta Biomaterialia

JF - Acta Biomaterialia

SN - 1742-7061

IS - C

ER -