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

Journal Article · · Acta Biomaterialia
 [1];  [2];  [2];  [3];  [3];  [4]
  1. Northwestern Univ., Evanston, IL (United States). Dept. of Materials Science and Engineering; Northwestern Univ., Evanston, IL (United States). Simpson Querrey Inst. for BioNanotechnology
  2. Northwestern Univ., Evanston, IL (United States). Simpson Querrey Inst. for BioNanotechnology
  3. Northwestern Univ., Evanston, IL (United States). Dept. of Molecular Pharmacology and Biological Chemistry
  4. Northwestern Univ., Evanston, IL (United States). Dept. of Materials Science and Engineering; Northwestern Univ., Evanston, IL (United States). Dept. of Chemistry; Northwestern Univ., Evanston, IL (United States). Simpson Querrey Inst. for BioNanotechnology; Northwestern Univ., Evanston, IL (United States). Dept. of Medicine

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, in conclusion, 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.

Research Organization:
Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Organization:
USDOE Office of Science (SC); National Institutes of Health (NIH); National Cancer Institute (NCI)
Grant/Contract Number:
AC02-06CH11357; NCI CA060553; 5U54CA151880-03; CA079736
OSTI ID:
1168848
Alternate ID(s):
OSTI ID: 1251696
Journal Information:
Acta Biomaterialia, Vol. 12, Issue C; ISSN 1742-7061
Publisher:
Acta Materialia, Inc.Copyright Statement
Country of Publication:
United States
Language:
ENGLISH
Citation Metrics:
Cited by: 21 works
Citation information provided by
Web of Science

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Cited By (3)

Aqueous self-assembly of short hydrophobic peptides containing norbornene amino acid into supramolecular structures with spherical shape journal January 2016
Drug delivery by supramolecular design journal January 2017
Supramolecular Nanofibers Enhance Growth Factor Signaling by Increasing Lipid Raft Mobility journal April 2016