Supramolecular assembly of multifunctional maspin-mimetic nanostructures as a potent peptide-based angiogenesis inhibitor
Journal Article
·
· Acta Biomaterialia
- Northwestern Univ., Evanston, IL (United States). Dept. of Materials Science and Engineering; Northwestern Univ., Evanston, IL (United States). Simpson Querrey Inst. for BioNanotechnology
- Northwestern Univ., Evanston, IL (United States). Simpson Querrey Inst. for BioNanotechnology
- Northwestern Univ., Evanston, IL (United States). Dept. of Molecular Pharmacology and Biological Chemistry
- 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:
- Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
- Sponsoring Organization:
- National Cancer Institute (NCI); National Institutes of Health (NIH); USDOE; USDOE Office of Science (SC)
- Grant/Contract Number:
- AC02-06CH11357
- OSTI ID:
- 1168848
- Alternate ID(s):
- OSTI ID: 1251696
- Journal Information:
- Acta Biomaterialia, Journal Name: Acta Biomaterialia Journal Issue: C Vol. 12; ISSN 1742-7061
- Publisher:
- Acta Materialia, Inc.Copyright Statement
- Country of Publication:
- United States
- Language:
- ENGLISH
Supramolecular Nanofibers Enhance Growth Factor Signaling by Increasing Lipid Raft Mobility
|
journal | April 2016 |
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 |
Similar Records
Type I Collagen and Collagen Mimetics as Angiogenesis Promoting Superpolymers
Angiogenin-induced protein kinase B/Akt activation is necessary for angiogenesis but is independent of nuclear translocation of angiogenin in HUVE cells
Suppression of alpha-tocopherol ether-linked acetic acid in VEGF-induced angiogenesis and the possible mechanisms in human umbilical vein endothelial cells
Journal Article
·
Fri Jul 18 00:00:00 EDT 2008
· Curr. Pharm. Design
·
OSTI ID:1007649
Angiogenin-induced protein kinase B/Akt activation is necessary for angiogenesis but is independent of nuclear translocation of angiogenin in HUVE cells
Journal Article
·
Thu Jan 11 23:00:00 EST 2007
· Biochemical and Biophysical Research Communications
·
OSTI ID:20857958
Suppression of alpha-tocopherol ether-linked acetic acid in VEGF-induced angiogenesis and the possible mechanisms in human umbilical vein endothelial cells
Journal Article
·
Sun Dec 14 23:00:00 EST 2014
· Toxicology and Applied Pharmacology
·
OSTI ID:22439935