Growth factor binding on heparin mimetic peptide nanofibers

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buir.contributor.authorMammadov, Rashad
buir.contributor.authorMammadov, Busra
buir.contributor.authorGüler, Mustafa O.
buir.contributor.authorTekinay, Ayşe B.
dc.citation.epage3319en_US
dc.citation.issueNumber10en_US
dc.citation.spage3311en_US
dc.citation.volumeNumber13en_US
dc.contributor.authorMammadov, Rashaden_US
dc.contributor.authorMammadov, Busraen_US
dc.contributor.authorGüler, Mustafa O.en_US
dc.contributor.authorTekinay, Ayşe B.en_US
dc.date.accessioned2016-02-08T09:44:30Z
dc.date.available2016-02-08T09:44:30Z
dc.date.issued2012en_US
dc.departmentInstitute of Materials Science and Nanotechnology (UNAM)en_US
dc.departmentNanotechnology Research Center (NANOTAM)en_US
dc.departmentAysel Sabuncu Brain Research Center (BAM)en_US
dc.description.abstractImmobilization of growth factors in scaffolds is important for controlling their dose and bioactivity for regenerative medicine applications. Although numerous covalent and noncovalent immobilization strategies have been proposed, better growth factor loading and dose control inside the scaffold is necessary. Nature of the binding site on the growth factor interacting with scaffold is critical for preserving and achieving maximal growth factor functionality, which has been a relatively less emphasized issue in previous studies. We recently reported heparin mimetic peptide nanofibers, which mimic chemistry of heparan sulfates. Heparin mimetic nanofibers were shown to bind to vascular endothelial growth factor (VEGF) and direct endothelial cells to angiogenesis. Here, we further investigated interactions between heparin mimetic peptide nanofibers and growth factors. We tested bioactivity of the nanofiber bound growth factors in order to understand the potential use of these peptide nanofiber scaffolds as analogues of heparan sulfates. We observed that heparin mimetic peptide nanofibers demonstrate better binding profiles to VEGF, hepatocyte growth factor (HGF), and fibroblast growth factor-2 (FGF-2) than control peptide nanofibers. We also identified that the heparin-binding domain of VEGF is critical for its interaction with these nanofibers. However, the heparin-binding site is not indispensable for binding of all growth factors to nanofibers. We also showed that binding of growth factors to nanofibers does not cause any loss in bioactivity through in vitro cell culture assays with PC-12 cells. These results reveal that heparin mimetic peptide nanofibers can effectively mimic heparan sulfates in extracellular matrix and provide an optimal milieu for spatial presentation of important growth factors. These properties make peptide nanofiber scaffolds promising materials for regenerative medicine applications through efficient and precisely controlled growth factor delivery. © 2012 American Chemical Society.en_US
dc.identifier.doi10.1021/bm3010897en_US
dc.identifier.eissn1526-4602
dc.identifier.issn1525-7797
dc.identifier.urihttp://hdl.handle.net/11693/21305
dc.language.isoEnglishen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.isversionofhttp://dx.doi.org/10.1021/bm3010897en_US
dc.source.titleBiomacromoleculesen_US
dc.titleGrowth factor binding on heparin mimetic peptide nanofibersen_US
dc.typeArticleen_US
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Institute of Materials Science and Nanotechnology (UNAM)
Aysel Sabuncu Brain Research Center (BAM)
Nanotechnology Research Center (NANOTAM)