File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Differences between top-down and bottom-up approaches in mineralizing thick, partially demineralized collagen scaffolds

TitleDifferences between top-down and bottom-up approaches in mineralizing thick, partially demineralized collagen scaffolds
Authors
KeywordsBiomimetics
Bottom-up
Collagen
Mineralization
Particle-mediated
Top-down
Issue Date2011
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/actabiomat
Citation
Acta Biomaterialia, 2011, v. 7 n. 4, p. 1742-1751 How to Cite?
AbstractBiominerals exhibit complex hierarchical structures derived from bottom-up self-assembly mechanisms. Type I collagen serves as the building block for mineralized tissues such as bone and dentin. In the present study, 250-300 μm thick, partially demineralized collagen scaffolds exhibiting a gradient of demineralization from the base to surface were mineralized using a classical top-down approach and a non-classical bottom-up approach. The top-down approach involved epitaxial growth over seed crystallites. The bottom-up approach utilized biomimetic analogs of matrix proteins to stabilize amorphous calcium phosphate nanoprecursors and template apatite nucleation and growth within the collagen matrix. Micro-computed tomography and transmission electron microscopy were employed to examine mineral uptake and apatite arrangement within the mineralized collagen matrix. The top-down approach could mineralize only the base of the partially demineralized scaffold, where remnant seed crystallites were abundant. Minimal mineralization was observed along the surface of the scaffold; extrafibrillar mineralization was predominantly observed. Conversely, the entire partially demineralized scaffold, including apatite-depleted collagen fibrils, was mineralized by the bottom-up approach, with evidence of both intrafibrillar and extrafibrillar mineralization. Understanding the different mechanisms involved in these two mineralization approaches is pivotal in adopting the optimum strategy for fabricating novel nanostructured materials in bioengineering research. © 2010 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/154658
ISSN
2023 Impact Factor: 9.4
2023 SCImago Journal Rankings: 1.925
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
National Institute of Dental and Craniofacial ResearchR21 DE019213-01
Medical College of Georgia
Funding Information:

This study was generously supported by Grant R21 DE019213-01 from the National Institute of Dental and Craniofacial Research and the PSRP grant from the Medical College of Georgia (P.I. Franklin R. Tay). We thank Lisha Gu for assistance with the operation of the micro-CT, Jongryul Kim for preparing the completely demineralized specimen in the Supplementary Material, Bob Smith for TEM technical assistance and Michelle Barnes for secretarial support.

References

 

DC FieldValueLanguage
dc.contributor.authorLiu, Yen_US
dc.contributor.authorMai, Sen_US
dc.contributor.authorLi, Nen_US
dc.contributor.authorYiu, CKYen_US
dc.contributor.authorMao, Jen_US
dc.contributor.authorPashley, DHen_US
dc.contributor.authorTay, FRen_US
dc.date.accessioned2012-08-08T08:26:46Z-
dc.date.available2012-08-08T08:26:46Z-
dc.date.issued2011en_US
dc.identifier.citationActa Biomaterialia, 2011, v. 7 n. 4, p. 1742-1751en_US
dc.identifier.issn1742-7061en_US
dc.identifier.urihttp://hdl.handle.net/10722/154658-
dc.description.abstractBiominerals exhibit complex hierarchical structures derived from bottom-up self-assembly mechanisms. Type I collagen serves as the building block for mineralized tissues such as bone and dentin. In the present study, 250-300 μm thick, partially demineralized collagen scaffolds exhibiting a gradient of demineralization from the base to surface were mineralized using a classical top-down approach and a non-classical bottom-up approach. The top-down approach involved epitaxial growth over seed crystallites. The bottom-up approach utilized biomimetic analogs of matrix proteins to stabilize amorphous calcium phosphate nanoprecursors and template apatite nucleation and growth within the collagen matrix. Micro-computed tomography and transmission electron microscopy were employed to examine mineral uptake and apatite arrangement within the mineralized collagen matrix. The top-down approach could mineralize only the base of the partially demineralized scaffold, where remnant seed crystallites were abundant. Minimal mineralization was observed along the surface of the scaffold; extrafibrillar mineralization was predominantly observed. Conversely, the entire partially demineralized scaffold, including apatite-depleted collagen fibrils, was mineralized by the bottom-up approach, with evidence of both intrafibrillar and extrafibrillar mineralization. Understanding the different mechanisms involved in these two mineralization approaches is pivotal in adopting the optimum strategy for fabricating novel nanostructured materials in bioengineering research. © 2010 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.en_US
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/actabiomaten_US
dc.relation.ispartofActa Biomaterialiaen_US
dc.subjectBiomimetics-
dc.subjectBottom-up-
dc.subjectCollagen-
dc.subjectMineralization-
dc.subjectParticle-mediated-
dc.subjectTop-down-
dc.subject.meshCollagen - Metabolism - Ultrastructureen_US
dc.subject.meshHumansen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshMinerals - Metabolismen_US
dc.subject.meshNanotechnology - Methodsen_US
dc.subject.meshTime Factorsen_US
dc.subject.meshTissue Scaffolds - Chemistryen_US
dc.titleDifferences between top-down and bottom-up approaches in mineralizing thick, partially demineralized collagen scaffoldsen_US
dc.typeArticleen_US
dc.identifier.emailYiu, CKY:ckyyiu@hkucc.hku.hken_US
dc.identifier.authorityYiu, CKY=rp00018en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.doi10.1016/j.actbio.2010.11.028en_US
dc.identifier.pmid21111071en_US
dc.identifier.pmcidPMC3050119-
dc.identifier.scopuseid_2-s2.0-79952184601en_US
dc.identifier.hkuros184894-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79952184601&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume7en_US
dc.identifier.issue4en_US
dc.identifier.spage1742en_US
dc.identifier.epage1751en_US
dc.identifier.isiWOS:000288971300035-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridLiu, Y=36013814100en_US
dc.identifier.scopusauthoridMai, S=8553591000en_US
dc.identifier.scopusauthoridLi, N=36659653900en_US
dc.identifier.scopusauthoridYiu, CKY=7007115156en_US
dc.identifier.scopusauthoridMao, J=9042779600en_US
dc.identifier.scopusauthoridPashley, DH=35448600800en_US
dc.identifier.scopusauthoridTay, FR=7102091962en_US
dc.identifier.issnl1742-7061-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats