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- Publisher Website: 10.1002/jbm.a.34004
- Scopus: eid_2-s2.0-84856235129
- PMID: 22213622
- WOS: WOS:000299414400018
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Article: Evaluation of chemically modified SLA implants (modSLA) biofunctionalized with integrin (RGD)- and heparin (KRSR)-binding peptides
Title | Evaluation of chemically modified SLA implants (modSLA) biofunctionalized with integrin (RGD)- and heparin (KRSR)-binding peptides |
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Authors | |
Keywords | removal torque value extracellular matrix protein binding sequences histomorphometry titanium surfaces biofunctionalized with biologically active peptides chemically modified sandblasted and acid-etched titanium implant surfaces |
Issue Date | 2012 |
Citation | Journal of Biomedical Materials Research - Part A, 2012, v. 100 A, n. 3, p. 703-711 How to Cite? |
Abstract | Enhancing osseointegration through surface immobilization of multiple short peptide sequences that mimic extracellular matrix (ECM) proteins, such as arginine-glycine-aspartic acid (RGD) and lysine-arginine-serine-arginine (KRSR), has not yet been extensively explored. Additionally, the effect of biofunctionalizing chemically modified sandblasted and acid-etched surfaces (modSLA) is unknown. The present study evaluated modSLA implant surfaces modified with RGD and KRSR for potentially enhanced effects on bone apposition and interfacial shear strength during early stages of bone regeneration. Two sets of experimental implants were placed in the maxillae of eight miniature pigs, known for their rapid wound healing kinetics: bone chamber implants creating two circular bone defects for histomorphometric analysis on one side and standard thread configuration implants for removal torque testing on the other side. Three different biofunctionalized modSLA surfaces using poly-L-lysine-graft-poly(ethylene glycol) (PLL-g-PEG) as a carrier minimizing nonspecific protein adsorption [(i) 20 pmol cm -2 KRSR alone (KRSR); or in combination with RGD in two different concentrations; (ii) 0.05 pmol cm -2 RGD (KRSR/RGD-1); (iii) 1.26 pmol cm -2 RGD (KRSR/RGD-2)] were compared with (iv) control modSLA. Animals were sacrificed at 2 weeks. Removal torque values (701.48-780.28 N mm), bone-to-implant contact (BIC) (35.22%-41.49%), and new bone fill (28.58%-30.62%) demonstrated no significant differences among treatments. It may be concluded that biofunctionalizing modSLA surfaces with KRSR and RGD derivatives of PLL-g-PEG polymer does not increase BIC, bone fill, or interfacial shear strength. Copyright © 2011 Wiley Periodicals, Inc. |
Persistent Identifier | http://hdl.handle.net/10722/236191 |
ISSN | 2023 Impact Factor: 3.9 2023 SCImago Journal Rankings: 0.807 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Broggini, Nina | - |
dc.contributor.author | Tosatti, Samuele | - |
dc.contributor.author | Ferguson, Stephen J. | - |
dc.contributor.author | Schuler, Martin | - |
dc.contributor.author | Textor, Marcus | - |
dc.contributor.author | Bornstein, Michael M. | - |
dc.contributor.author | Bosshardt, Dieter D. | - |
dc.contributor.author | Buser, Daniel | - |
dc.date.accessioned | 2016-11-11T07:43:11Z | - |
dc.date.available | 2016-11-11T07:43:11Z | - |
dc.date.issued | 2012 | - |
dc.identifier.citation | Journal of Biomedical Materials Research - Part A, 2012, v. 100 A, n. 3, p. 703-711 | - |
dc.identifier.issn | 1549-3296 | - |
dc.identifier.uri | http://hdl.handle.net/10722/236191 | - |
dc.description.abstract | Enhancing osseointegration through surface immobilization of multiple short peptide sequences that mimic extracellular matrix (ECM) proteins, such as arginine-glycine-aspartic acid (RGD) and lysine-arginine-serine-arginine (KRSR), has not yet been extensively explored. Additionally, the effect of biofunctionalizing chemically modified sandblasted and acid-etched surfaces (modSLA) is unknown. The present study evaluated modSLA implant surfaces modified with RGD and KRSR for potentially enhanced effects on bone apposition and interfacial shear strength during early stages of bone regeneration. Two sets of experimental implants were placed in the maxillae of eight miniature pigs, known for their rapid wound healing kinetics: bone chamber implants creating two circular bone defects for histomorphometric analysis on one side and standard thread configuration implants for removal torque testing on the other side. Three different biofunctionalized modSLA surfaces using poly-L-lysine-graft-poly(ethylene glycol) (PLL-g-PEG) as a carrier minimizing nonspecific protein adsorption [(i) 20 pmol cm -2 KRSR alone (KRSR); or in combination with RGD in two different concentrations; (ii) 0.05 pmol cm -2 RGD (KRSR/RGD-1); (iii) 1.26 pmol cm -2 RGD (KRSR/RGD-2)] were compared with (iv) control modSLA. Animals were sacrificed at 2 weeks. Removal torque values (701.48-780.28 N mm), bone-to-implant contact (BIC) (35.22%-41.49%), and new bone fill (28.58%-30.62%) demonstrated no significant differences among treatments. It may be concluded that biofunctionalizing modSLA surfaces with KRSR and RGD derivatives of PLL-g-PEG polymer does not increase BIC, bone fill, or interfacial shear strength. Copyright © 2011 Wiley Periodicals, Inc. | - |
dc.language | eng | - |
dc.relation.ispartof | Journal of Biomedical Materials Research - Part A | - |
dc.subject | removal torque value | - |
dc.subject | extracellular matrix protein binding sequences | - |
dc.subject | histomorphometry | - |
dc.subject | titanium surfaces biofunctionalized with biologically active peptides | - |
dc.subject | chemically modified sandblasted and acid-etched titanium implant surfaces | - |
dc.title | Evaluation of chemically modified SLA implants (modSLA) biofunctionalized with integrin (RGD)- and heparin (KRSR)-binding peptides | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1002/jbm.a.34004 | - |
dc.identifier.pmid | 22213622 | - |
dc.identifier.scopus | eid_2-s2.0-84856235129 | - |
dc.identifier.volume | 100 A | - |
dc.identifier.issue | 3 | - |
dc.identifier.spage | 703 | - |
dc.identifier.epage | 711 | - |
dc.identifier.eissn | 1552-4965 | - |
dc.identifier.isi | WOS:000299414400018 | - |
dc.identifier.issnl | 1549-3296 | - |