Document Detail


Tunable delivery of bioactive peptides from HA biomaterials and allograft bone using variable length polyglutamate domains.
MedLine Citation:
PMID:  23625466     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Hydroxyapatite (HA) biomaterials and allograft bone are common alternatives to autogenous grafts, however these materials lack the strong osteoinductive potential of autologous bone. Previous studies have established that polyglutamate domains, which bind selectively to HA, can be engineered onto bioactive peptides as a mechanism for coupling osteoinductive signals onto HA and allograft. In the current investigation, we adapted the polyglutamate approach to tailor delivery of a model collagen-derived peptide, DGEA, by manipulating the number of glutamates in the HA binding domain. Specifically, DGEA was modified with diglutamate (E2-DGEA), tetraglutamate (E4-DGEA) or heptaglutamate (E7-DGEA), and it was found that initial peptide binding to HA and allograft was significantly enhanced as the number of glutamates increased. We also determined that the rate of release of polyglutamate-DGEA from substrates over a 5-day interval increased proportionally as the number of glutamate residues was decreased. Additionally, we tuned the peptide release rate by creating mixtures of E2-DGEA, E4-DGEA and E7-DGEA, and observed that release kinetics of the mixtures were distinct from pure solutions of each respective peptide. These collective results suggest that variable length polyglutamate domains provide an effective mechanism for controlled delivery of osteoregenerative peptides on HA-containing bone graft materials.
Authors:
Bonnie K Culpepper; William M Webb; Paul P Bonvallet; Susan L Bellis
Related Documents :
23485856 - Coiled-coil-mediated grafting of bioactive vascular endothelial growth factor.
2895646 - Dynorphin a (1-13) peptide nh groups are solvent exposed: ft-ir and 500 mhz 1h nmr spec...
23657596 - Exploring the dermal "template effect" and its structure.
2177176 - Conantokin-g: a novel peptide antagonist to the n-methyl-d-aspartic acid (nmda) receptor.
20091676 - Synthesis by native chemical ligation and crystal structure of human ccl2.
8015966 - Purification and characterization of aplysia atrial gland secretory granules containing...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-4-27
Journal Detail:
Title:  Journal of biomedical materials research. Part A     Volume:  -     ISSN:  1552-4965     ISO Abbreviation:  J Biomed Mater Res A     Publication Date:  2013 Apr 
Date Detail:
Created Date:  2013-4-29     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101234237     Medline TA:  J Biomed Mater Res A     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2013 Wiley Periodicals, Inc., A Wiley Company.
Affiliation:
Department of Biomedical Engineering, University of Alabama at Birmingham.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  The entotympanic in late fetal artiodactyla (Mammalia).
Next Document:  The schizoaffective disorder diagnosis: a conundrum in the clinical setting.