Document Detail

Modulating protein adsorption onto hydroxyapatite particles using different amino acid treatments.
MedLine Citation:
PMID:  21957116     Owner:  NLM     Status:  MEDLINE    
Hydroxyapatite (HA) is a material of choice for bone grafts owing to its chemical and structural similarities to the mineral phase of hard tissues. The combination of osteogenic proteins with HA materials that carry and deliver the proteins to the bone-defective areas will accelerate bone regeneration. The study investigated the treatment of HA particles with different amino acids such as serine (Ser), asparagine (Asn), aspartic acid (Asp) and arginine (Arg) to enhance the adsorption ability of HA carrier for delivering therapeutic proteins to the body. The crystallinity of HA reduced when amino acids were added during HA preparation. Depending on the types of amino acid, the specific surface area of the amino acid-functionalized HA particles varied from 105 to 149 m(2) g(-1). Bovine serum albumin (BSA) and lysozyme were used as model proteins for adsorption study. The protein adsorption onto the surface of amino acid-functionalized HA depended on the polarities of HA particles, whereby, compared with lysozyme, BSA demonstrated higher affinity towards positively charged Arg-HA. Alternatively, the binding affinity of lysozyme onto the negatively charged Asp-HA was higher when compared with BSA. The BSA and lysozyme adsorptions onto the amino acid-functionalized HA fitted better into the Freundlich than Langmuir model. The amino acid-functionalized HA particles that had higher protein adsorption demonstrated a lower protein-release rate.
Wing-Hin Lee; Ching-Yee Loo; Kim Linh Van; Alexander V Zavgorodniy; Ramin Rohanizadeh
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2011-09-28
Journal Detail:
Title:  Journal of the Royal Society, Interface / the Royal Society     Volume:  9     ISSN:  1742-5662     ISO Abbreviation:  J R Soc Interface     Publication Date:  2012 May 
Date Detail:
Created Date:  2012-03-23     Completed Date:  2012-07-26     Revised Date:  2013-06-27    
Medline Journal Info:
Nlm Unique ID:  101217269     Medline TA:  J R Soc Interface     Country:  England    
Other Details:
Languages:  eng     Pagination:  918-27     Citation Subset:  IM    
Advanced Drug Delivery Group, Faculty of Pharmacy, University of Sydney, Sydney, New South Wales 2006, Australia.
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MeSH Terms
Amino Acids / chemistry*
Durapatite / chemistry*
Microscopy, Electron, Scanning
Proteins / chemistry*
Serum Albumin, Bovine / chemistry
Reg. No./Substance:
0/Amino Acids; 0/Proteins; 0/Serum Albumin, Bovine; 1306-06-5/Durapatite

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

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