Document Detail


Flagellar display of bone-protein-derived peptides for studying peptide-mediated biomineralization.
MedLine Citation:
PMID:  23148645     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A bacterial flagellum is self-assembled primarily from thousands of flagellin (FliC), a protein subunit. A foreign peptide can be fully displayed on the surface of the flagellum through inserting it into every constituent protein subunit. To shed light on the role of bone proteins during the nucleation of hydroxyapatite (HAP), representative domains from type I collagen, including part of the N-,C-terminal, N-,C-zone around the hole zone and an eight repeat unit Gly-Pro-Pro (GPP8) sequence similar to the central sequence of type I collagen, were separately displayed on the surface of the flagella. Moreover, eight negatively charged, contiguous glutamic acid residues (E8) and two other characteristic sequences derived from a representative noncollagenous protein called bone sialoprotein (BSP) were also displayed on flagella. After being incubated in an HAP supersaturated precursor solution, flagella displaying E8 or GPP8 sequences were found to be coated with a layer of HAP nanocrystals. Very weak or no nucleation was observed on flagella displaying other peptides being tested. We also found that calcium ions can induce the assembly of the negatively charged E8 flagella into bundles mimicking collagen fibers, followed by the formation of HAP nanocrystals with the crystallographic c axis preferentially aligned with long axis of flagella, which is similar to that along the collagen fibrils in bone. This work demonstrates that because of the ease of the peptide display on flagella and the self-assembly of flagella, flagella can serve as a platform for studying biomineralization and as a building block to generate bonelike biomaterials.
Authors:
Dong Li; Salete M C Newton; Philip E Klebba; Chuanbin Mao
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-11-14
Journal Detail:
Title:  Langmuir : the ACS journal of surfaces and colloids     Volume:  28     ISSN:  1520-5827     ISO Abbreviation:  Langmuir     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-27     Completed Date:  2013-07-23     Revised Date:  2013-12-04    
Medline Journal Info:
Nlm Unique ID:  9882736     Medline TA:  Langmuir     Country:  United States    
Other Details:
Languages:  eng     Pagination:  16338-46     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Bioengineering
Biomimetics
Bone and Bones / metabolism*
Calcification, Physiologic*
Calcium / metabolism
Durapatite / metabolism*
Flagella / metabolism*
Peptide Fragments / metabolism*
Peptide Library*
Tissue Engineering
Grant Support
ID/Acronym/Agency:
1R21EB015190-01A1/EB/NIBIB NIH HHS; 4R03AR056848-03/AR/NIAMS NIH HHS; 5R01DE01563309/DE/NIDCR NIH HHS; 5R01HL092526-02/HL/NHLBI NIH HHS; 5R21EB009909-02/EB/NIBIB NIH HHS; R01 HL092526/HL/NHLBI NIH HHS; R03 AR056848/AR/NIAMS NIH HHS; R21 EB009909/EB/NIBIB NIH HHS; R21 EB015190/EB/NIBIB NIH HHS
Chemical
Reg. No./Substance:
0/Peptide Fragments; 0/Peptide Library; 91D9GV0Z28/Durapatite; SY7Q814VUP/Calcium
Comments/Corrections

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