| Flagellar Display of Bone-Protein-Derived Peptides for Studying Peptide-Mediated Biomineralization. | |
| | |
MedLine Citation:
|
PMID: 23148645 Owner: NLM Status: Publisher |
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 |
Related Documents
:
|
9266275 - Sh3 domain-mediated interactions involving the phox components of the nadph oxidase. 16226275 - Structure of the hematopoietic tyrosine phosphatase (heptp) catalytic domain: structure... 15611135 - Crystal structure of the ptpl1/fap-1 human tyrosine phosphatase mutated in colorectal c... 15684325 - Structural basis for the function and regulation of the receptor protein tyrosine phosp... 23183105 - Importance of tap-independent processing pathways. 6415485 - The heavy chain of human b-cell alloantigen hla-ds has a variable n-terminal region and... |
Publication Detail:
|
Type: JOURNAL ARTICLE Date: 2012-11-14 |
Journal Detail:
|
Title: Langmuir : the ACS journal of surfaces and colloids Volume: - ISSN: 1520-5827 ISO Abbreviation: Langmuir Publication Date: 2012 Nov |
Date Detail:
|
Created Date: 2012-11-14 Completed Date: - Revised Date: - |
Medline Journal Info:
|
Nlm Unique ID: 9882736 Medline TA: Langmuir Country: - |
Other Details:
|
Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
|
Department of Chemistry & Biochemistry, Stephenson Life Sciences Research Center, University of Oklahoma , Norman, Oklahoma 73019, United States. |
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: On the Mechanisms of Triplet Excited State Population in 8-Azaadenine.
Next Document: Cutting and unzipping multi-walled carbon nanotubes into curved graphene nanoribbons and their enhan...