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Templated Biomineralization on Self-Assembled Protein Fibers

Proceedings of the National Academy of Sciences - PNAS, 2006-10, Vol.103 (40), p.14672-14677 [Peer Reviewed Journal]

Copyright 2006 The National Academy of Sciences of the United States of America ;Copyright National Academy of Sciences Oct 3, 2006 ;2006 by The National Academy of Sciences of the USA 2006 ;ISSN: 0027-8424 ;EISSN: 1091-6490 ;DOI: 10.1073/pnas.0602952103 ;PMID: 17003131

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Title:
Templated Biomineralization on Self-Assembled Protein Fibers
Author: Subburaman, K. ; Pernodet, N. ; Kwak, S. Y. ; DiMasi, E. ; Ge, S. ; Zaitsev, V. ; Ba, X. ; Yang, N. L. ; Rafailovich, M.
Subjects: Animals ; Biomineralogy ; Calcification, Physiologic - physiology ; Calcium ; Calcium Carbonate - metabolism ; Calcium carbonates ; Cattle ; Chemistry ; Crystallization ; Crystals ; Elasticity ; Elastin - chemistry ; Elastin - metabolism ; Elastin - ultrastructure ; Extracellular matrix ; Extracellular Matrix - metabolism ; Fibers ; Fibronectins - chemistry ; Fibronectins - metabolism ; Fibronectins - ultrastructure ; Mass Spectrometry ; Materials science ; Microscopy, Atomic Force ; Minerals ; Optical microscopy ; Physical Sciences ; Polymers ; Proteins ; Salts ; Shear Strength ; Spectrum analysis ; Time Factors
Is Part Of: Proceedings of the National Academy of Sciences - PNAS, 2006-10, Vol.103 (40), p.14672-14677
Description: Biological mineralization of tissues in living organisms relies on proteins that preferentially nucleate minerals and control their growth. This process is often referred to as "templating," but this term has become generic, denoting various proposed mineralorganic interactions including both chemical and structural affinities. Here, we present an approach using self-assembled networks of elastin and fibronectin fibers, similar to the extracellular matrix. When induced onto negatively charged sulfonated polystyrene surfaces, these proteins form fiber networks of ≈10-pm spacing, leaving open regions of disorganized protein between them. We introduce an atomic force microscopy-based technique to measure the elastic modulus of both structured and disorganized protein before and during calcium carbonate mineralization. Mineral-induced thickening and stiffening of the protein fibers during early stages of mineralization is clearly demonstrated, well before discrete mineral crystals are large enough to image by atomic force microscopy. Calcium carbonate stiffens the protein fibers selectively without affecting the regions between them, emphasizing interactions between the mineral and the organized protein fibers. Late-stage observations by optical microscopy and secondary ion mass spectroscopy reveal that Ca is concentrated along the protein fibers and that crystals form preferentially on the fiber crossings. We demonstrate that organized versus unstructured proteins can be assembled mere nanometers apart and probed in identical environments, where mineralization is proved to require the structural organization imposed by fibrillogenesis of the extracellular matrix.
Publisher: United States: National Academy of Sciences
Language: English
Identifier: ISSN: 0027-8424
EISSN: 1091-6490
DOI: 10.1073/pnas.0602952103
PMID: 17003131
Source: Geneva Foundation Free Medical Journals at publisher websites
MEDLINE
PubMed Central

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Templated Biomineralization on Self-Assembled Protein Fibers

Copyright 2006 The National Academy of Sciences of the United States of America ;Copyright National Academy of Sciences Oct 3, 2006 ;2006 by The National Academy of Sciences of the USA 2006 ;ISSN: 0027-8424 ;EISSN: 1091-6490 ;DOI: 10.1073/pnas.0602952103 ;PMID: 17003131

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