Templated biomineralization on self-assembled protein fibers.

Content Provider	Semantic Scholar
Author	Subburaman, K. Pernodet, Nadine Kwak, Seo Young Dimasi, Elaine Ge, Shaoyu Zaitsev, Vladimir Ba, Xiaolan Yang, Nancy Rafailovich, Miriam
Copyright Year	2006
Abstract	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 mineral-organic 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 approximately 10-mum 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.
Starting Page	5
Ending Page	12
Page Count	8
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.pnas.org/content/103/40/14672.full.pdf
PubMed reference number	17003131v1
Volume Number	103
Issue Number	40
Journal	Proceedings of the National Academy of Sciences of the United States of America
Language	English
Access Restriction	Open
Subject Keyword	Alkanesulfonates Body tissue Calcium Carbonate 800 MG / Famotidine 10 MG / Magnesium Hydroxide 165 MG Chewable Tablet Charge (electrical) Concentrate Dosage Form Departure - action Elastic Modulus Extracellular Matrix Generic Drugs Intrinsically Disordered Proteins Ions Mass Spectrometry Microscopy, Atomic Force Minerals Morphogenesis Organism Physiologic calcification Polystyrenes Spectrometry, Mass, Secondary Ion Tissue fiber
Content Type	Text
Resource Type	Article