Single Adhesive Nanofibers from a Live Diatom Have the Signature Fingerprint of Modular Proteins

The adhesive and mechanical properties of a cell-substratum adhesive secreted by live diatom cells were examined in situ using atomic force microscopy. The resulting force curves have a regular saw-tooth pattern, the characteristic fingerprint of modular proteins, and when bridged between tip and su...

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Bibliographic Details
Published inBiophysical journal Vol. 89; no. 6; pp. 4252 - 4260
Main Authors Dugdale, T.M., Dagastine, R., Chiovitti, A., Mulvaney, P., Wetherbee, R.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.12.2005
Biophysical Society
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Summary:The adhesive and mechanical properties of a cell-substratum adhesive secreted by live diatom cells were examined in situ using atomic force microscopy. The resulting force curves have a regular saw-tooth pattern, the characteristic fingerprint of modular proteins, and when bridged between tip and surface can repeatedly be stretched and relaxed resulting in precisely overlaying saw-tooth curves (up to ∼600 successive cycles). The average rupture force of the peaks is 0.794 ± 0.007 (mean ± SE) nN at a loading rate of 0.8 μm/s and the average persistence length is 0.026 ± <0.001 (mean ± SE) nm (fit using the worm-like chain model). We propose that we are pulling on single adhesive nanofibers, each a cohesive unit composed of a set number of modular proteins aligned in register. Furthermore, we can observe and differentiate when up to three adhesive nanofibers are pulled based upon multimodal distributions of force and persistence length. The high force required for bond rupture, high extensibility (∼1.2 μm), and the accurate and rapid refolding upon relaxation, together provide strong and flexible properties ideally suited for the cell-substratum adhesion of this fouling diatom and allow us to understand the mechanism responsible for the strength of adhesion.
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Address reprint requests to Dr. R. Wetherbee, School of Botany, University of Melbourne, Parkville, VIC 3010, Australia. E-mail: richardw@unimelb.edu.au.
ISSN:0006-3495
1542-0086
DOI:10.1529/biophysj.105.062489