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Diatom Adhesive Mucilage Contains Distinct Supramolecular Assemblies of a Single Modular Protein

T. M. Dugdale ^*, R. Dagastine , A. Chiovitti ^* and R. Wetherbee ^*

^* School of Botany, and School of Chemical and Biomolecular Engineering, University of Melbourne, Victoria, Australia

Correspondence: Address reprint requests to Dr. R. Wetherbee, School of Botany, University of Melbourne, Parkville, VIC 3010, Australia. E-mail: richardw{at}unimelb.edu.au.

A previous study used atomic force microscopy saw-tooth retraction curves to characterize the adhesive mucilage pads of the diatom Toxarium undulatum. The major mucilage component consisted of adhesive nanofibers (ANFs) made up of modular proteins arranged into cohesive units, each containing a set number of modular proteins aligned in parallel. This study shows that T. undulatum adhesive mucilage is a biocomposite containing four additional adhesive components, including single modular proteins that are likely to be the structural units from which the ANFs are assembled. Two further distinct supramolecular assemblies were observed to coexist with ANFs (ANFs II and III), along with a continuum of single modular proteins through oligomers made up of varying numbers of modular proteins arranged in parallel. All components of the adhesive biocomposite produce a characteristic force spectrum with the same interpeak distance (35.3 ± 0.3 (mean ± SE) nm), suggesting they are derived from discrete supramolecular assemblies of the same modular protein, but they are distinguishable from one another based on the rupture force, persistence length, and interpeak force measured from their saw-tooth curves.

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