Skip to main content
Duke University Libraries
DukeSpace Scholarship by Duke Authors
  • Login
  • Ask
  • Menu
  • Login
  • Ask a Librarian
  • Search & Find
  • Using the Library
  • Research Support
  • Course Support
  • Libraries
  • About
View Item 
  •   DukeSpace
  • Theses and Dissertations
  • Duke Dissertations
  • View Item
  •   DukeSpace
  • Theses and Dissertations
  • Duke Dissertations
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Barnacle cement: a polymerization model based on evolutionary concepts.

Thumbnail
View / Download
26.6 Mb
Date
2009-11
Author
Dickinson, Gary H.
Advisors
Rittschof, Daniel
Forward, Richard
Barber, Richard
McClellan-Green, Patricia
Holm, Eric
Repository Usage Stats
683
views
607
downloads
Abstract
The tenacity by which barnacles adhere has sparked a long history of scientific investigation into their adhesive mechanisms. To adhere, barnacles utilize proteinaceous cement that rapidly polymerizes and forms adhesive bonds underwater, and is insoluble once polymerized. Although progress has been made towards understanding the chemical properties of cement proteins, the biochemical mechanisms of cement polymerization remain largely unknown. In this dissertation, I used evolutionary concepts to elucidate barnacle cement polymerization. Well-studied biological phenomena (blood coagulation in vertebrates and invertebrates) were used as models to generate hypotheses on proteins/biochemical mechanisms involved in cement polymerization. These model systems are under similar selective pressures to cement polymerization (life or death situations) and show similar chemical characteristics (soluble protein that quickly/efficiently coagulates). I describe a novel method for collection of unpolymerized cement. Multiple, independent techniques (AFM, FTIR, chemical staining for peroxidase and tandem mass spectroscopy) support the validity of the collection technique. Identification of a large number of proteins besides ‘barnacle cement proteins’ with mass spectrometry, andobservations of hemocytes in unpolymerized cement inspired the hypothesis that barnacle cement is hemolymph. A striking biochemical resemblance was shown between barnacle cement polymerization and vertebrate blood coagulation. Clotted fibrin and polymerized cement were shown to be structurally similar (mesh of fibrous protein) but biochemically distinct. Heparin, trypsin inhibitor and Ca2+ chelators impeded cement polymerization, suggesting trypsin and Ca2+ involvement in polymerization. The presence/activity of a cement trypsin-like serine protease was verified and shown homologous to bovine pancreatic trypsin. Protease activity may activate cement structural precursors, allowing loose assembly with other structural proteins and surface rearrangement. Tandem mass spectrometry and Western blotting revealed a homologous protein to human coagulation factor XIII (fibrin stabilizing factor: transglutaminase that covalently cross-links fibrin monomers). Transglutaminase activity was verified and may covalently cross-link assembled cement monomers. Similar to other protein coagulation systems, heritable defects occur during cement polymerization. High plasma protein concentration combined with sub-optimal enzyme, and/or cofactor concentrations and sub-optimal physical/muscular parameters (associated with hemolymph release) results in improperly cured cement in certain individuals when polymerization occurs in contact with low surface energy silicone and its associated leached molecules.
Type
Dissertation
Department
Ecology
Subject
Amino Acid Sequence
Animals
Biological Evolution
Calcium
Cattle
Humans
Microscopy, Atomic Force
Models, Biological
Molecular Sequence Data
Polymers
Proteins
Tandem Mass Spectrometry
Thoracica
Transglutaminases
Trypsin
Permalink
https://hdl.handle.net/10161/653
Citation
Dickinson, Gary H. (2009). Barnacle cement: a polymerization model based on evolutionary concepts. Dissertation, Duke University. Retrieved from https://hdl.handle.net/10161/653.
Collections
  • Duke Dissertations
More Info
Show full item record
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 United States License.

Rights for Collection: Duke Dissertations


Works are deposited here by their authors, and represent their research and opinions, not that of Duke University. Some materials and descriptions may include offensive content. More info

Make Your Work Available Here

How to Deposit

Browse

All of DukeSpaceCommunities & CollectionsAuthorsTitlesTypesBy Issue DateDepartmentsAffiliations of Duke Author(s)SubjectsBy Submit DateThis CollectionAuthorsTitlesTypesBy Issue DateDepartmentsAffiliations of Duke Author(s)SubjectsBy Submit Date

My Account

LoginRegister

Statistics

View Usage Statistics
Duke University Libraries

Contact Us

411 Chapel Drive
Durham, NC 27708
(919) 660-5870
Perkins Library Service Desk

Digital Repositories at Duke

  • Report a problem with the repositories
  • About digital repositories at Duke
  • Accessibility Policy
  • Deaccession and DMCA Takedown Policy

TwitterFacebookYouTubeFlickrInstagramBlogs

Sign Up for Our Newsletter
  • Re-use & Attribution / Privacy
  • Harmful Language Statement
  • Support the Libraries
Duke University