JDR JDR Most Cited Articles
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Abstract Freely available
Right arrow Full Text
Right arrow Full Text (PDF)
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Google Scholar
Right arrow Articles by Holten-Andersen, N.
Right arrow Articles by Waite, J. H.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Holten-Andersen, N.
Right arrow Articles by Waite, J. H.

Mussel-designed Protective Coatings for Compliant Substrates

N. Holten-Andersen1, and J. H. Waite2,*

1 Graduate Program in BioMolecular Science & Engineering,
2 Marine Science Institute, University of California at Santa Barbara, Santa Barbara, CA 93106, USA


Figure 1
View larger version (65K):
[in this window]
[in a new window]

 
Figure 1. A mussel attached by a byssus to glass (A) and a cartoon of the same mussel on the half-shell (B), showing the relationship of the foot, stem, threads, and attachment plaque.

 

Figure 2
View larger version (56K):
[in this window]
[in a new window]

 
Figure 2. Microstructure of mussel byssal cuticle. (a) SEM of M. galloprovincialis distal thread with partial delamination of cuticle, exposing the underlying collagenous core. (b) TEM of transverse cross-section of M. galloprovincialis distal thread cuticle, illustrating its granular composite morphology as well as the interior granular structure, osmium-tetroxide-stained for contrast. (c) AFM of untreated transverse cross-section of cuticle of M. galloprovincialis distal thread, confirming the observations made in TEM.

 

Figure 3
View larger version (27K):
[in this window]
[in a new window]

 
Figure 3. Mytilus edulis foot protein (mefp-1) and the other mfp-1s are all highly repetitive proteins. The consensus repeat sequence in mefp-1 is a decapeptide. Lys-2, Tyr-5, Pro-6, Tyr-9, and Lys-10 are highly conserved. Residues Pro-6, Pro-7, and Tyr-9 are completely post-translationally hydroxylated. Conversion of Pro-3, Tyr-5 (gray), in contrast, is < 30%. Mefp-1 contains a non-repetitive N-terminus, followed by mostly decapeptide and some hexapeptide sequences.

 

Figure 4
View larger version (14K):
[in this window]
[in a new window]

 
Figure 4. Dopa side-chains of mfp-1 are susceptible to oxidation. A two-electron oxidation produces dopaquinone, which is able produce 2 semi-quinones by reverse dismutation with unreacted dopa. The Dopa semi-quinones can couple to produce di-dopa cross-links.

 

Figure 5
View larger version (16K):
[in this window]
[in a new window]

 
Figure 5. Dopa side-chains in mfp-1s coordinate both soluble and insoluble metal oxides. Lee et al. (2006) have shown that the coordinate chelate bond between Dopa and a TiO2 surface has half the interaction energy of a covalent bond, but re-forms spontaneously following breakage.

 

Figure 6
View larger version (12K):
[in this window]
[in a new window]

 
Figure 6. Comparison of the behavior of mefp-1 and mefp-3 following introduction between 2 mica surfaces, as measured by the surface forces apparatus (Lin et al., 2007). Like a good adhesive, mefp-3 both coats and bridges the 2 mica surfaces; mefp-1, in contrast, only coats each surface.

 





HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
IADR Journals Advances in Dental Research ®
Journal of Dental Research ® Critical Reviews (1990-2004)
Copyright © 2008 Institutional Access Guidelines