Strong Reversible Fe3+-mediated Bridging between Dopa-Containing Protein Films in Water
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SCOPUS
- Title
- Strong Reversible Fe3+-mediated Bridging between Dopa-Containing Protein Films in Water
- Authors
- Hongbo Zeng; Hwang, DS; Jacob N Israelachv; J. Herbert Waite
- Date Issued
- 2010-07-20
- Publisher
- the National Academy of Sciences
- Abstract
- Metal-containing polymer networks are widespread in biology, particularly for load-bearing exoskeletal biomaterials. Mytilus byssal cuticle is an especially interesting case containing moderate levels of Fe3+ and cuticle protein-mussel foot protein-1 (mfp-1), which has a peculiar combination of high hardness and high extensibility. Mfp-1, containing 13 mol % of dopa (3, 4-dihydroxyphenylalanine) side-chains, is highly positively charged polyelectrolyte (pI similar to 10) and didn't show any cohesive tendencies in previous surface forces apparatus (SFA) studies. Here, we show that Fe3+ ions can mediate unusually strong interactions between the positively charged proteins. Using an SFA, Fe3+ was observed to impart robust bridging (W-ad approximate to 4.3 mJ/m(2)) between two noninteracting mfp-1 films in aqueous buffer approaching the ionic strength of seawater. The Fe3+ bridging between the mfp-1-coated surfaces is fully reversible in water, increasing with contact time and iron concentration up to 10 mu M; at 100 mu M, Fe3+ bridging adhesion is abolished. Bridging is apparently due to the formation of multivalent dopa-iron complexes. Similar Fe-mediated bridging (W-ad approximate to 5.7 mJ/m(2)) by a smaller recombinant dopa-containing analogue indicates that bridging is largely independent of molecular weight and posttranslational modifications other than dopa. The results suggest that dopa-metal interactions may provide an energetic new paradigm for engineering strong, self-healing interactions between polymers under water.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/12756
- DOI
- 10.1073/PNAS.1007416107
- ISSN
- 0027-8424
- Article Type
- Article
- Citation
- PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, vol. 107, no. 29, page. 12850 - 12853, 2010-07-20
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