Coil dimensions of the mussel adhesive protein Mefp-1

Haemers, Sander; Leeden, M.C. van der; Frens, G.

doi:10.1016/j.biomaterials.2004.04.032

Cited by 32 publications

(30 citation statements)

References 34 publications

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“…[11][12][13][14]30 CD analysis of a shortened recombinant mfp-1 analog suggested a random-coil shape, 11 whereas 2D-NMR and dynamics simulation of a mfp-1 decapeptide consensus sequence suggested a kinked left-handed polyproline II helix. 12,14 Collagen-like peptides such as [Gly-Pro-Pro] n generally exhibit polyproline II helix-like CD spectra when properly folded in a collagen triple helix.…”

Section: Discussionmentioning

confidence: 99%

Three intrinsically unstructured mussel adhesive proteins, mfp‐1, mfp‐2, and mfp‐3: Analysis by circular dichroism

Hwang

Waite

2012

Protein Science

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Mussel foot proteins (mfps) mediate fouling by the byssal holdfast and have been extensively investigated as models for versatile polymer-mediated underwater adhesion and coatings. However, insights into the structural properties of mfps have lagged far behind the nanomechanical advances, owing in part to the inability of these proteins to crystallize as well as their limited solubility. Here, solution secondary structures of mfp-1, mfp-2, and mfp-3, localized in the mussel byssal cuticle, adhesive plaque, and plaque-substratum interface, respectively, were investigated using circular dichroism. All three have significant extended coil solution structure, but two, mfp-1 and mfp-2, appear to have punctuated regions of structure separated by unstructured domains. Apart from its punctuated distribution, the structure in mfp-1 resembles other structural proteins such as collagen and plant cell-wall proteins with prominent polyproline II helical structure. As in collagen, PP II structure of mfp-1 is incrementally disrupted by increasing the temperature and by raising pH. However, no recognizable change in mfp-1's PP II structure was evident with the addition with Ca 21 and Fe 31 . In contrast, mfp-2 exhibits Ca 21 -and disulfidestabilized epidermal growth factor-like domains separated by unstructured sequence. Mfp-2 showed calcium-binding ability. Bound calcium in mfp-2 was not removed by chelation at pH 5.5, but it was released upon reduction of disulfide bonds. Mfp-3, in contrast, appears to consist largely of unstructured extended coils.

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Section: Discussionmentioning

confidence: 99%

Three intrinsically unstructured mussel adhesive proteins, mfp‐1, mfp‐2, and mfp‐3: Analysis by circular dichroism

Hwang

Waite

2012

Protein Science

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“…These results indicate that bridging involves dopa but may be independent of prolyldirected posttranslational modifications and molecular weight. The thicker hard wall, however, suggests that some rmfp-1 may be aggregating to higher molecular weights during the introduction of dopa (18).…”

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confidence: 99%

“…Although it is reasonable to conclude that mfp-1 mimics need neither the non-dopa modifications nor the high mass in order to bridge with iron, mfp-1 is known to undergo measurable aggregation at pH 5 linked to spontaneous dopa oxidation (18). The extent to which aggregates are preferentially adsorbed to mica over the nonaggregated monomers needs to be further investigated.…”

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confidence: 99%

Strong reversible Fe ³⁺ -mediated bridging between dopa-containing protein films in water

Zeng

Hwang

Israelachvili³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

460

391

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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 Fe 3þ 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 ∼ 10) and didn't show any cohesive tendencies in previous surface forces apparatus (SFA) studies. Here, we show that Fe 3þ ions can mediate unusually strong interactions between the positively charged proteins. Using an SFA, Fe 3þ was observed to impart robust bridging (W ad ≈ 4.3 mJ∕m 2 ) between two noninteracting mfp-1 films in aqueous buffer approaching the ionic strength of seawater. The Fe 3þ bridging between the mfp-1-coated surfaces is fully reversible in water, increasing with contact time and iron concentration up to 10 μM; at 100 μM, Fe 3þ bridging adhesion is abolished. Bridging is apparently due to the formation of multivalent dopa-iron complexes. Similar Fe-mediated bridging (W ad ≈ 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.byssus | metal coordination | tris-catecholato-iron (III) complex M etallopolymers are increasingly viewed as a transformative platform for the next generation of materials. This platform is related in part to their capacity for multifunctionality, but also to their wide and adjustable range of electronic, photonic, and magnetic properties (1). The load-bearing properties of metallopolymers are equally important but have received less attention with few exceptions (2). This oversight needs to be rectified given how widespread metal-containing polymer networks are in biology, particularly for load-bearing exoskeletal biomaterials (3, 4). The byssal cuticle of mussels in the genus Mytilus is an especially interesting case study because of its peculiar combination of hardness (100-150 MPa) and extensibility (>70% strain) (5). Mytilus byssal cuticle contains moderate levels of Fe 3þ and a single protein-mussel foot protein-1 (mfp-1) (6). Mfp-1 has a mass of about 108 kDa in Mytilus edulis (7) and consists largely of tan-

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“…Mfp-1 contains 20.8 mol% basic amino acid and has a pI of 8.3-10.3, which has 28.6 mol% hydrophobic amino acid, including approximately 19.2 mol% DOPA. Mcfp-1 is the most rigid protein among all the mfps tested based on the B-factor and is composed of tandem repeats of stiff decapeptide units [13,36].…”

Section: Properties Of Mfps and Substrate Surfacesmentioning

confidence: 99%

Adhesion of mussel foot proteins to different substrate surfaces

Danner

Waite

et al. 2013

J. R. Soc. Interface.

281

243

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Mussel foot proteins (mfps) have been investigated as a source of inspiration for the design of underwater coatings and adhesives. Recent analysis of various mfps by a surface forces apparatus (SFA) revealed that mfp-1 functions as a coating, whereas mfp-3 and mfp-5 resemble adhesive primers on mica surfaces. To further refine and elaborate the surface properties of mfps, the force-distance profiles of the interactions between thin mfp (i.e. mfp-1, mfp-3 or mfp-5) films and four different surface chemistries, namely mica, silicon dioxide, polymethylmethacrylate and polystyrene, were measured by an SFA. The results indicate that the adhesion was exquisitely dependent on the mfp tested, the substrate surface chemistry and the contact time. Such studies are essential for understanding the adhesive versatility of mfps and related/similar adhesion proteins, and for translating this versatility into a new generation of coatings and (including in vivo) adhesive materials.

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Coil dimensions of the mussel adhesive protein Mefp-1

Cited by 32 publications

References 34 publications

Three intrinsically unstructured mussel adhesive proteins, mfp‐1, mfp‐2, and mfp‐3: Analysis by circular dichroism

Three intrinsically unstructured mussel adhesive proteins, mfp‐1, mfp‐2, and mfp‐3: Analysis by circular dichroism

Strong reversible Fe ³⁺ -mediated bridging between dopa-containing protein films in water

Adhesion of mussel foot proteins to different substrate surfaces

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Coil dimensions of the mussel adhesive protein Mefp-1

Cited by 32 publications

References 34 publications

Three intrinsically unstructured mussel adhesive proteins, mfp‐1, mfp‐2, and mfp‐3: Analysis by circular dichroism

Three intrinsically unstructured mussel adhesive proteins, mfp‐1, mfp‐2, and mfp‐3: Analysis by circular dichroism

Strong reversible Fe 3+ -mediated bridging between dopa-containing protein films in water

Adhesion of mussel foot proteins to different substrate surfaces

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Strong reversible Fe ³⁺ -mediated bridging between dopa-containing protein films in water