Interaction of adsorbed polymers with supported cationic bilayers

Das, Saurabh; Donaldson, Stephen H.; Kaufman, Yair; Israelachvili, Jacob N.

doi:10.1039/c3ra43500h

Cited by 12 publications

(17 citation statements)

References 36 publications

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“…4b), which show that COL1A1 (width of ~ 1.5 nm), dispersed and intercalated within the mfp-3f films. Similarly, the more hydrophobic variant, mfp-3s, showed a cohesive force ( W c = 5.4 ± 0.2 mJ/m 2 ) for t c ~ 2 min, and COL1A1 increased the bridging interactions [16] between the two films ( W c = 7.2± 0.6 mJ/m 2 ) (Fig. S4).…”

Section: Resultsmentioning

confidence: 93%

Mussel adhesive protein provides cohesive matrix for collagen type-1α

et al. 2015

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Understanding the interactions between collagen and adhesive mussel foot proteins (mfps) can lead to improved medical and dental adhesives, particularly for collagen-rich tissues. Here we investigated interactions between collagen type-1, the most abundant loadbearing animal protein, and mussel foot protein-3 (mfp-3) using a quartz crystal microbalance and surface forces apparatus (SFA). Both hydrophilic and hydrophobic variants of mfp-3 were exploited to probe the nature of the interaction between the protein and collagen. Our chief findings are: 1) mfp-3 is an effective chaperone for tropocollagen adsorption to TiO2 and mica surfaces; 2) at pH 3, collagen addition between two mfp-3 films (Wc = 5.4 ± 0.2 mJ/m2) increased their cohesion by nearly 35%; 3) oxidation of Dopa in mfp-3 by periodate did not abolish the adhesion between collagen and mfp-3 films, and 4) collagen bridging between both hydrophilic and hydrophobic mfp-3 variant films is equally robust, suggesting that hydrophobic interactions play a minor role. Extensive H-bonding, π-cation and electrostatic interactions are more plausible to explain the reversible bridging of mfp-3 films by collagen.

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Section: Resultsmentioning

confidence: 93%

Mussel adhesive protein provides cohesive matrix for collagen type-1α

et al. 2015

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“…Dopa-modified Pro-pep dimer showed cohesion energy similar to the unmodified dimer. The forces measured between unmodified mfp-1 Pro-pep dimer films on approach were purely repulsive due to steric and hydration forces [28] (Fig. 4 A ).…”

Section: Resultsmentioning

confidence: 99%

Peptide Length and Dopa Determine Iron‐Mediated Cohesion of Mussel Foot Proteins

Das

Rodriguez

Wei

et al. 2015

Adv Funct Materials

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Mussel adhesion to mineral surfaces is widely attributed to 3,4-dihydroxyphenylalanine (Dopa) functionalities in the mussel foot proteins (mfps). Several mfps, however, show a broad range (30–100%) of Tyrosine (Tyr) to Dopa conversion suggesting that Dopa is not the only desirable outcome for adhesion. Here, we used a partial recombinant construct of mussel foot protein-1 (rmfp-1) and short decapeptide dimers with and without Dopa and assessed both their cohesive and adhesive properties on mica using a surface forces apparatus (SFA). Our results demonstrate that at low pH, both the unmodified and Dopa-containing rmfp-1s show similar energies for adhesion to mica and self-self interaction. Cohesion between two Dopa-containing rmfp-1 surfaces can be doubled by Fe3+ chelation, but remains unchanged with unmodified rmfp-1. At the same low pH, the Dopa modified short decapeptide dimer did not show any change in cohesive interactions even with Fe3+. Our results suggest that the most probable intermolecular interactions are those arising from electrostatic (i.e., cation-π) and hydrophobic interactions. We also show that Dopa in a peptide sequence does not by itself mediate Fe3+ bridging interactions between peptide films: peptide length is a crucial enabling factor.

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“…At C fp1 = 100 μg/mL, cohesion decreased significantly to W c = 0.18 ± 0.04 mJ/m 2 (Figure 2). The surfaces exhibited poor bridging cohesion 32 at C fp1 = 25 and 100 μg/mL compared with mfp-1 ( Mc ) bridging at C fp1 ~ 50 μg/mL (Figure 1). …”

Section: Resultsmentioning

confidence: 99%

“…32,33 Mfp-1 ( Mc ) films were made by adsorbing 50 μL of the protein from a C fp1 = 10–100 μg/mL in a buffer solution (0.1 M sodium acetate buffer, pH 5.5, 0.25 M KNO 3 , and 1 mM bis–tris) onto the mica surfaces for 30 min, then rinsing the excess protein with the same buffer. During the protein adsorption, the discs were kept in a saturated Petri dish to minimize evaporation of the water from the surfaces.…”

Section: Methodsmentioning

confidence: 99%

Tough Coating Proteins: Subtle Sequence Variation Modulates Cohesion

Das¹,

Miller²,

Kaufman³

et al. 2015

Biomacromolecules

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Mussel foot protein-1 (mfp-1) is an essential constituent of the protective cuticle covering all exposed portions of the byssus (plaque and the thread) that marine mussels use to attach to intertidal rocks. The reversible complexation of Fe3+ by the 3,4-dihydroxyphenylalanine (Dopa) side chains in mfp-1 in Mytilus californianus cuticle is responsible for its high extensibility (120%) as well as its stiffness (2 GPa) due to the formation of sacrificial bonds that help to dissipate energy and avoid accumulation of stresses in the material. We have investigated the interactions between Fe3+ and mfp-1 from two mussel species, M. californianus (Mc) and M. edulis (Me), using both surface sensitive and solution phase techniques. Our results show that although mfp-1 homologues from both species bind Fe3+, mfp-1 (Mc) contains Dopa with two distinct Fe3+-binding tendencies and prefers to form intramolecular complexes with Fe3+. In contrast, mfp-1 (Me) is better adapted to intermolecular Fe3+ binding by Dopa. Addition of Fe3+ did not significantly increase the cohesion energy between the mfp-1 (Mc) films at pH 5.5. However, iron appears to stabilize the cohesive bridging of mfp-1 (Mc) films at the physiologically relevant pH of 7.5, where most other mfps lose their ability to adhere reversibly. Understanding the molecular mechanisms underpinning the capacity of M. californianus cuticle to withstand twice the strain of M. edulis cuticle is important for engineering of tunable strain tolerant composite coatings for biomedical applications.

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Interaction of adsorbed polymers with supported cationic bilayers

Cited by 12 publications

References 36 publications

Mussel adhesive protein provides cohesive matrix for collagen type-1α

Mussel adhesive protein provides cohesive matrix for collagen type-1α

Peptide Length and Dopa Determine Iron‐Mediated Cohesion of Mussel Foot Proteins

Tough Coating Proteins: Subtle Sequence Variation Modulates Cohesion

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