Unknown

Dataset Information

0

Mussel adhesive protein provides cohesive matrix for collagen type-1?.


ABSTRACT: 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 load-bearing 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/m(2)) 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, ?-cation and electrostatic interactions are more plausible to explain the reversible bridging of mfp-3 films by collagen.

SUBMITTER: Martinez Rodriguez NR 

PROVIDER: S-EPMC4361793 | BioStudies | 2015-01-01

REPOSITORIES: biostudies

Similar Datasets

1000-01-01 | S-EPMC3785749 | BioStudies
2012-01-01 | S-EPMC3482130 | BioStudies
1000-01-01 | S-EPMC2919964 | BioStudies
2015-01-01 | S-EPMC4514026 | BioStudies
2015-01-01 | S-EPMC5488267 | BioStudies
2010-01-01 | S-EPMC3098815 | BioStudies
2020-01-01 | S-EPMC7644685 | BioStudies
2016-01-01 | S-EPMC4934423 | BioStudies
2012-01-01 | S-EPMC3527705 | BioStudies
1000-01-01 | S-EPMC4310636 | BioStudies