Rapid Gel Formation and Adhesion in Photocurable and Biodegradable Block Copolymers with High DOPA Content

Lee, Bruce P.; Chao, Chi-Yang; Nunalee, F. Nelson; Motan, Emre; Shull, Kenneth R.; Messersmith, Phillip B.

doi:10.1021/ma0518959

Cited by 193 publications

(177 citation statements)

References 59 publications

Supporting

Mentioning

173

Contrasting

Unclassified

Order By: Relevance

“…mcfp-5 and -6 are phosphoryl- ated though apparently less so than mefp-5 (13) and Pc-3, a cement protein in the sandcastle worm (14). Phosphorylation imparts a potential for both cohesive (by Ca ϩ2 bridging) and adsorptive contributions to the glue (14,23).…”

Section: Discussionmentioning

confidence: 99%

Linking Adhesive and Structural Proteins in the Attachment Plaque of Mytilus californianus

Zhao

Waite

2006

Journal of Biological Chemistry

258

243

View full text Add to dashboard Cite

The byssal attachment of California mussels Mytilus californianus provides secure adhesion in the presence of moisture, a feat that still eludes most synthetic polymers. Matrix-assisted laser desorption ionization mass spectrometry was used to probe the footprints of byssal attachment plaques on glass cover slips for adhesive proteins. Besides the abundant mcfp-3 protein family (Zhao, H., Robertson, N. B., Jewhurst, S. A., and Waite, J. H. (2006) J. Biol. Chem. 281, 11090 -11096), two new proteins, mcfp-5 and mcfp-6, with masses of 8.9 kDa and 11.6 kDa, respectively, were identified in footprints, partially characterized and completely sequenced from a cDNA library. mcfp-5 resembles mcfp-3 in its basic pI and abundant 3,4-dihydroxyphenyl-L-alanine (Dopa; 30 mol %), but is distinct in two respects: it is more homogeneous in primary sequence and is polyphosphorylated. mcfp-6 is basic and contains a small amount of Dopa (<5 mol %). In contrast to mcfp-3 and -5, tyrosine prevails at 20 mol %, and cysteine is present at 11 mol %, one-third of which remains thiolate. Given the oxidative instability of Dopa and cysteine at pH 8.2 (seawater), we tested the hypothesis that thiols serve to scavenge dopaquinones by adduct formation. Plaque footprints were hydrolyzed and screened for cysteine dopaquinone adducts using phenylboronate affinity chromatography. 5-S-Cysteinyldopa was detected at nearly 1 mol %. The results suggest that mcfp-6 may provide a cohesive link between the surface-coupling Dopa-rich proteins and the bulk of the plaque proteins.Mussels inhabit wind and wave swept rocky seashores. Such habitats are deathtraps for exposed organisms lacking a secure attachment. Accordingly, mussels have evolved a robust holdfast known as the byssus, which is essentially a specialized 4 -5-cm long bundle of collagenous fibers that is proximally rooted in the mussel and distally bonded to foreign surfaces underwater by flattened attachment plaques (1).Given that engineering durable adhesive bonds between minerals and organic polymers in the presence of moisture remains a serious technological challenge, fundamental insights into the mechanism of holdfast adhesion in mussels and other sessile marine organisms represent a potential data base of bio-inspired solutions to the moisture problem (1). One popular technique for improving "wet" adhesion on siliceous substrates involves the application of surface-coupling agents or adhesion promoters (2). Organosilanes are the best known synthetic adhesion promoters and typically designed with specific moieties for silica ligation at one end and reactivity toward the organic polymer at the other (2).The use of surface-coupling agents to promote adhesion resonates with the adhesive biochemistry of byssal plaques made by mussels. A recent investigation of plaque footprints in Mytilus californianus has revealed a family of protein variants (mcfp-3) with a 3,4-dihydroxyphenyl-L-alanine (Dopa) 2 content that approaches 25 mol % (3, 4). With its many Dopa residues, mcfp-3 has been compared wi...

show abstract

Section: Discussionmentioning

confidence: 99%

Linking Adhesive and Structural Proteins in the Attachment Plaque of Mytilus californianus

Zhao

Waite

2006

Journal of Biological Chemistry

258

243

View full text Add to dashboard Cite

show abstract

“…Comparable increases in surface adhesion have been reported in other catechol-bearing hydrogel networks. [ 69,70 ] The improved adhesion could be attributed to several types of bonds Adv. Mater.…”

Section: Communicationmentioning

confidence: 99%

Transfer Printing of Metallic Microstructures on Adhesion‐Promoting Hydrogel Substrates

Sariola

Zhu

et al. 2015

Advanced Materials

View full text Add to dashboard Cite

“…In contrast, mfp-1, the protein of the outer coating, has up to 15 mol% DOPA and a mass of Ϸ108 kDa. Previous studies of mussel adhesive proteins have proposed that the adhesion depends on DOPA (14,16), and engineered synthetic analogs have generally confirmed that the higher the DOPA content, the stronger the adhesion (17)(18)(19). Whether stronger adhesion is the effect of redox chemistry (20, 21), metal coordination (22), or a combination of reactions remains unresolved (23).…”

mentioning

confidence: 91%

Adhesion mechanisms of the mussel foot proteins mfp-1 and mfp-3

Lin¹,

Gourdon²,

Sun

et al. 2007

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

496

394

View full text Add to dashboard Cite

Mussels adhere to a variety of surfaces by depositing a highly specific ensemble of 3,4-dihydroxyphenyl-L-alanine (DOPA) containing proteins. The adhesive properties of Mytilus edulis foot proteins mfp-1 and mfp-3 were directly measured at the nano-scale by using a surface forces apparatus (SFA). An adhesion energy of order W Ϸ3 ؋ 10 ؊4 J/m 2 was achieved when separating two smooth and chemically inert surfaces of mica (a common alumino-silicate clay mineral) bridged or ''glued'' by mfp-3. This energy corresponds to an approximate force per plaque of Ϸ100 gm, more than enough to hold a mussel in place if no peeling occurs. In contrast, no adhesion was detected between mica surfaces bridged by mfp-1. AFM imaging and SFA experiments showed that mfp-1 can adhere well to one mica surface, but is unable to then link to another (unless sheared), even after prolonged contact time or increased load (pressure). Although mechanistic explanations for the different behaviors are not yet possible, the results are consistent with the apparent function of the proteins, i.e., mfp-1 is disposed as a ''protective'' coating, and mfp-3 as the adhesive or ''glue'' that binds mussels to surfaces. The results suggest that the adhesion on mica is due to weak physical interactions rather than chemical bonding, and that the strong adhesion forces of plaques arise as a consequence of their geometry (e.g., their inability to be peeled off) rather than a high intrinsic surface or adhesion energy, W. bioadhesion ͉ Mytilus edulis

show abstract

Rapid Gel Formation and Adhesion in Photocurable and Biodegradable Block Copolymers with High DOPA Content

Cited by 193 publications

References 59 publications

Linking Adhesive and Structural Proteins in the Attachment Plaque of Mytilus californianus

Linking Adhesive and Structural Proteins in the Attachment Plaque of Mytilus californianus

Transfer Printing of Metallic Microstructures on Adhesion‐Promoting Hydrogel Substrates

Adhesion mechanisms of the mussel foot proteins mfp-1 and mfp-3

Contact Info

Product

Resources

About