Understanding Marine Mussel Adhesion

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Abstract

In addition to identifying the proteins that have a role in underwater adhesion by marine mussels, research efforts have focused on identifying the genes responsible for the adhesive proteins, environmental factors that may influence protein production, and strategies for producing natural adhesives similar to the native mussel adhesive proteins. The production-scale availability of recombinant mussel adhesive proteins will enable researchers to formulate adhesives that are water-impervious and ecologically safe and can bind materials ranging from glass, plastics, metals, and wood to materials, such as bone or teeth, biological organisms, and other chemicals or molecules. Unfortunately, as of yet scientists have been unable to duplicate the processes that marine mussels use to create adhesive structures. This study provides a background on adhesive proteins identified in the blue mussel, Mytilus edulis, and introduces our research interests and discusses the future for continued research related to mussel adhesion.

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Most cited references 178

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Rapidly recovering hydrogel scaffolds from self-assembling diblock copolypeptide amphiphiles.

Andrew P Nowak, Victor Breedveld, Lisa Pakstis … (2002)

Protein-based hydrogels are used for many applications, ranging from food and cosmetic thickeners to support matrices for drug delivery and tissue replacement. These materials are usually prepared using proteins extracted from natural sources, which can give rise to inconsistent properties unsuitable for medical applications. Recent developments have utilized recombinant DNA methods to prepare artificial protein hydrogels with specific association mechanisms and responsiveness to various stimuli. Here we synthesize diblock copolypeptide amphiphiles containing charged and hydrophobic segments. Dilute solutions of these copolypeptides would be expected to form micelles; instead, they form hydrogels that retain their mechanical strength up to temperatures of about 90 degrees C and recover rapidly after stress. The use of synthetic materials permits adjustment of copolymer chain length and composition, which we varied to study their effect on hydrogel formation and properties. We find that gelation depends not only on the amphiphilic nature of the polypeptides, but also on chain conformations--alpha-helix, beta-strand or random coil. Indeed, shape-specific supramolecular assembly is integral to the gelation process, and provides a new class of peptide-based hydrogels with potential for applications in biotechnology.

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Polyphosphoprotein from the adhesive pads of Mytilus edulis.

J H Waite, X. QIN (2001)

Achieving a satisfactory biochemical explanation for the opportunistic underwater adhesion of marine invertebrates such as mussels and barnacles requires a detailed characterization of proteins extracted from holdfast structures produced by these organisms. Mefp-5 is an adhesive protein derived from the foot of the common mussel, Mytilus edulis, and deposited into the byssal attachment pads. Purification and primary structure of mefp-5 was determined by peptide mapping and cDNA sequencing. The protein is 74 residues long and has a mass of about 9500 Da. Mefp-5 composition shows a strong amino acid bias: aromatic amino acids, lysine, and glycine represent 65 mol % of the composition. More than a third of all the residues in the protein are posttranslationally modified by hydroxylation or phosphorylation. The conversion of tyrosine to 3, 4-dihydroxyphenyl-L-alanine (DOPA) and serine to O-phosphoserine accounts for the hydroxylation and phosphorylation, respectively. Neither modification is complete since variations in the extent of phosphorylation and hydroxylation can be detected by mass spectrometry. More than 75% of the DOPA is adjacent to basic residues, e.g., Lys-DOPA and DOPA-Lys. Phosphoserine occurs in sequences strikingly reminiscent of acidic mineral-binding motifs that appear in statherin, osteopontin, and others. This may be an adaptation for adhesion to the most common substrata for mussels, i.e., calcareous materials.

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Nature's underwater adhesive specialist

J.H. Waite (1987)

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Contributors

: Heather.Silverman@inl.gov,

Bio :

Ms. Heather G. Silverman is a senior scientist in the Biological Systems department at the Department of Energy’s Idaho National Laboratory (DOE-INL). She is a principal investigator for projects related to mussel adhesive proteins. She also is a lead scientist for projects ranging from detection of pathogens to investigating microbial genomes. Ms. Silverman received a B.S. in Physical Education (exercise science) from the University of California, Davis, an M.S. in Kinesiology (exercise physiology) from the University of Colorado, Boulder, and an M.S. in Biology (molecular biology) from Idaho State University. She has been acknowledged for her mussel adhesives research from the Technology Transfer Research and Academic Linkage for Students (TRAILS) program at the INL and has two U.S. patent applications related to large-scale production of recombinant mussel adhesive proteins. Ms. Silverman is an Idaho Innovation Stoel Rives Chemical Division Finalist for her work on the “Blue Mussel Adhesive.”

Bio :

Dr. Francisco F. Roberto is a senior consulting scientist in the Biological Systems department at the Department of Energy’s Idaho National Laboratory (DOE-INL). He is a principal investigator for projects ranging from sulfide mineral bioleaching to detection of priority pathogens using real-time PCR. Dr. Roberto received a B.S. in biochemistry from the University of California, Davis, and Ph.D. in biochemistry from the University of California, Riverside. Before joining the INL, he was a postdoctoral fellow in plant pathology at the University of California, Davis. He is an affiliate faculty member in Biological Sciences at Idaho State University, Microbiology, Molecular Biology and Biochemistry, and Plant, Soil, and Entomological Sciences at the University of Idaho, and adjunct graduate faculty at Texas Tech University. He has authored or co-authored more than 50 peer-reviewed publications and presentations, 4 U.S. patents, and has served on the editorial board of the peer-reviewed journals Applied and Environmental Microbiology and Journal of Industrial Microbiology and Biotechnology. He is a recipient of the Lockheed Martin NOVA Award for Technical Excellence and the British Biotechnology and Biological Sciences Research Council Underwood Fund travel grant.

Journal

Journal ID (nlm-ta): Mar Biotechnol (NY)

Title: Marine Biotechnology (New York, N.y.)

Publisher: Springer-Verlag (New York )

ISSN (Print): 1436-2228

ISSN (Electronic): 1436-2236

Publication date (Electronic): 8 November 2007

Publication date (Print): December 2007

Volume: 9

Issue: 6

Pages: 661-681

Affiliations

Biological Systems Department, Idaho National Laboratory, Idaho Falls, Idaho 83415 USA

Article

Publisher ID: 9053

DOI: 10.1007/s10126-007-9053-x

PMC ID: 2100433

PubMed ID: 17990038

SO-VID: 84358b6e-ea2b-470d-ab1d-e23b58ca02ac

History

Date received : 7 March 2007

Date revision received : 24 August 2007

Date accepted : 5 September 2007

Custom metadata

ScienceOpen disciplines: Biotechnology

Keywords: recombinant protein, marine mussel (mytilus edulis),adhesion,biomimetics

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ScienceOpen disciplines: Biotechnology

Keywords: recombinant protein, marine mussel (mytilus edulis), adhesion, biomimetics

Understanding Marine Mussel Adhesion

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Abstract

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Marine Life Science & Technology

Most cited references 178

Rapidly recovering hydrogel scaffolds from self-assembling diblock copolypeptide amphiphiles.

Polyphosphoprotein from the adhesive pads of Mytilus edulis.

Nature's underwater adhesive specialist

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