Cited by 610Marine Biology and Environmental ChemistryPolymer Surface Interaction StudiesCalcium Carbonate Crystallization and Inhibition

Polyphosphoprotein from the Adhesive Pads of Mytilus edulis

Waite, J. Herbert, Qin, Xiaoxia·2001·Biochemistry

Abstract

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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Crossref · 10.1021/bi002718x

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  • The adhesive function of polydopamine originates from the study of mussel adhesive proteins (MAPs) secreted by marine mussel (e.g., Mytilus edulis).

    “The adhesive function of polydopamine originates from the study of mussel adhesive proteins (MAPs) secreted by marine mussel (e.g., Mytilus edulis).”
  • MAPs contain abundant 3,4-dihydroxy-L-phenylalanine (DOPA) that enable mussel organism to adhere to almost all kinds of materials via covalent and noncovalent bonding.

    “MAPs contain abundant 3,4-dihydroxy-L-phenylalanine (DOPA) that enable mussel organism to adhere to almost all kinds of materials via covalent and noncovalent bonding [19, 20].”
  • MAP is able to form adhesive "feet" to attach to different materials in humid environment and even rigorously trembling environment.

    “It was found that MAP is able to form adhesive “feet” to attach to different materials in humid environment and even rigorously trembling environment [19].”
  • On organic material surfaces, oxidation of catechol groups exposed on the polydopamine coating layer forms quinone/semiquinone, leading to irreversible covalent bonding between biomolecules and the organic material surface via Michael addition and Schiff formation reactions, and further triggering intermolecular cross-linking among polydopamine polymers.

    “For the surface of organic material, the oxidation of catechol group exposed on the PDA coating layer results in the formation of quinone/semiquinone to form irreversible covalent bonding [19] between biomolecules and the surface of organic material via similar Michael addition and Schiff formation reactions [29] and thereby further trigger the intermolecular cross-linking reactions among PDA”

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Authors
Waite, J. H., & Qin, X.
Affiliations
  • University of California, Santa Barbara (US)
  • Duke University (US)
Corresponding author
Waite, J. Herbert
Venue
Biochemistry
Published
2001-02-08
Volume
40
Issue
9
Pages
2887-2893
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
OpenAlex
W2006167320
Cited by
610
References
1
Citations by year
2026: 12 · 2025: 30 · 2024: 16 · 2023: 27 · 2022: 20 · 2021: 35 · 2020: 31 · 2019: 34 · 2018: 51 · 2017: 28 · 2016: 28 · 2015: 25 · 2014: 43 · 2013: 38 · 2012: 41
FWCI
17.71
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Ministerio de Educación y Formación Profesional
  • National Institutes of Health (5r01de010042-11)
  • Office of Naval Research
  • National Institute of Dental and Craniofacial Research (DE10042-7A1)
Topics
  • Physical Sciences › Engineering › Ocean Engineering › Marine Biology and Environmental Chemistry
  • Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
  • Physical Sciences › Materials Science › Biomaterials › Calcium Carbonate Crystallization and Inhibition
Keywords
Mytilus edulis, mussel foot, wet adhesion, hydroxylation, phosphorylation, DOPA, phosphoserine, post-translational modification, primary structure, amino acid composition
MeSH terms
Amino Acid Sequence, Amino Acids, Animals, Base Sequence, Chromatography, High Pressure Liquid, Molecular Sequence Data, Phosphoproteins, Proteins, Polymerase Chain Reaction, DNA, Complementary, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Sequence Analysis, Protein, Bivalvia

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