Mussels attach to hard surfaces with DOPA‑rich byssus threads
Question asked:
“Mosselen (Mytilus edulis) hechten zich onder water stevig aan harde oppervlakken door byssusdraden die rijk zijn aan het aminozuur DOPA (3,4-dihydroxyfenylalanine).”
Summary
Blue mussels (Mytilus edulis) adhere strongly to hard underwater surfaces by producing byssal threads whose adhesive plaques contain high levels of the amino acid DOPA (3,4‑dihydroxyphenylalanine). This DOPA‑rich composition provides the strong, versatile bonding observed in mussel attachment.
Sources 57 searched
- Polyphenolic Substance of Mytilus edulis: Novel Adhesive Containing L-Dopa and Hydroxyproline - PubMed
The fouling marine mussel Mytilus edulis attaches itself to various substrates by spinning byssal threads, the adhesive discs of which are rich in the amino acid 3,4-dihydroxyphenylalanine (dopa).
- Expression sites of two byssal protein genes of Mytilus galloprovincialis - PubMed
Both proteins contain 3,4-dihydroxyphenylalanine (DOPA) in their primary sequences. In this study, the sites of expression of the genes encoding the polyphenolic proteins were investigated in Mytilus galloprovincialis.
- Identification and characterization of a wet adhesive protein extracted from Dreissena bugensis, the freshwater quagga mussel - PubMed
To identify adhesive proteins in the quagga mussel byssus, we utilized quantitative proteomics and found several proteins enriched at the byssus-substrate interface. Among the identified proteins was the Dbfp7 protein family. Dbfp7 is a small, polymorphic, and mostly disordered protein that lacks significant amounts of 3,4-dihydroxyphenylalanine (DOPA), a modified amino acid found in several marine mussel byssal proteins.
- Mytilus - an overview | ScienceDirect Topics
Extensive analysis of the byssal thread has identified load-bearing protein constituents, which resemble elastin, collagen, and silk,51 along with several adhesive pad proteins that contain the modified residue 3,4-dihydroxyphenylalanine (DOPA), derived by posttranslational modification of ...
- Byssus - an overview | ScienceDirect Topics
Extensive analysis of the byssal ... along with several adhesive pad proteins that contain the modified residue 3,4-dihydroxyphenylalanine (DOPA), derived by posttranslational modification of tyrosine residues....
- The effect of spawning of cultured mussels (Mytilus edulis) on mechanical properties, chemical and biochemical composition of byssal threads - ScienceDirect
Areas rich in histidine and 3,4-dihydroxyphenylalanine (DOPA) are located at the end of the flanking domains for all PreCOLs (Waite et al., 1998). The byssal thread envelope consists of a solid sheath of proteins called Mefp-1 (M. edulis foot ...
- Polyphenolic Substance of Mytilus edulis: Novel Adhesive Containing L-Dopa and Hydroxyproline | Science
The fouling marine mussel Mytilus edulis attaches itself to various substrates by spinning byssal threads, the adhesive discs of which are rich in the amino acid 3,4-dihydroxyphenylalanine (dopa).
- Why mussel byssal plaques are tiny yet strong in attachment: Matter
The byssal plaque is a thin film that connects the byssal thread to the rock surface (Figure 1B) and it is composed of six kinds of mussel foot proteins (mfps) with high concentrations of L-3,4-dihydroxyphenylalanine (DOPA), which gives a strong bond to almost any type of material surface by forming either non-covalent bonding interactions (e.g., ionic and/or hydrogen bonds) or covalent bonding interaction to different substrates.10
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