Recombinant Proteins: A Molecular Tool to Understand Marine Adhesion and to Advance Biomaterials

Inspiration for innovation in healthcare regularly comes from observing the natural environment. Secreted adhesives are important for marine invertebrate attachment to submerged surfaces, and these systems have inspired investigations for better performing surgical adhesives. Natural marine adhesives are fundamentally proteins, therefore, most materials research has focused on the structure and function of proteinaceous components. Omics technologies have been used to identify proteins, but these candidates require further exploration to resolve function. Functional characterization begins by producing one specific protein in larger quantities with recombinant DNA technology. Recombinant proteins (RPs) are generally seen as mimics of individual marine adhesive proteins, representing a fundamental step in the development of bio-inspired glues. The literature details production of RPs from mussels, scallops, barnacles, tubeworms, ascidians, sea anemones, and sea stars, using bacteria, yeast, or insect and mammalian cells. Whole proteins, or components thereof, have been produced comprising the relevant amino acid sequences required for adhesion and have been investigated for use in healthcare via the production of materials that push the current limits of bio-inspired design. This is a thorough review of invertebrate marine adhesives investigated using biomimetic RPs, and a comprehensive overview of the innovative biomaterials designed utilizing knowledge from biological systems.

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Publication Details

Journal
Advanced Healthcare Materials
Published
2025-10-02
DOI
https://doi.org/10.1002/adhm.202502340
Primary Topic
Polymer Surface Interaction Studies
Type
article
Field-Weighted Citation Impact
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article

Recombinant Proteins: A Molecular Tool to Understand Marine Adhesion and to Advance Biomaterials

Elise Hennebert, Patrick Flammang, Alessandra Whaite, Mathilde Lefevre et al.
Advanced Healthcare Materials
Polymer Surface Interaction Studies
article

Recombinant Proteins: A Molecular Tool to Understand Marine Adhesion and to Advance Biomaterials

Elise Hennebert, Patrick Flammang, Alessandra Whaite, Mathilde Lefevre, Emilie Duthoo
article en

Abstract

Inspiration for innovation in healthcare regularly comes from observing the natural environment. Secreted adhesives are important for marine invertebrate attachment to submerged surfaces, and these systems have inspired investigations for better performing surgical adhesives. Natural marine adhesives are fundamentally proteins, therefore, most materials research has focused on the structure and function of proteinaceous components. Omics technologies have been used to identify proteins, but these candidates require further exploration to resolve function. Functional characterization begins by producing one specific protein in larger quantities with recombinant DNA technology. Recombinant proteins (RPs) are generally seen as mimics of individual marine adhesive proteins, representing a fundamental step in the development of bio-inspired glues. The literature details production of RPs from mussels, scallops, barnacles, tubeworms, ascidians, sea anemones, and sea stars, using bacteria, yeast, or insect and mammalian cells. Whole proteins, or components thereof, have been produced comprising the relevant amino acid sequences required for adhesion and have been investigated for use in healthcare via the production of materials that push the current limits of bio-inspired design. This is a thorough review of invertebrate marine adhesives investigated using biomimetic RPs, and a comprehensive overview of the innovative biomaterials designed utilizing knowledge from biological systems.

Advanced Healthcare MaterialsVol. 15(3)
University of Mons (BE)
Openalex Percentile: Top 74%
Polymer Surface Interaction Studies
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Recombinant Proteins: A Molecular Tool to Understand Marine Adhesion and to Advance Biomaterials — Elise Hennebert, Patrick Flammang, et al. · Advanced Healthcare Materials (2025) | TGRS Research Map | TGRS