Following the thread: Mytilus mussel byssus as an inspired multi-functional biomaterial

Over the last 15 years, the byssus of marine mussels (Mytilus spp.) has emerged as an important model system for the bio-inspired development and synthesis of advanced polymers and adhesives. But how did these seemingly inconsequential fibers that are routinely discarded in mussel hors d’oeuvres become the focus of intense international research. In the present review, we take a historical perspective to understand this phenomenon. Our purpose is not to review the sizeable literature of mussel-inspired materials as there are numerous excellent reviews that cover this topic in great depth. Instead, we explore how the byssus became a magnet for bio-inspired materials science, with a focus on the specific breakthroughs in the understanding of composition, structure, function and formation of the byssus achieved through fundamental scientific investigation. Extracted principles have led to bio-inspired design of novel materials with both biomedical and technical applications, including surgical adhesives, self-healing polymers, tunable hydrogels and even actuated composites. Continued study into the byssus of Mytilid mussels and other species will provide a rich source of inspiration for years to come.

From vesicles to materials: bioinspired strategies for fabricating hierarchically structured soft matter

Certain organisms including species of mollusks, polychaetes, onychophorans and arthropods produce exceptional polymeric materials outside their bodies under ambient conditions using concentrated fluid protein precursors. While much is understood about the structure-function relationships that define the properties of such materials, comparatively less is understood about how such materials are fabricated and specifically, how their defining hierarchical structures are achieved via bottom-up assembly. Yet this information holds great potential for inspiring sustainable manufacture of advanced polymeric materials with controlled multi-scale structure. In the present perspective, we first examine recent work elucidating the formation of the tough adhesive fibres of the mussel byssus via secretion of vesicles filled with condensed liquid protein phases (coacervates and liquid crystals)—highlighting which design principles are relevant for bio-inspiration. In the second part of the perspective, we examine the potential of recent advances in drops and additive manufacturing as a bioinspired platform for mimicking such processes to produce hierarchically structured materials. This article is part of the theme issue ‘Bio-derived and bioinspired sustainable advanced materials for emerging technologies (part 1)’.

Mussel byssus cuticle-inspired ultrastiff and stretchable triple-crosslinked hydrogels

The triple-crosslinked hydrogel constructed through a crosslinking hierarchy exhibits significant increase in stiffness but without sacrificing the maximum elongation.

Compartmentalized processing of catechols during mussel byssus fabrication determines the destiny of DOPA

Inspired largely by the role of the posttranslationally modified amino acid dopa (DOPA) in mussel adhesion, catechol functional groups have become commonplace in medical adhesives, tissue scaffolds, and advanced smart polymers. Yet, the complex redox chemistry of catechol groups complicates cross-link regulation, hampering fabrication and the long-term stability/performance of mussel-inspired polymers. Here, we investigated the various fates of DOPA residues in proteins comprising mussel byssus fibers before, during, and after protein secretion. Utilizing a combination of histological staining and confocal Raman spectroscopy on native tissues, as well as peptide-based cross-linking studies, we have identified at least two distinct DOPA-based cross-linking pathways during byssus fabrication, achieved by oxidative covalent cross-linking or formation of metal coordination interactions under reducing conditions, respectively. We suggest that these end states are spatiotemporally regulated by the microenvironments in which the proteins are stored prior to secretion, which are retained after formation—in particular, due to the presence of reducing moieties. These findings provide physicochemical pathways toward greater control over properties of synthetic catechol-based polymers and adhesives.