Tough Tendons

Xx, Qin; Coyne, Kathryn J.; Jh, Waite

doi:10.1074/jbc.272.51.32623

Cited by 136 publications

(88 citation statements)

References 38 publications

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“…The microstructure of byssal threads is roughly similar to that of tendons. The distal region consists of many bundles of collagen fibrils separated by fibrion-like domains and histidine-rich blocks, including possible b-sheet regions [259][260][261]. An illustration of the byssal thread micro and macrostructure is presented in Fig.…”

Section: Mussel Byssusmentioning

confidence: 99%

Biological materials: Structure and mechanical properties

Meyers

Chen

Lin

et al. 2008

Progress in Materials Science

2,164

1,129

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Most natural (or biological) materials are complex composites whose mechanical properties are often outstanding, considering the weak constituents from which they are assembled. These complex structures, which have risen from hundreds of million years of evolution, are inspiring Materials Scientists in the design of novel materials.Their defining characteristics, hierarchy, multifunctionality, and self-healing capability, are illustrated. Self-organization is also a fundamental feature of many biological materials and the manner by which the structures are assembled from the molecular level up. The basic building blocks are described, starting with the 20 amino acids and proceeding to polypeptides, polysaccharides, and polypeptides-saccharides. These, on their turn, compose the basic proteins, which are the primary constituents of 'soft tissues' and are also present in most biominerals. There are over 1000 proteins, and we describe only the principal ones, with emphasis on collagen, chitin, keratin, and elastin. The 'hard' phases are primarily strengthened by minerals, which nucleate and grow in a biomediated environment that determines the size, shape and distribution of individual crystals. The most important mineral phases are discussed: hydroxyapatite, silica, and aragonite.Using the classification of Wegst and Ashby, the principal mechanical characteristics and structures of biological ceramics, polymer composites, elastomers, and cellular materials are presented. Selected systems in each class are described with emphasis on the relationship between their structure and mechanical response. A fifth class is added to this: functional biological materials, which have a structure developed for a specific function: adhesion, optical properties, etc.An outgrowth of this effort is the search for bioinspired materials and structures. Traditional approaches focus on design methodologies of biological materials using conventional synthetic 0079-6425/$ -see front matter Ó

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Section: Mussel Byssusmentioning

confidence: 99%

Biological materials: Structure and mechanical properties

Meyers

Chen

Lin

et al. 2008

Progress in Materials Science

2,164

1,129

View full text Add to dashboard Cite

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“…2). [31][32][33] The polymer that is predominant at the proximal end of the thread (i.e. closest to the mussel tissue) consists of a central collagen block flanked by 2 elastic domains and 2 polyhistidine sequences.…”

Section: Mussel Byssus Threadmentioning

confidence: 99%

Protein-based materials, toward a new level of structural control

2001

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Through billions of years of evolution nature has created and refined structural proteins for a wide variety of specific purposes. Amino acid sequences and their associated folding patterns combine to create elastic, rigid or tough materials. In many respects, nature's intricately designed products provide challenging examples for materials scientists, but translation of natural structural concepts into bio-inspired materials requires a level of control of macromolecular architecture far higher than that afforded by conventional polymerization processes. An increasingly important approach to this problem has been to use biological systems for production of materials. Through protein engineering, artificial genes can be developed that encode protein-based materials with desired features. Structural elements found in nature, such as b-sheets and a-helices, can be combined with great flexibility, and can be outfitted with functional elements such as cell binding sites or enzymatic domains. The possibility of incorporating non-natural amino acids increases the versatility of protein engineering still

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“…A cDNA library of the foot (ZAP expression vector, Stratagene, La Jolla, CA) of Mytilus edulis initially was screened with an oligonucleotide probe encoding the signal peptide and N terminus of preCol-D with the aim of finding whole transcripts of preCol-D (8). Positive phages were converted into plasmids (Pbk-CVM) in the presence of helper phage (Stratagene).…”

Section: Methodsmentioning

confidence: 99%

“…To wit, byssal collagens have departed from several hallmarks of the type I-III fibrillar collagens: There is no apparent quarterstagger array during fibrillogenesis of byssal collagens (6); there is no procollagen precursor that requires activation to a tropocollagen (7,8), and maturation is not based on lysyl oxidase-catalyzed cross-linking (9). Detailed biochemical analysis of byssal threads, however, has been largely thwarted because of extensive quinone-tanning (10).…”

Section: Introductionmentioning

confidence: 99%

“…Two major thread precursors secreted by the foot are preCol-D and preCol-P. PreCol-P is a molecular hybrid of collagen with flanking domains having elastin-like sequences; its expression predominates in the proximal portion of the foot (7). PreCol-D, which is expressed strongly at the distal end of the foot, has a collagenous domain flanked by sequences resembling spider dragline silk motifs (8). Because the patterns of preCol expression in the foot mirror the graded distributions of Col-P and Col-D in byssal threads, the gradients appear to be predetermined in the foot before secretion.…”

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confidence: 99%

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A potential mediator of collagenous block copolymer gradients in mussel byssal threads

Qin

Waite²

1998

Proc. Natl. Acad. Sci. U.S.A.

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Mussel byssal threads contain unusual block copolymer-like proteins that combine collagen with f lanking domains that resemble silk-fibroin (preCol-D) or elastin (preCol-P). These are distributed in complementary gradients along the length of the threads and as precursors in the mussel foot. We discuss a 76-kDa precursor, preCol-NG, from a cDNA library of the foot where it has no gradient but rather is distributed evenly along the distal to proximal axis. A pepsinresistant fragment of preCol-NG has been confirmed in byssal threads. Like preCol-D and -P, this protein has a central collagenous domain, f lanking domains, an acidic patch, and histidine-rich termini. The f lanking domains of preCol-NG resemble the glycine-rich proteins of plant cell walls with tandem XGly n repeats where X denotes alanine, leucine, or asparagine but not proline. Similarity with the (glycinealanine) repeats and poly(alanine) runs of arthropod silks also exists. Based on available evidence, a model of preCol axial assembly is proposed in which preCol-NG functions as a mediator between preCol-D͞-P molecules. This is consistent with the observed progression of mechanical properties in byssal threads.A primary goal in the study of biomolecular materials is a fundamental understanding of how chemical and physical structure determines mechanical behavior. Byssal threads of marine mussels have three attributes that make them an attractive model system in pursuit of this goal: a comparatively simple morphology, rapid, reproducible formation, and interesting biomechanical properties. Byssal threads are proteinaceous tethers used by marine mussels to attach themselves to hard surfaces in the sea (Fig. 1A). Based on their collagen content, displacement outside the confines of living tissue, and proximal fusion with the byssal retractor muscles, the threads often are described as extracorporeal tendons (1, 2).Ironically, biomechanical analyses of byssal threads have revealed properties that differ significantly from those of vertebrate tendons (3, 4). Distally, they are as strong as tendon but with 3-5 times more extensibility; proximally, they are weaker but 15-20 times more extensible. In terms of strain energy density, byssal threads are Ϸ6 times tougher than tendon, and the distal portion may actually approach the toughness of silk (3). Even more intriguing is the observation by Bell (as cited in ref. 5) that, given sufficient relaxation time, stretched threads can recover their initial length and stiffness after yield.Recent biochemical analyses have sought a molecular explanation for the nontendon-like behavior of byssus. To wit, byssal collagens have departed from several hallmarks of the type I-III fibrillar collagens: There is no apparent quarterstagger array during fibrillogenesis of byssal collagens (6); there is no procollagen precursor that requires activation to a tropocollagen (7,8), and maturation is not based on lysyl oxidase-catalyzed cross-linking (9). Detailed biochemical analysis of byssal threads, however, has been l...

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Tough Tendons

Cited by 136 publications

References 38 publications

Biological materials: Structure and mechanical properties

Biological materials: Structure and mechanical properties

Protein-based materials, toward a new level of structural control

A potential mediator of collagenous block copolymer gradients in mussel byssal threads

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