Solid-State NMR Analysis of Cross-Linking in Mussel Protein Glue

Holl, Susan M.; Hansen, Douglas C.; Waite, J. Herbert; Schaefer, Juergen R.

doi:10.1006/abbi.1993.1207

Cited by 49 publications

(34 citation statements)

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“…The mussel byssus threads seen in Fig. 196 are 5 times tougher and 16 times more extensible then the human tendon [346,347], furthermore the natural glue which attaches each thread to a surface is stronger then any man-made marine adhesive [258]. They are described in greater detail in Section 8.4.…”

Section: Marine Adhesivesmentioning

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: Marine Adhesivesmentioning

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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“…This constitutes an inherent difficulty in the case of natural fibers in which the intermolecular distance can be close to the intramolecular distance of 13 C-carbonyl groups in successive amino acid residues. The problem is aggravated if isotopic labeling is only partial, as is often the case when it is performed by feeding amino acids to the fiber-producing organism (73)(74)(75). Finally, the spin diffusion time should be short enough to minimize loss of intensity through T 1 relaxation.…”

Section: Spin Diffusion Experimentsmentioning

confidence: 99%

“…REDOR was used by the group of Schaefer to study cross-linking in mussel byssus threads (85) and adhesive plaques (74,85,86). Using 13 C-2 H REDOR, an increase in DOPA (3,4-dihydroxy-lphenylalanine) cross-linking was detected in the plaques when mussels produced byssus under raised water flow conditions (86).…”

Section: Measurement Of Internuclear Distancesmentioning

confidence: 99%

Studying natural structural protein fibers by solid‐state nuclear magnetic resonance

Arnold

Marcotte

2009

Concepts Magnetic Resonance

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As a consequence of evolutionary pressure, various organisms have developed structural fibers displaying a range of exceptional mechanical properties adapted specifically to their functions. An understanding of these properties at the molecular level requires a detailed description of local structure, orientation with respect to the fiber and size of constitutive units, and dynamics on various timescales. The size and lack of long-range order in these protein systems constitute an important challenge to classical structural techniques such as high-resolution NMR and X-ray diffraction. Solidstate NMR overcomes these constraints and is uniquely suited to the study of these inherently disordered systems. Solid-state NMR experiments developed or applied to determine structure, orientation, and dynamics of these complex proteins will be reviewed and illustrated through examples of their applications to fibers such as spider and silkworm silks, collagen, elastin, and keratin.

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“…Despite frequent references to in vitro studies postulating that quinone tanning involves nucleophilic addition of amine groups to quinones (2), nothing of substance is known about the actual cross-linking chemistry in these organisms. Indeed, previous efforts from our own laboratories seemed to rule out the existence of lysine-aromatic or aromaticaromatic coupling products in the mussel byssus (3,4). In 1994, Dolmer and Svane (5) reported that individual threads in a mussel byssus behaved as "smart materials" in flow: by doubling the flow of seawater, the tensile strength of the threads could be doubled.…”

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confidence: 99%

Rotational Echo Double Resonance Detection of Cross-links Formed in Mussel Byssus under High-Flow Stress

McDowell

Burzio

Waite

et al. 1999

Journal of Biological Chemistry

175

147

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13 C{2 H} rotational echo double resonance NMR has been used to provide the first evidence for the formation of quinone-derived cross-links in mussel byssal plaques. Labeling of byssus was achieved by allowing mussels to filter feed from seawater containing L-[phenol-4-13 C]tyrosine and L-[ring-d 4 ]tyrosine for 2 days. Plaques and threads were harvested from two groups of mussels over a period of 28 days. One group was maintained in stationary water while the other was exposed to turbulent flow at 20 cm/s. The flow-stressed byssal plaques exhibited significantly enhanced levels of 5, 5-di-dihydroxyphenylalanine cross-links. The average concentration of di-dihydroxyphenylalanine cross-links in byssal plaques is 1 per 1800 total protein amino acid residues.The attachment strategies of marine organisms that rely on DOPA-containing 1 adhesive proteins have recently come under much scrutiny. A number of these organisms, including tubebuilding polychaetes, black corals, ascidians, and mussels, cure their proteinaceous adhesives by a process called "quinone tanning" (1). Despite frequent references to in vitro studies postulating that quinone tanning involves nucleophilic addition of amine groups to quinones (2), nothing of substance is known about the actual cross-linking chemistry in these organisms. Indeed, previous efforts from our own laboratories seemed to rule out the existence of lysine-aromatic or aromaticaromatic coupling products in the mussel byssus (3, 4). In 1994, Dolmer and Svane (5) reported that individual threads in a mussel byssus behaved as "smart materials" in flow: by doubling the flow of seawater, the tensile strength of the threads could be doubled. This suggested that there were different degrees of quinone-tanning in a given material that relied in some way on maturation by imposed stresses. This paper reports on the continuation of work on the biosynthetic labeling of byssus with 13 C-and 2 H-containing analogs of tyrosine and the in situ analysis of this label-rich material by rotational echo double resonance (REDOR) NMR (6). We have repeated the byssus labeling under high flow conditions and compared directly REDOR spectra of byssal plaques collected under stressed (flow) and unstressed (stationary or minimal flow) conditions. The difference between these REDOR spectra reveal the preferential routing of tyrosine labels to diphenolics. The 13 C{ 2 H} REDOR dephasing is only consistent with the formation of 5, 5Ј-di-DOPA covalent crosslinks stabilizing the byssal plaques formed under stress. EXPERIMENTAL PROCEDURESMussel Labeling-170 Adult mussels (Mytilus edulis) were collected in the vicinity of Roosevelt Inlet at Lewes, Delaware. The mussels ranged in size from 3 to 10 cm. They were tethered to acrylic plates as described previously (4). The plates were put into two 140-liter marine aquarium tanks with salt water (no flow) at 14°C. The tanks were aerated. Labels H 4 ]tyrosine. The mussels were incubated with the labels for 48 h, after which control samples of plaques and threads were harv...

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Solid-State NMR Analysis of Cross-Linking in Mussel Protein Glue

Cited by 49 publications

References 0 publications

Biological materials: Structure and mechanical properties

Biological materials: Structure and mechanical properties

Studying natural structural protein fibers by solid‐state nuclear magnetic resonance

Rotational Echo Double Resonance Detection of Cross-links Formed in Mussel Byssus under High-Flow Stress

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