Amyloid-like Conformation and Interaction for the Self-Assembly in Barnacle Underwater Cement

Nakano, Masahiro; Kamino, Kei

doi:10.1021/bi500965f

Cited by 68 publications

(73 citation statements)

References 71 publications

(109 reference statements)

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“…10,36 Previous in vitro efforts to form fibrils in solution from individual barnacle proteins have been successful by generating unstable peptide segments of parent proteins. 19,37 In contrast, our work here shows that interactions with periodic surface features can serve to destabilize intact cement proteins in forming nanostructured fibrils.…”

Section: Discussioncontrasting

confidence: 58%

Self-Assembly of Protein Nanofibrils Orchestrates Calcite Step Movement through Selective Nonchiral Interactions

Liu

Fears

et al. 2015

ACS Nano

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The recognition of atomically distinct surface features by adsorbed biomolecules is central to the formation of surface-templated peptide or protein nanostructures. On mineral surfaces such as calcite, biomolecular recognition of, and self-assembly on, distinct atomic kinks and steps could additionally orchestrate changes to the overall shape and symmetry of a bulk crystal. In this work, we show through in situ atomic force microscopy (AFM) experiments that an acidic 20 kDa cement protein from the barnacle Megabalanus rosa (MRCP20) binds specifically to step edge atoms on {101̅4} calcite surfaces, remains bound and further assembles over time to form one-dimensional nanofibrils. Protein nanofibrils are continuous and organized at the nanoscale, exhibiting striations with a period of ca. 45 nm. These fibrils, templated by surface steps of a preferred geometry, in turn selectively dissolve underlying calcite features displaying the same atomic arrangement. To demonstrate this, we expose the protein solution to bare and fibril-associated rhombohedral etch pits to reveal that nanofibrils accelerate only the movement of fibril-forming steps when compared to undecorated steps exposed to the same solution conditions. Calcite mineralized in the presence of MRCP20 results in asymmetric crystals defined by frustrated faces with shared mirror symmetry, suggesting a similar step-selective behavior by MRCP20 in crystal growth. As shown here, selective surface interactions with step edge atoms lead to a cooperative regime of calcite modification, where templated long-range protein nanostructures shape crystals.

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Section: Discussioncontrasting

confidence: 58%

Self-Assembly of Protein Nanofibrils Orchestrates Calcite Step Movement through Selective Nonchiral Interactions

Liu

Fears

et al. 2015

ACS Nano

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“…30% of all identifiable peptides in cement, where most align to a specific egg stalk silk. Since GSrCPs comprise a large portion of a fibrous material with amyloid-like secondary structure1214, we believe homology with arthropod silks to be biologically significant. The highly varied compositions of other proteins in the barnacle cement proteome such as LrCPs, SIPCs and other miscellaneous enzymes indicate that alignments are not from a bias in overall barnacle protein composition.…”

Section: Discussionmentioning

confidence: 99%

“…In contrast to marine organisms that use glues to fabricate protective shelters (e.g., sand-castle worm tubes5, case-maker fly larva retreats2, and amphipod tubes67) or tie themselves to rocks, (e.g., mussel byssus threads89) adult barnacles produce their adhesive interface in a sequential process hidden under their base as a part of their normal growth cycle1011. The recent finding that barnacle adhesive is nanostructured and held together as an amyloid-like material121314 further distinguishes it from archetypal marine adhesives processed into solid foams1915 or spun threads26.…”

mentioning

confidence: 99%

“…High levels of aliphatic residues in these cement components have led to a hypothesis that the barnacle adhesive is partially held together and operates through a hydrophobic effect1720222324. However, it has been difficult to establish the main components of bulk cement as many demonstrate in vitro fibril formation14252627, while a significant portion remains insoluble and, therefore, unidentifiable.…”

mentioning

confidence: 99%

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Sequence basis of Barnacle Cement Nanostructure is Defined by Proteins with Silk Homology

Fears

Leary

et al. 2016

Sci Rep

194

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Barnacles adhere by producing a mixture of cement proteins (CPs) that organize into a permanently bonded layer displayed as nanoscale fibers. These cement proteins share no homology with any other marine adhesives, and a common sequence-basis that defines how nanostructures function as adhesives remains undiscovered. Here we demonstrate that a significant unidentified portion of acorn barnacle cement is comprised of low complexity proteins; they are organized into repetitive sequence blocks and found to maintain homology to silk motifs. Proteomic analysis of aggregate bands from PAGE gels reveal an abundance of Gly/Ala/Ser/Thr repeats exemplified by a prominent, previously unidentified, 43 kDa protein in the solubilized adhesive. Low complexity regions found throughout the cement proteome, as well as multiple lysyl oxidases and peroxidases, establish homology with silk-associated materials such as fibroin, silk gum sericin, and pyriform spidroins from spider silk. Distinct primary structures defined by homologous domains shed light on how barnacles use low complexity in nanofibers to enable adhesion, and serves as a starting point for unraveling the molecular architecture of a robust and unique class of adhesive nanostructures.

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“…If more widely practiced, it may offer a significant potential control point against biofouling that has not previously been considered. On this note, Dopa-deficient cement proteins of barnacles rely on pH and ionic strength to undergo a triggered self-assembly reminiscent of amyloid formation (Nakano & Kamino 2014). …”

Section: Discussionmentioning

confidence: 99%

Interfacial pH during mussel adhesive plaque formation

et al. 2015

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Mussel (Mytilus californianus) adhesion to marine surfaces involves an intricate and adaptive synergy of molecules and spatio-temporal processes. Although the molecules, such as mussel foot proteins (mfps), are well characterized, deposition details remain vague and speculative. Developing methods for the precise surveillance of conditions that apply during mfp deposition would aid both in understanding mussel adhesion and translating this adhesion into useful technologies. To probe the interfacial pH at which mussels buffer the local environment during mfp deposition, a lipid bilayer with tethered pH-sensitive fluorochromes was assembled on mica. The interfacial pH during foot contact with modified mica ranged from 2.2−3.3, which is well below the seawater pH of ~8. The acidic pH serves multiple functions: it limits mfp-Dopa oxidation, thereby enabling the catecholic functionalities to adsorb to surface oxides by H-bonding and metal ion coordination, and provides a solubility switch for mfps, most of which aggregate at pH ≥ 7-8.

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Amyloid-like Conformation and Interaction for the Self-Assembly in Barnacle Underwater Cement

Cited by 68 publications

References 71 publications

Self-Assembly of Protein Nanofibrils Orchestrates Calcite Step Movement through Selective Nonchiral Interactions

Self-Assembly of Protein Nanofibrils Orchestrates Calcite Step Movement through Selective Nonchiral Interactions

Sequence basis of Barnacle Cement Nanostructure is Defined by Proteins with Silk Homology

Interfacial pH during mussel adhesive plaque formation

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