Adsorption and Self‐Assembly of Peptides on Mica Substrates

Whitehouse, Conor; Fang, Jiyu; Aggeli, Amalia; Bell, Mark; Brydson, Rik; Fishwick, Colin W. G.; Henderson, J. Gordon; Knobler, Charles M.; Owens, Robert W.; Thomson, Neil H.; Smith, D. A.; Boden, N.

doi:10.1002/anie.200462160

Cited by 113 publications

(101 citation statements)

References 16 publications

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“…Surprisingly, the thickness of the ribbons was determined by AFM to be much lower than previously found for other self-assembled fibrous IDPs (52). The determined thickness of AMBN ribbons was comparable to the thickness of ␤-sheet structures or to that reported for ssDNA (53)(54)(55).…”

Section: Discussionsupporting

confidence: 49%

“…It has previously been shown that certain model peptides, such as those forming the cross-␤-sheet ribbon structures in solution, can undergo reorganization on mica surface during water evaporation. This then results in formation of monomolecular highly ordered films because of alignment of these ribbons on mica surface (55). We hypothesize that a similar process could have been taking place also during AMBN monolayer formation on mica surface.…”

Section: Discussionmentioning

confidence: 82%

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Intrinsically Disordered Enamel Matrix Protein Ameloblastin Forms Ribbon-like Supramolecular Structures via an N-terminal Segment Encoded by Exon 5

Wald

Osičková

Šulc

et al. 2013

Journal of Biological Chemistry

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Background: Ameloblastin plays a key role in the complex biomineralization process that forms tooth enamel, the hardest tissue of the body. Results: Ameloblastin self-associates into ribbon-like supramolecular structures via a short segment encoded by exon 5. Conclusion: Ameloblastin self-association may be essential for correct structural organization and mineralization of the enamel in vivo. Significance: The results provide molecular insight into biology of tooth enamel formation.

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Section: Discussionsupporting

confidence: 49%

Section: Discussionmentioning

confidence: 82%

Intrinsically Disordered Enamel Matrix Protein Ameloblastin Forms Ribbon-like Supramolecular Structures via an N-terminal Segment Encoded by Exon 5

Wald

Osičková

Šulc

et al. 2013

Journal of Biological Chemistry

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“…The peptide GAV-9 (NH 2 -VGGAVVAGV-CONH 2 ) was synthesized using the t-Butyloxy carbonyl (Boc) solid-phase method and cleaved from the resin with hydrogen fluoride. The sample had a purity of 98.8% m/m, which was verified by HPLC and was further characterized using a mass spectrum (9). Before use, freeze-dried peptide powder was dissolved to a concentration of ∼3 mM in aqueous solutions of certain salts.…”

Section: Methodsmentioning

confidence: 99%

“…In addition to a series of factors (4-6) previously discovered to modulate peptide self-assembly, solid substrates have been found to drive this process directly acting as templates (7,8), controlling both assembly kinetics and morphology of amyloid peptide aggregates (8)(9)(10)(11). These findings emphasize the importance of the substrate surface, whether it be a cellular membrane or an inorganic solid surface, on the assembly of various peptides, which is critical in many biological processes.…”

mentioning

confidence: 87%

Salts drive controllable multilayered upright assembly of amyloid-like peptides at mica/water interface

Dai

Kang

Huynh

et al. 2013

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

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Surface-assisted self-assembly of amyloid-like peptides has received considerable interest in both amyloidosis research and nanotechnology in recent years. Despite extensive studies, some controlling factors, such as salts, are still not well understood, even though it is known that some salts can promote peptide selfassemblies through the so-called "salting-out" effect. However, they are usually noncontrollable, disordered, amorphous aggregates. Here, we show via a combined experimental and theoretical approach that a conserved consensus peptide NH 2 -VGGAVVAGV-CONH 2 (GAV-9) (from representative amyloidogenic proteins) can self-assemble into highly ordered, multilayered nanofilaments, with surprising all-upright conformations, under high-salt concentrations. Our atomic force microscopy images also demonstrate that the vertical stacking of multiple layers is highly controllable by tuning the ionic strength, such as from 0 mM (monolayer) to 100 mM (mainly double layer), and to 250 mM MgCl 2 (double, triple, quadruple, and quintuple layers). Our atomistic molecular dynamics simulations then reveal that these individual layers have very different internal nanostructures, with parallel β-sheets in the first monolayer but antiparallel β-sheets in the subsequent upper layers due to their different microenvironment. Further studies show that the growth of multilayered, all-upright nanostructures is a common phenomenon for GAV-9 at the mica/water interface, under a variety of salt types and a wide range of salt concentrations.amyloid peptide | atomic force microscopy | salt effect | self-assembly on mica A better understanding of the self-assembly of highly ordered peptide nanostructures is critical because it not only helps to uncover the pathogenesis of various neurodegenerative diseases (1) but provides an attractive "bottom-up" nanotechnology for de novo nanodevice design (2) and fabrication (3). In addition to a series of factors (4-6) previously discovered to modulate peptide self-assembly, solid substrates have been found to drive this process directly acting as templates (7,8), controlling both assembly kinetics and morphology of amyloid peptide aggregates (8-11). These findings emphasize the importance of the substrate surface, whether it be a cellular membrane or an inorganic solid surface, on the assembly of various peptides, which is critical in many biological processes. It has been shown recently that fibrous nanostructures form a fundamental framework ubiquitous in normal cellular metabolism, including cell division and signaling, as well as in over 27 different human amyloid diseases and 9 in animals (12).Due to the complexity of cellular membranes and associated physiological conditions (13,14), hydrophilic mica and hydrophobic highly oriented pyrolytic graphite (HOPG) are the two commonly used model substrates for the investigation of surface effects (10,11,15). For example, it was found that amyloid-β (Aβ) peptide formed oligomeric protofibrillar aggregates on mica but only 1D nanofilaments on HOPG (...

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“…Such a mechanism has practical applications in industrial biosensors, in biotechnology, and in nanotechnology [3,8]. Surface-mediated fibril formation occurs in oligopeptides (typically around 20 residues long) [9][10][11][12] and amyloid beta peptide [13][14][15][16], but also for silkelastine-like polymers [17,18]. The surface-induced fibril selfassembly process can occur via several routes.…”

Section: Introductionmentioning

confidence: 99%

Competition between surface adsorption and folding of fibril-forming polypeptides

Kleijn

Abeln

et al. 2015

Phys. Rev. E

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Competition between surface adsorption and folding of fibril-forming polypeptidesNi, R.; Kleijn, J.M.; Abeln, S.; Cohen Stuart, M.A.; Bolhuis, P.G. Published in:Physical Review E DOI:10.1103/PhysRevE.91.022711 Link to publication Citation for published version (APA):Ni, R., Kleijn, J. M., Abeln, S., Cohen Stuart, M. A., & Bolhuis, P. G. (2015). Competition between surface adsorption and folding of fibril-forming polypeptides. Physical Review E, 91(2), 022711. DOI: 10.1103/PhysRevE.91.022711 General rightsIt is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. Download date: 11 May 2018PHYSICAL REVIEW E 91, 022711 (2015) Competition between surface adsorption and folding of fibril-forming polypeptides Self-assembly of polypeptides into fibrillar structures can be initiated by planar surfaces that interact favorably with certain residues. Using a coarse-grained model, we systematically studied the folding and adsorption behavior of a β-roll forming polypeptide. We find that there are two different folding pathways depending on the temperature: (i) at low temperature, the polypeptide folds in solution into a β-roll before adsorbing onto the attractive surface; (ii) at higher temperature, the polypeptide first adsorbs in a disordered state and folds while on the surface. The folding temperature increases with increasing attraction as the folded β-roll is stabilized by the surface. Surprisingly, further increasing the attraction lowers the folding temperature again, as strong attraction also stabilizes the adsorbed disordered state, which competes with folding of the polypeptide. Our results suggest that to enhance the folding, one should use a weakly attractive surface. They also explain the recent experimental observation of the nonmonotonic effect of charge on the fibril formation on an oppositely charged surface [C.

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Adsorption and Self‐Assembly of Peptides on Mica Substrates

Cited by 113 publications

References 16 publications

Intrinsically Disordered Enamel Matrix Protein Ameloblastin Forms Ribbon-like Supramolecular Structures via an N-terminal Segment Encoded by Exon 5

Intrinsically Disordered Enamel Matrix Protein Ameloblastin Forms Ribbon-like Supramolecular Structures via an N-terminal Segment Encoded by Exon 5

Salts drive controllable multilayered upright assembly of amyloid-like peptides at mica/water interface

Competition between surface adsorption and folding of fibril-forming polypeptides

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