Computationally designed peptides for self-assembly of nanostructured lattices

Zhang, Huixi Violet; Polzer, Frank; Haider, Michael; Tian, Yu; Villegas, José A.; Kiick, Kristi L.; Pochan, Darrin J.; Saven, Jeffery G.

doi:10.1126/sciadv.1600307

Cited by 68 publications

(121 citation statements)

References 52 publications

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“…Saven and co‐workers used a computational approach to identify a sequence variant of a 3‐helix bundle that would self‐interact to form a crystalline lattice with a specific geometry (Figure g) . This computational approach was also used to design robust arrays of two‐dimensional helical bundles that could tolerate variability in the solution conditions as well as chemical modification of the termini …”

Section: Agglomeration For the Design Of Biomaterialsmentioning

confidence: 99%

Infinite Assembly of Folded Proteins in Evolution, Disease, and Engineering

2019

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Mutations and changes in a protein's environment are well characterized for their potential to induce misfolding and aggregation, including amyloid formation. Alternatively, such perturbations can trigger new interactions leading to the polymerization of folded proteins. In contrast to aggregation, this process does not require misfolding and to mark this difference, we refer to it as agglomeration. This term encompasses the amorphous assembly of folded proteins as well as their folded-state polymerization in one-, two-, or three-dimensions. We stress the remarkable potential of symmetric homo-oligomers to agglomerate even by single surface point mutations, and we review the double-edged nature of this potential: how aberrant assemblies resulting from agglomeration can lead to disease, but also how agglomeration can serve in cellular adaptation and be exploited for the rational design of novel biomaterials.

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Section: Agglomeration For the Design Of Biomaterialsmentioning

confidence: 99%

Infinite Assembly of Folded Proteins in Evolution, Disease, and Engineering

2019

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“…Saven und Mitarbeiter verfolgten einen computerbasierten Ansatz, um eine Sequenzvariante eines Drei‐Helix‐Bündels zu identifizieren, das durch Selbstinteraktion ein Kristallgitter mit spezifischer Geometrie bildete (Abbildung g) . Derselbe Ansatz wurde auch für die Entwicklung widerstandsfähiger zweidimensionaler helikaler Bündel verwendet, die Variationen der Lösungsmittelumgebung sowie chemische Modifikationen der Enden tolerierten …”

Section: Agglomeration Im Design Von Biomaterialienunclassified

Infinite Ansammlungen gefalteter Proteine im Kontext von Evolution, Krankheiten und Proteinentwicklung

2019

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Mutationen und Veränderungen in der Umgebung eines Proteins sind bekannt dafür, potenziell Fehlfaltungen und Aggregation wie Amyloidbildung zu verursachen. Derartige Einflüsse können allerdings auch neue Interaktionen bewirken, die zur Polymerisation gefalteter Proteine führen. Im Unterschied zur Aggregation können solche Vorgänge aber auch ohne Fehlfaltungen ablaufen. Um diesen Unterschied hervorzuheben, bezeichnen wir sie als Agglomeration. Dieser Begriff umfasst die amorphe Zusammenlagerung gefalteter Proteine wie auch deren ein‐, zwei‐ und dreidimensionale Polymerisation. Wir möchten auf die bemerkenswerte Fähigkeit symmetrischer Homooligomere hinweisen, sogar infolge einzelner Oberflächenmutationen zu agglomerieren. Wir erörtern des Weiteren die ambivalente Natur dieser Eigenschaft: Durch Agglomeration entstandene anomale Ansammlungen können einerseits zum Entstehen von Krankheiten beitragen, sind aber andererseits auch für die zelluläre Anpassung verantwortlich und können zudem für das zielgerichtete Design neuer Biomaterialien genutzt werden.

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“…Moreover, the Protein Data Bank contains numerous structures that crystallize within p3-related space groups that can be described in terms of layered, open-framework packing arrangements. Recently, computational design has been employed to optimize protein -protein interfaces within these structures to afford stable, free-standing two-dimensional assemblies of singlemolecule thickness [60], or, alternatively, to create synthetic protein tectons that are capable of self-associating selectively in such packing arrangements [19,58,61]. Perhaps an even greater challenge might be the intentional design of a peptide system that self-assembled into a nanosheet based on a 'frustrated' trigonal unit cell, such as a heterotrimeric system in which the three peptides had distinct sequences and were chemically and physically distinguishable within the two-dimensional assembly.…”

Section: Periodic Defect Lattice Formation In Helical Nanosheet Assemmentioning

confidence: 99%

Geometrical frustration as a potential design principle for peptide-based assemblies

Jiang¹,

Magnotti²,

Conticello³

2017

Interface Focus.

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Two-dimensional peptide and protein assemblies have been the focus of increased scientific research as they display significant potential for the creation of functional nanomaterials. Soluble subunits derived from a variety of protein motifs have been demonstrated to self-assemble into structurally defined nanosheets under environmentally benign conditions in which the components often retain their native structure and function. These types of two-dimensional assemblies may have an advantage for nanofabrication in that their extended planar shapes can be more straightforwardly incorporated into the current formats of nanoscale devices. However, significant challenges remain in the fabrication of these materials, particularly in devising methods to control the size, shape and internal structure of the resultant materials. Geometrical frustration may be envisioned as a possible mechanism to exert control over these structural parameters through rational design. While this objective has yet to be realized in practice, we discuss in this article the potential role of geometrical frustration as a principle to rationalize unusual self-assembly behaviour in several examples of two-dimensional peptide assemblies.

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Computationally designed peptides for self-assembly of nanostructured lattices

Abstract: Peptide lattices were designed using computational methods and controlled by tuning self-assembly solution conditions.

Cited by 68 publications

References 52 publications

Infinite Assembly of Folded Proteins in Evolution, Disease, and Engineering

Infinite Assembly of Folded Proteins in Evolution, Disease, and Engineering

Infinite Ansammlungen gefalteter Proteine im Kontext von Evolution, Krankheiten und Proteinentwicklung

Geometrical frustration as a potential design principle for peptide-based assemblies

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