Effects of mutations in de novo designed synthetic amphiphilic β-sheet peptides on self-assembly of fibrils

Atsmon-Raz, Yoav; Rubinov, Boris; Matmor, Maayan; Rapaport, Hanna; Ashkenasy, Gonen; Miller, Yifat

doi:10.1039/c3cc42879f

Cited by 32 publications

(35 citation statements)

References 40 publications

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“…Herein, we employed all-atom MD simulations, proven an effective technique to observe molecular order and dynamics of supramolecular systems 19 20 21 22 . While significant computational effort has been given to BTA assemblies in the gas phase 23 24 25 , and organic solvents 26 , very little atomistic-level work has been performed on any synthetic supramolecular fibres in water 20 , aside from peptide amphiphile structures 27 28 29 .…”

Section: Resultsmentioning

confidence: 99%

Consequences of chirality on the dynamics of a water-soluble supramolecular polymer

et al. 2015

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The rational design of supramolecular polymers in water is imperative for their widespread use, but the design principles for these systems are not well understood. Herein, we employ a multi-scale (spatial and temporal) approach to differentiate two analogous water-soluble supramolecular polymers: one with and one without a stereogenic methyl. Initially aiming simply to understand the molecular behaviour of these systems in water, we find that while the fibres may look identical, the introduction of homochirality imparts a higher level of internal order to the supramolecular polymer. Although this increased order does not seem to affect the basic dimensions of the supramolecular fibres, the equilibrium dynamics of the polymers differ by almost an order of magnitude. This report represents the first observation of a structure/property relationship with regard to equilibrium dynamics in water-soluble supramolecular polymers.

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Section: Resultsmentioning

confidence: 99%

Consequences of chirality on the dynamics of a water-soluble supramolecular polymer

et al. 2015

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“…Recently, the morphologies of the self-assembly of amphiphilic β-sheet peptides into various organizations have been investigated at high resolution. 37 …”

Section: Discussionmentioning

confidence: 99%

Polymorphism in Self-Assembly of Peptide-Based β-Hairpin Contributes to Network Morphology and Hydrogel Mechanical Rigidity

Miller¹,

Nussinov

2014

J. Phys. Chem. B

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Hydrogels are proving to be an excellent class of materials for biomedical applications. The molecular self-assembly of designed MAX1 β-hairpin peptides into fibrillar networks has emerged as a novel route to form responsive hydrogels. Herein, computational modeling techniques are used to investigate the relative arrangements of individual hairpins within the fibrils that constitute the gel. The modeling provides insight into the morphology of the fibril network, which defines the gel’s mechanical properties. Our study suggests polymorphic arrangements of the hairpins within the fibrils; however, the relative populations and the relative conformational energies of the polymorphic arrangements show a preference toward an arrangement of hairpins where their turn regions are not capable of forming intermolecular interaction. Repulsive intramolecular electrostatic interactions appear to dictate the formation of fibrils with shorter, rather than longer, persistent lengths. These repulsive intramolecular interactions also disfavor the formation of fibril entanglements. Taken together, the modeling predicts that MAX1 forms a network containing a large number of branch points, a network morphology supported by the formation of short fibril segments. We posit that, under static conditions, the preferred branched structures of the MAX1 peptide assembly result in a cross-linked hydrogel organization. At the same time, the shear stress leads to short fibrillar structures, thus fluidic hydrogel states.

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“…Significant differences were,however,found in the Cotton effect peaks at 300-400 nm that correspond to the polarized transition along the NDI moiety z axis. [11] . a) Molecular structures of the P NDI and KFE-8 peptides.…”

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confidence: 90%

“…MD simulationsw ere performed in the NPT ensemble at 310 Kf or 80 ns, using the NAMD program with all-atom CHARMM27 force-field( see the Supporting Information). [11] . Figure 2.…”

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The Strong Influence of Structure Polymorphism on the Conductivity of Peptide Fibrils

et al. 2016

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Peptide fibril nanostructures have been advocated as components of future biotechnology and nanotechnology devices. However, the ability to exploit the fibril functionality for applications, such as catalysis or electron transfer, depends on the formation of well-defined architectures. Fibrils made of peptides substituted with aromatic groups are described presenting efficient electron delocalization. Peptide self-assembly under various conditions produced polymorphic fibril products presenting distinctly different conductivities. This process is driven by a collective set of hydrogen bonding, electrostatic, and π-stacking interactions, and as a result it can be directed towards formation of a distinct polymorph by using the medium to enhance specific interactions rather than the others. This method facilitates the detailed characterization of different polymorphs, and allows specific conditions to be established that lead to the polymorph with the highest conductivity.

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Effects of mutations in de novo designed synthetic amphiphilic β-sheet peptides on self-assembly of fibrils

Cited by 32 publications

References 40 publications

Consequences of chirality on the dynamics of a water-soluble supramolecular polymer

Consequences of chirality on the dynamics of a water-soluble supramolecular polymer

Polymorphism in Self-Assembly of Peptide-Based β-Hairpin Contributes to Network Morphology and Hydrogel Mechanical Rigidity

The Strong Influence of Structure Polymorphism on the Conductivity of Peptide Fibrils

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