Intrinsic defect formation in peptide self-assembly

Deng, Li; Zhao, Yurong; Xu, Hai; Wang, Yanting

doi:10.1063/1.4927708

Cited by 6 publications

(3 citation statements)

References 29 publications

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“…The influence of r s , the attraction between neighboring layers, to the selfassembled morphology was calculated and discussed in the supplementary material. 30 Although most parts of our results qualitatively agree with Aggeli's model, since the primary layer in our model is allowed to deform, in agreement with the experimental observation, in regime 4 our model results in a tube-like structure with a defect (Fig. S2), rather than a twisted ribbon by Aggeli's model.…”

Section: -6951/2015/107(4)/043701/5supporting

confidence: 79%

Direct observation of closure domain wall mediated spin waves

Mozooni

McCord

2015

Applied Physics Letters

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The generation and guiding of spin waves from and by magnetic domain walls are demonstrated. The spin waves radiate from pinned and oscillating magnetic closure domain walls and propagate linearly along a narrow path formed by the surrounding 180° asymmetric Bloch domain walls. The propagating spin wave modes are directly visualized by time-resolved magneto-optical Kerr microscopy with picosecond temporal resolution. A linear relationship between excitation frequency, wavelength, and number of spin waves per domain exists. Independent of the field excitation frequency, a constant phase velocity of spin waves propagation is obtained. Spin waves characteristics can be tuned by varying the magnetic domain dynamics, allowing for variable spin wave characteristics with magnetic field characteristics and histories.

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Section: -6951/2015/107(4)/043701/5supporting

confidence: 79%

Direct observation of closure domain wall mediated spin waves

Mozooni

McCord

2015

Applied Physics Letters

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“…The increase in PSERS intensity after annealing can be attributed to several complementary effects. First, an apparently increased surface area [visible in SEM images (Figures bi–iii and S1)] provides more opportunity for probe molecule attachment − and potentially higher Raman signals. Second, as shown in Figure biv, there was an associated change in wettability from hydrophilic to less hydrophilic with increasing temperature, as mentioned earlier.…”

Section: Resultsmentioning

confidence: 99%

Structural Transition-Induced Raman Enhancement in Bioinspired Diphenylalanine Peptide Nanotubes

Almohammed

Fularz

Kanoun

et al. 2022

ACS Appl. Mater. Interfaces

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Semiconducting materials are increasingly proposed as alternatives to noble metal nanomaterials to enhance Raman scattering. We demonstrate that bioinspired semiconducting diphenylalanine peptide nanotubes annealed through a reported structural transition can support Raman detection of 10–7 M concentrations for a range of molecules including mononucleotides. The enhancement is attributed to the introduction of electronic states below the conduction band that facilitate charge transfer to the analyte molecule. These results show that organic semiconductor-based materials can serve as platforms for enhanced Raman scattering for chemical sensing. As the sensor is metal-free, the enhancement is achieved without the introduction of electromagnetic surface-enhanced Raman spectroscopy.

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“…[28,29] Many theoretical works have further demonstrated that the competition between the intra-and inter-sheet interactions determines the morphology of a laminated structure composed of cross-β sheets. [30][31][32] Quantitative information such as the bond stiffness and the compositions of the intermolecular forces is essential for understanding the nanomechanics and morphology of peptide nanostructures. Similar to covalent bond stiffness, the intermolecular bond stiffness is a measurement of the resistance offered by the structure to the deviation from its equilibrated structure stabilized by the non-covalent force.…”

Section: Introductionmentioning

confidence: 99%

Anisotropic formation mechanism and nanomechanics for the self-assembly process of cross- β peptides

et al. 2017

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Nanostructures self-assembled by cross-β peptides with ordered structures and advantageous mechanical properties have many potential applications in biomaterials and nanotechnologies. Quantifying the intra-and inter-molecular driving forces for peptide self-assembly at the atomistic level is essential for understanding the formation mechanism and nanomechanics of various morphologies of self-assembled peptides. We investigate the thermodynamics of the intra-and inter-sheet structure formations in the self-assembly process of cross-β peptide KIIIIK by means of steered molecular dynamics simulation combined with umbrella sampling. It is found that the mechanical properties of the intra-and inter-sheet structures are highly anisotropic with their intermolecular bond stiffness at the temperature of 300 K being 5.58 N/m and 0.32 N/m, respectively. This mechanical anisotropy comes from the fact that the intra-sheet structure is stabilized by enthalpy but the inter-sheet structure is stabilized by entropy. Moreover, the formation process of KIIIIK intra-sheet structure is cooperatively driven by the van der Waals (VDW) interaction between the hydrophobic side chains and the electrostatic interaction between the hydrophilic backbones, but that of the inter-sheet structure is primarily driven by the VDW interaction between the hydrophobic side chains. Although only peptide KIIIIK is studied, the qualitative conclusions on the formation mechanism should also apply to other cross-β peptides.

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Intrinsic defect formation in peptide self-assembly

Cited by 6 publications

References 29 publications

Direct observation of closure domain wall mediated spin waves

Direct observation of closure domain wall mediated spin waves

Structural Transition-Induced Raman Enhancement in Bioinspired Diphenylalanine Peptide Nanotubes

Anisotropic formation mechanism and nanomechanics for the self-assembly process of cross- β peptides

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