Dataset Information

Amyloid Peptide Mixtures: Self-Assembly, Hydrogelation, Nematic Ordering, and Catalysts in Aldol Reactions.

ABSTRACT: Morphological, spectroscopic, and scattering studies of the self-assembly and aggregation of mixtures of [RF]4 and P[RF]4 peptides (where R = arginine; F = phenylalanine; P = proline), in solution and as hydrogels, were performed to obtain information about polymorphism. CD data confirmed a ?-sheet secondary structure in aqueous solution, and TEM images revealed nanofibers with diameters of ?10 nm and micrometer lengths. SAXS curves were fitted using a mass fractal-component and a long cylinder shell form factor for the liquid samples, and only a long cylinder shell form factor for the gels. Increasing the P[RF]4 content in the systems leads to a reduction in cylinder radius and core scattering density, suggesting an increase in packing of the peptide molecules; however, the opposite effect is observed for the gels, where the scattering density is higher in the shell for the systems containing higher P[RF]4 content. These compounds show potential as catalysts in the asymmetric aldol reactions, with cyclohexanone and p-nitrobenzaldehyde in aqueous media. A moderate conversion (36.9%) and a good stereoselectivity (69:31) were observed for the system containing only [RF]4. With increasing P[RF]4 content, a considerable decrease of the conversion was observed, suggesting differences in the self-assembly and packing factor. Rheological measurements were performed to determine the shear moduli for the soft gels.

SUBMITTER: Pelin JNBD

PROVIDER: S-EPMC7146849 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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Publications

Amyloid Peptide Mixtures: Self-Assembly, Hydrogelation, Nematic Ordering, and Catalysts in Aldol Reactions.

Pelin Juliane N B D JNBD Gerbelli Barbara B BB Edwards-Gayle Charlotte J C CJC Aguilar Andrea M AM Castelletto Valeria V Hamley Ian W IW Alves Wendel A WA

Langmuir : the ACS journal of surfaces and colloids 20200312 11

Morphological, spectroscopic, and scattering studies of the self-assembly and aggregation of mixtures of [RF]<sub>4</sub> and P[RF]<sub>4</sub> peptides (where R = arginine; F = phenylalanine; P = proline), in solution and as hydrogels, were performed to obtain information about polymorphism. CD data confirmed a β-sheet secondary structure in aqueous solution, and TEM images revealed nanofibers with diameters of ∼10 nm and micrometer lengths. SAXS curves were fitted using a mass fractal-componen ...[more]

PMID: 32131599

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Project description:We report an investigation of the self-assembly of the monosialoganglioside (GM(1)) at interfaces formed between aqueous solutions of 10 microM GM(1) (at 25 degrees C) and micrometer-thick films of the nematic liquid crystal (LC) 4'-pentyl-4-cyanobiphenyl (5CB). We observe the process of spontaneous transfer of GM(1) onto the interfaces to be accompanied by continuous ordering transitions within the micrometer-thick films of the LC. At saturation coverage, the GM(1) orders the LC in an orientation that is perpendicular to the interface, an orientation that is similar to that caused by phospholipids such as dilauroylphosphatidylcholine (DLPC). This result suggests an interaction between the LC and GM(1) that is dominated by the hydrophobic tails of the GM(1). Relative to DLPC, however, we observe the dynamics of the LC ordering transition driven by GM(1) to be slow (2 h for DLPC versus 100 h for GM(1)). To provide insight into the origins of the slow dynamics of the GM(1)-induced ordering transition in the LC, we performed two additional measurements. First, we quantified the time-dependent adsorption of GM(1) at the LC interface by using fluorescently-labeled GM(1). Second, we used the Langmuir-Schaefer method to transfer preorganized monolayers of GM(1) from an air-water interface to the aqueous-LC interface. Results obtained from these two experiments are consistent with a physical picture in which the final stages of spontaneous adsorption/ordering of GM(1) at the aqueous-LC interface dictate the dynamics of the LC ordering transition. This rate limiting process underlying the ordering transition was substantially accelerated by heating the system above the phase transition temperature of GM(1)(26 degrees C), suggesting that the phase state of the GM(1) micellar aggregates in bulk solution strongly influences the kinetics of the final stages of ordering/adsorption of GM(1) at the LC interface. Overall, these results and others presented in this manuscript reveal that it is possible to decorate interfaces of a nematic LC with GM(1), and that the assembly of GM(1) at these interfaces impacts the dynamic and equilibrium ordering of the LC.

Dataset Information

Amyloid Peptide Mixtures: Self-Assembly, Hydrogelation, Nematic Ordering, and Catalysts in Aldol Reactions.

Publications

Amyloid Peptide Mixtures: Self-Assembly, Hydrogelation, Nematic Ordering, and Catalysts in Aldol Reactions.

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