Scanning Electron Microscope Imaging of Amyloid Fibrils

Takai,

doi:10.3844/ajbbsp.2014.31.39

Cited by 20 publications

(7 citation statements)

References 35 publications

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“…From a supramolecular perspective, several nanoscale microscopy techniques, such as AFM [29], TEM [30], STM [31], and SEM [32], can provide compelling images that reveal fine nanostructure detail. Nowadays even light microscopy can be a useful tool in the field of nanomaterials thanks to the realization of super-resolution instrumentation to unveil features in the relatively remarkably high resolution of a few tens of nanometers [33].…”

Section: Characterization Of Compounds Bearing the Phe-phe Motifmentioning

confidence: 99%

The Phe-Phe Motif for Peptide Self-Assembly in Nanomedicine

2015

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Abstract:Since its discovery, the Phe-Phe motif has gained in popularity as a minimalist building block to drive the self-assembly of short peptides and their analogues into nanostructures and hydrogels. Molecules based on the Phe-Phe motif have found a range of applications in nanomedicine, from drug delivery and biomaterials to new therapeutic paradigms. Here we discuss the various production methods for this class of compounds, and the characterization, nanomorphologies, and application of their self-assembled nanostructures. We include the most recent findings on their remarkable properties, which hold substantial promise for the creation of the next generation nanomedicines.

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Section: Characterization Of Compounds Bearing the Phe-phe Motifmentioning

confidence: 99%

The Phe-Phe Motif for Peptide Self-Assembly in Nanomedicine

2015

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“…The formation of amyloid protein deposition is associated with more than 20 human disorders, as for example Alzheimer’s disease, Parkinson’s disease, type II diabetes, and prion disorders [ 1 , 2 ]. The amyloid fibrils, which have a diameter less than 10 nm, are assemblies with a high degree of order along the long axis of the fibril, as has been observed by atomic force microscopy (AFM), transmission electron microscopy (TEM), and scanning electron microscopy (SEM) [ 3 , 4 , 5 ]. The order of the fibrils is also reflected in their typical green-gold birefringence when examined between cross-polarizers upon staining with the Congo Red dye.…”

Section: Introductionmentioning

confidence: 99%

Revisiting the Self-Assembly of Highly Aromatic Phenylalanine Homopeptides

Mayans

Alemán

2020

Molecules

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Diphenylalanine peptide (FF), which self-assembles into rigid tubular nanostructures, is a very short core recognition motif in Alzheimer’s disease β-amyloid (Aβ) polypeptide. Moreover, the ability of the phenylalanine (F or Phe)-homopeptides to self-assemble into ordered nanostructures has been proved. Within this context it was shown that the assembly preferences of this family of compounds is altered by capping both the N- and C-termini using highly aromatic fluorenyl groups (i.e., fluorenyl-9-methoxycarbonyl and 9-fluorenylmethyl ester, named Fmoc and OFm, respectively). In this article the work performed in the field of the effect of the structure and incubation conditions on the morphology and polymorphism of short (from two to four amino acid residues) Phe-homopeptides is reviewed and accompanied by introducing some new results for completing the comparison. Special attention has been paid to the influence of solvent: co-solvent mixture used to solubilize the peptide, the peptide concentration and, in some cases, the temperature. More specifically, uncapped (FF, FFF, and FFFF), N-capped with Fmoc (Fmoc-FF, Fmoc-FFF, and Fmoc-FFFF), C-capped with OFm (FF-OFm), and doubly capped (Fmoc-FF-OFm, Fmoc-FFF-OFm, and Fmoc-FFFF-OFm) Phe-homopeptides have been re-measured. Although many of the experienced assembly conditions have been only revisited as they were previously reported, other experimental conditions have been examined by the first time in this work. In any case, pooling the effect of highly aromatic blocking groups in a single study, using a wide variety of experimental conditions, allows a perspective of how the disappearance of head-to-tail electrostatic interactions and the gradual increase in the amount of π–π stacking interactions, affects the morphology of the assemblies. Future technological applications of Phe-homopeptides can be envisaged by choosing the most appropriate self-assemble structure, defining not only the length of the peptide but also the amount and the position of fluorenyl capping groups.

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“…In previous studies, formation of lysozyme amyloid fibrils at low concentrations in an aqueous environment has been examined by using heat, low pH, ionic elements and stirring. 12,13 Herein, lysozyme amyloid fibril has been produced using self-assembly method under harsh environment, providing a natural/biological template for the hybrid scaffold. To monitor the efficiency of interaction with amyloid fibrils, assembly of pristine and PSS-modified plasmonic nanostructures of gold with rod morphology (GNRs) was monitored on the nanoscaffold.…”

Section: Introductionmentioning

confidence: 99%

Surface Functionalization of Gold Nanorods Improves Nanostructure Assemblies on Amyloid Fibril Scaffolds

Salimian

Moghadam

Ranjbar

2020

ACSi

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A hybrid scaffold containing gold nanorods and lysozyme amyloid fibrils has been fabricated, and the effect of surface modification on improving nanostructure assembly on the biological template has been investigated. The nanohybrid system was characterized by monitoring surface plasmon resonance bands, dynamic light scattering spectroscopy, Thioflavin-T assay, and transmission electron microscopy. Surface of gold nanorods (GNRs) was modified with polystyrene sulfonate (PSS), and possible difference in assembly of the pristine and modified nanostructures was compared upon interaction with amyloid fibrils. Analysis of transmission electron microscopy showed that changing the surface charge of GNRs with biocompatible polymer improved electrostatic interactions between the nanostructures and amyloid fibril templates. Analysis of cell viability assays also showed that surface functionalization of GNRs remarkably improved biocompatibility of the nanoscaffold. Results of this study encourage utilization of modification strategies to fabricate a new generation of nanoscaffolds with fruitful applications in regenerative medicine.

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Scanning Electron Microscope Imaging of Amyloid Fibrils

Cited by 20 publications

References 35 publications

The Phe-Phe Motif for Peptide Self-Assembly in Nanomedicine

The Phe-Phe Motif for Peptide Self-Assembly in Nanomedicine

Revisiting the Self-Assembly of Highly Aromatic Phenylalanine Homopeptides

Surface Functionalization of Gold Nanorods Improves Nanostructure Assemblies on Amyloid Fibril Scaffolds

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