Self-Assembled Biophotonic Lasing Network Driven by Amyloid Fibrils in Microcavities

ACS Nano ◽  
2021 ◽  
Vol 15 (9) ◽  
pp. 15007-15016
Author(s):  
Chaoyang Gong ◽  
Zhen Qiao ◽  
Song Zhu ◽  
Wenjie Wang ◽  
Yu-Cheng Chen
Nano Letters ◽  
2008 ◽  
Vol 8 (6) ◽  
pp. 1736-1740 ◽  
Author(s):  
Mahiar Hamedi ◽  
Anna Herland ◽  
Roger H. Karlsson ◽  
Olle Inganäs

2021 ◽  
Vol 8 ◽  
Author(s):  
Peter Faller ◽  
Christelle Hureau

The self-assembly of peptides and proteins into amyloid fibrils and other aggregates are linked to several diseases. One of the most studied cases is the peptide amyloid-β (Aβ), found self-assembled in Alzheimer's disease patients' brains. In test tubes, assays with chemically synthesized or recombinant Aβ are widely investigated to understand the aggregation process and to find modulators, which could be of therapeutic interest. Experience over more than a decade in our laboratory through discussions with colleagues, expertly studying the literature, and as reviewers revealed to us the widely encountered difficulty to control the aggregation and obtain reproducible results in the test tube. However, this issue is scarcely reported and discussed in the publications, which we think hampers strongly the progress in this field and can deceive newcomers. Here, we describe the difficulty and potential reasons to obtain reproducible aggregation data and propose some guidelines for working with it.


2018 ◽  
Vol 24 (8) ◽  
pp. 5742-5747
Author(s):  
Madhihalli Basavaraju Divakara ◽  
Chunchanakuppe Renukaprasad Ravi Kumar ◽  
Narendra Reddy ◽  
Mysore Sridhar Santosh

Insulin resistance is considered to be the most common cause of type 2 diabetes (T2D) wherein pancreatic β-cells cosecrete islet amyloid polypeptide (IAPP) with insulin and forms amyloid fibrils at low concentrations. Localization of IAPP between the secretory vesicle membrane and the crystal inhibits IAPP fibrillation. Moreover, inhibition of monomeric insulin and lipid membranes accelerate the fibrillation of IAPP in vitro. The present work investigates the interactions in vitro between lipid-IAPP-insulin under amyloid disease state. Fluorescence microscopy is used to investigate insulin’s effect on fibrillation of IAPP and to study the interactions of crystalline insulin with lipids and IAPP but revealed no significant interaction between IAPP and insulin. However, stable insulin-IAPP interactions are apparent in larger assemblies of crystalline insulin or IAPP fibres favouring the chances of various physiological interactions between these two β-cell hormones. The atomic force microscopy and electron microscopy studies indicate that the assembling process of hIAPP fibre can be tuned by the large surface of insulin. Also, the morphology of self-assembled nanostructures of hIAPP is modulated by the effect of insulin. These results are expected to offer a greater understanding of the interactions between insulin, lipids and peptides paving new dimensions in amyloid disease based therapeutics.


2019 ◽  
Vol 26 (2) ◽  
pp. 88-97 ◽  
Author(s):  
Santu Bera ◽  
Ehud Gazit

The self-assembly of short peptide building blocks into well-ordered nanostructures is a key direction in bionanotechnology. The formation of β -sheet organizations by short peptides is well explored, leading to the development of a wide range of functional assemblies. Likewise, many natural proteinaceous materials, such as silk and amyloid fibrils, are based on β-sheet structures. In contrast, collagen, the most abundant protein in mammals, is based on helical arrangement. Similar to β-sheet structures, short helical peptides have been recently discovered to possess a diverse set of functionalities with the potential to fabricate artificial self-assembling materials. Here, we outline the functional roles of self-assembled nanostructures formed by short helical peptides and their potential as artificial materials. We focus on the association between self-assembled mesoscale structures and their material function and demonstrate the way by which this class of building blocks bears the potential for diverse applications, such as the future fabrication of smart devices.


Author(s):  
Jiyong Park ◽  
Byungnam Kahng ◽  
Wonmuk Hwang

Self-assembly of β-sheet forming peptides into filaments has drawn great interests in biomedical applications [1,2]; Hydrogels formed by filaments self-assembled from de novo designed peptides possess potential applications for cell culture scaffolds [3]. On the other hand, peptides derived from amyloidogenic proteins in neurodegenerative diseases such as Alzheimer’s and Parkinson’s also form similar β-sheet filaments in vitro. They share little sequence homology, yet filaments formed by these self-assembling peptides commonly have the cross-β structure, the key signature of the amyloid fibril. Detailed structural information of the self-assembled β-sheet filaments has been limited partly due to the difficulty in preparing ordered filament samples, and it has been only recently that solid-state nuclear magnetic resonance and x-ray techniques have revealed their molecular structure at the atomic level [4,5]. Although molecular structures of amyloid fibrils are becoming available, physical principles governing their self-assembly and the properties of the filaments are not well-understood, for which computational as well as theoretical approaches are desirable [6].


2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Gyudo Lee ◽  
Wonseok Lee ◽  
Hyungbeen Lee ◽  
Chang Young Lee ◽  
Kilho Eom ◽  
...  

Author(s):  
D.F. Clapin ◽  
V.J.A. Montpetit

Alzheimer's disease is characterized by the accumulation of abnormal filamentous proteins. The most important of these are amyloid fibrils and paired helical filaments (PHF). PHF are located intraneuronally forming bundles called neurofibrillary tangles. The designation of these structures as "tangles" is appropriate at the light microscopic level. However, localized domains within individual tangles appear to demonstrate a regular spacing which may indicate a liquid crystalline phase. The purpose of this paper is to present a statistical geometric analysis of PHF packing.


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