Self-assembling DNA–peptide hybrids: morphological consequences of oligonucleotide grafting to a pathogenic amyloid fibrils forming dipeptide

2012 ◽  
Vol 48 (44) ◽  
pp. 5440 ◽  
Author(s):  
Nidhi Gour ◽  
Dawid Kedracki ◽  
Ilyès Safir ◽  
Kien Xuan Ngo ◽  
Corinne Vebert-Nardin
Keyword(s):  
Amyloid Fibrils ◽  
Self Assembling

scholarly journals Trehalose Effect on The Aggregation of Model Proteins into Amyloid Fibrils

Life ◽  
2020 ◽  
Vol 10 (5) ◽  
pp. 60
Author(s):  
Eleonora Mari ◽  
Caterina Ricci ◽  
Silvia Pieraccini ◽  
Francesco Spinozzi ◽  
Paolo Mariani ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Amyloid Fibrils ◽  
Uv Spectroscopy ◽  
Slowing Down ◽  
Self Assembling ◽  
X Ray Scattering ◽  
Key Factor ◽  
Plausible Mechanism ◽  
Protein Fibrillation ◽  
Reported Data

Protein aggregation into amyloid fibrils is a phenomenon that attracts attention from a wide and composite part of the scientific community. Indeed, the presence of mature fibrils is associated with several neurodegenerative diseases, and in addition these supramolecular aggregates are considered promising self-assembling nanomaterials. In this framework, investigation on the effect of cosolutes on protein propensity to aggregate into fibrils is receiving growing interest, and new insights on this aspect might represent valuable steps towards comprehension of highly complex biological processes. In this work we studied the influence exerted by the osmolyte trehalose on fibrillation of two model proteins, that is, lysozyme and insulin, investigated during concomitant variation of the solution ionic strength due to NaCl. In order to monitor both secondary structures and the overall tridimensional conformations, we have performed UV spectroscopy measurements with Congo Red, Circular Dichroism, and synchrotron Small Angle X-ray Scattering. For both proteins we describe the effect of trehalose in changing the fibrillation pattern and, as main result, we observe that ionic strength in solution is a key factor in determining trehalose efficiency in slowing down or blocking protein fibrillation. Ionic strength reveals to be a competitive element with respect to trehalose, being able to counteract its inhibiting effects toward amyloidogenesis. Reported data highlight the importance of combining studies carried out on cosolutes with valuation of other physiological parameters that may affect the aggregation process. Also, the obtained experimental results allow to hypothesize a plausible mechanism adopted by the osmolyte to preserve protein surface and prevent protein fibrillation.

Computational design of amyloid self-assembling peptides bearing aromatic residues and the cell adhesive motif Arg-Gly-Asp

2017 ◽  
Vol 2 (3) ◽  
pp. 321-335 ◽  
Author(s):  
Sai Vamshi R. Jonnalagadda ◽  
Eirini Ornithopoulou ◽  
Asuka A. Orr ◽  
Estelle Mossou ◽  
V. Trevor Forsyth ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Computational Design ◽  
Aromatic Residues ◽  
Self Assembling ◽  
Cell Adhesive

FESEM picture of the amyloid fibrils formed by the computationally designed self-assembling peptide RGDSGAITIGY.

scholarly journals The Human LL-37(17-29) Antimicrobial Peptide Reveals a Functional Supramolecular Nanostructure

2020 ◽  
Author(s):  
Yizhaq Engelberg ◽  
Meytal Landau
Keyword(s):  
Lipid Bilayers ◽  
Self Assembly ◽  
Amyloid Fibrils ◽  
Biological Activities ◽  
Building Blocks ◽  
Bacterial Cells ◽  
Bacterial Membranes ◽  
Self Assembling ◽  
Wide Ribbon ◽  
Wide Range

Protein fibrils that perform biological activities present attractive biomaterials. Here we demonstrate, by crystal structures, the self-assembly of the antibacterial human LL-37 active core (residues 17-29) into a stable structure of densely packed helices. The surface of the fibril encompasses alternating hydrophobic and positively charged zigzagged belts, which likely underlie interactions with and subsequent disruption of negatively charged lipid bilayers, such as bacterial membranes. LL-3717-29 correspondingly formed wide, ribbon-like, thermostable fibrils in solution, which co-localized with bacterial cells, and structure-guided mutagenesis analyses supported the role of self-assembly in antibacterial activity. LL-3717-29 resembled, in sequence and in the ability to form amphipathic helical fibrils, the bacterial cytotoxic PSMα3 peptide that assembles into cross-α amyloid fibrils. This suggests helical, self-assembling, basic building blocks across kingdoms of life and point to potential structural mimicry mechanisms. The findings offer a scaffold for functional and durable nanostructures for a wide range of medical and technological applications.

Amyloid Fibrils – Self-Assembling Proteins

2009 ◽  
pp. 559-594 ◽  
Author(s):  
Victoria A. Hughes ◽  
Dave E. Dunstan
Keyword(s):  
Amyloid Fibrils ◽  
Self Assembling

scholarly journals Self-assembly of Functional Nanostructures by Short Helical Peptide Building Blocks

2019 ◽  
Vol 26 (2) ◽  
pp. 88-97 ◽  
Author(s):  
Santu Bera ◽  
Ehud Gazit
Keyword(s):  
Self Assembly ◽  
Amyloid Fibrils ◽  
Building Blocks ◽  
Smart Devices ◽  
Helical Peptides ◽  
Functional Roles ◽  
Mesoscale Structures ◽  
Self Assembling ◽  
Wide Range ◽  
Self Assembled

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.

Amyloid Fibrils: From Disease to Design. New Biomaterial Applications for Self-Assembling Cross-β Fibrils

2007 ◽  
Vol 60 (5) ◽  
pp. 333 ◽  
Author(s):  
Sally L. Gras
Keyword(s):  
Enzyme Immobilization ◽  
Amyloid Fibrils ◽  
Protein Aggregates ◽  
Supporting Cells ◽  
Cell Behaviour ◽  
Biomimetic Materials ◽  
Self Assembling ◽  
Recent Advances ◽  
Positive Functions

Amyloid fibrils are self-assembling protein aggregates. They are essentially insoluble and resilient nanofibres that offer great potential as materials for nanotechnology and bionanotechnology. Fibrils are associated with several debilitating diseases, for example Alzheimer’s disease, but recent advances suggest they also have positive functions in nature and can be formed in vitro from generic proteins. This article explores how the unique nanotopography and advantageous properties of fibrils may be used to develop tools for probing cell behaviour, protein-based biomimetic materials for supporting cells, or platforms for biosensors and enzyme immobilization.

Selective and stoichiometric incorporation of ATP by self-assembling amyloid fibrils

2021 ◽  
Author(s):  
Robert Dec ◽  
Wojciech Puławski ◽  
Wojciech Dzwolak
Keyword(s):  
Amyloid Fibrils ◽  
Self Assembling ◽  
Chimeric Peptide

The merger of insulin's amyloidogenic segment and an octalysine stretch produces a chimeric peptide with the ability to bind and incorporate stoichiometric amounts of ATP upon co-aggregation and formation of amyloid fibrils.

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