scholarly journals Impact of porous nanomaterials on inhibiting protein aggregation behaviour

RSC Advances ◽  
2021 ◽  
Vol 11 (6) ◽  
pp. 3354-3362
Author(s):  
Munmun Bardhan ◽  
Sandip Dolui ◽  
Siddhi Chaudhuri ◽  
Uttam Paul ◽  
Gaurav Bhattacharjee ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Physiological Conditions ◽  
Intrinsically Disordered ◽  
Aggregation Behaviour ◽  
Inhibiting Protein ◽  
Porous Nanomaterials

Aggregation of intrinsically disordered as well as the ordered proteins under certain premises or physiological conditions leads to pathological disorder.

The effects of rutin and troxerutin on stabilizing SOD1 and inhibiting protein aggregation

2020 ◽  
Vol 34 (6) ◽  
Author(s):  
Xiaoyu Zhuang ◽  
Bing Zhao ◽  
Zhiqiang Liu ◽  
Fengrui Song ◽  
Jianzhong Lu
Keyword(s):  
Protein Aggregation ◽  
Inhibiting Protein

scholarly journals A comparative study of silver nanoparticle dissolution under physiological conditions

2020 ◽  
Vol 2 (12) ◽  
pp. 5760-5768
Author(s):  
Lukas Steinmetz ◽  
Christoph Geers ◽  
Sandor Balog ◽  
Mathias Bonmarin ◽  
Laura Rodriguez-Lorenzo ◽  
...  
Keyword(s):  
Silver Nanoparticles ◽  
Comparative Study ◽  
Silver Nanoparticle ◽  
Biologically Relevant ◽  
Physiological Conditions ◽  
Aggregation Behaviour

The dissolution and aggregation behaviour of silver nanoparticles under physiological conditions and in biologically relevant environments is investigated by exploiting their plasmonic properties.

scholarly journals The C Terminus of the Ribosomal-Associated Protein LrtA is an Intrinsically Disordered Oligomer

2018 ◽  
Vol 19 (12) ◽  
pp. 3902 ◽  
Author(s):  
José L. Neira ◽  
A. Marcela Giudici ◽  
Felipe Hornos ◽  
Arantxa Arbe ◽  
Bruno Rizzuti
Keyword(s):  
Computational Modelling ◽  
Terminal Region ◽  
Physiological Conditions ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
C Terminus ◽  
Conformational Preferences ◽  
Self Association ◽  
Association Equilibrium ◽  
Post Stress

The 191-residue-long LrtA protein of Synechocystis sp. PCC 6803 is involved in post-stress survival and in stabilizing 70S ribosomal particles. It belongs to the hibernating promoting factor (HPF) family, intervening in protein synthesis. The protein consists of two domains: The N-terminal region (N-LrtA, residues 1101), which is common to all the members of the HPF, and seems to be well-folded; and the C-terminal region (C-LrtA, residues 102-191), which is hypothesized to be disordered. In this work, we studied the conformational preferences of isolated C-LrtA in solution. The protein was disordered, as shown by computational modelling, 1D-1H NMR, steady-state far- UV circular dichroism (CD) and chemical and thermal denaturations followed by fluorescence and far-UV CD. Moreover, at physiological conditions, as indicated by several biochemical and hydrodynamic techniques, isolated C-LrtA intervened in a self-association equilibrium, involving several oligomerization reactions. Thus, C-LrtA was an oligomeric disordered protein.

scholarly journals Catechol-Containing Compounds are a Broad Class of Protein Aggregation Inhibitors: Redox State is a Key Determinant of the Inhibitory Activities

2020 ◽  
Author(s):  
Paul Velander ◽  
Ling Wu ◽  
Sherry B. Hildreth ◽  
Nancy J. Vogelaar ◽  
Biswarup Mukhopadhyay ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Small Molecule ◽  
Rational Design ◽  
Redox State ◽  
Broad Class ◽  
Intrinsically Disordered ◽  
Amyloidogenic Proteins ◽  
Key Factor ◽  
Inhibitory Activities ◽  
Screening Platform

Abstract Background: A range of neurodegenerative and related aging diseases, such as Alzheimer’s disease, Parkinson’s disease, and type 2 diabetes, are linked to toxic protein aggregation. Yet the mechanisms of protein aggregation inhibition by small molecule inhibitors remain poorly understood, in part because most protein targets of aggregation assembly are partially unfolded or intrinsically disordered, which hinders detailed structural characterization of protein-inhibitor complexes and structural-based mechanistic elucidation. Methods: Herein we employed a small molecule screening approach to identify inhibitors against three prototype amyloidogenic proteins in neurodegeneration and related proteinopathies: amylin, Ab and tau. We further systematically investigated selected class of inhibitors under aerobic and anaerobic conditions to uncover a key determinant of the inhibitory activities.Results: One remarkable class of inhibitors identified from all three parallel screenings against different amyloidogenic proteins was catechol-containing compounds and redox-related quinones/anthraquinones. Further mechanistic studies determined that the redox state of the broad class of catechol-containing compounds is a key determinant of the amyloid inhibitor activities. Conclusion: Our small molecule library screening platform was able to identify a broad class of amyloid inhibitors. Redox was found to be a key factor not only regulating the inhibitory activities but also involving the mechanism of inhibition. The molecular insights we gained not only explain why a large number of catechol-containing natural compounds, often enriched in healthy diet, have anti-neurodegeneration and anti-aging activities, but also could guide the rational design of therapeutic or nutraceutical strategies to target a broad range of neurodegenerative and related aging diseases.

scholarly journals Intrinsically Disordered Proteins in Chronic Diseases

Biomolecules ◽  
2019 ◽  
Vol 9 (4) ◽  
pp. 147 ◽  
Author(s):  
Prakash Kulkarni ◽  
Vladimir Uversky
Keyword(s):  
Chronic Diseases ◽  
Intrinsically Disordered Proteins ◽  
Large Fraction ◽  
3D Structure ◽  
Human Proteome ◽  
Disordered Proteins ◽  
3D Structures ◽  
Physiological Conditions ◽  
Intrinsically Disordered

It is now increasingly evident that a large fraction of the human proteome comprises proteins that, under physiological conditions, lack fixed, ordered 3D structures as a whole or have segments that are not likely to form a defined 3D structure [...]

scholarly journals Sweeping Away Protein Aggregation with Entropic Bristles: Intrinsically Disordered Protein Fusions Enhance Soluble Expression

Biochemistry ◽  
2012 ◽  
Vol 51 (37) ◽  
pp. 7250-7262 ◽  
Author(s):  
Aaron A. Santner ◽  
Carrie H. Croy ◽  
Farha H. Vasanwala ◽  
Vladimir N. Uversky ◽  
Ya-Yue J. Van ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Intrinsically Disordered Protein ◽  
Soluble Expression ◽  
Intrinsically Disordered ◽  
Disordered Protein

NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near-Physiological Conditions

2013 ◽  
Vol 125 (45) ◽  
pp. 12024-12028 ◽  
Author(s):  
Sergio Gil ◽  
Tomáš Hošek ◽  
Zsofia Solyom ◽  
Rainer Kümmerle ◽  
Bernhard Brutscher ◽  
...  
Keyword(s):  
Intrinsically Disordered Proteins ◽  
Spectroscopic Studies ◽  
Disordered Proteins ◽  
Physiological Conditions ◽  
Intrinsically Disordered
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