ChemInform Abstract: Biophysical Studies of the Amyloid β-Peptide: Interactions with Metal Ions and Small Molecules

ChemInform ◽  
2013 ◽  
Vol 44 (47) ◽  
pp. no-no
Author(s):  
Sebastian Waermlaender ◽  
Ann Tiiman ◽  
Axel Abelein ◽  
Jinghui Luo ◽  
Jyri Jarvet ◽  
...  
Keyword(s):  
Metal Ions ◽  
Small Molecules ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Peptide Interactions ◽  
Biophysical Studies

Biophysical Studies of the Amyloid β-Peptide: Interactions with Metal Ions and Small Molecules

ChemBioChem ◽  
2013 ◽  
Vol 14 (14) ◽  
pp. 1692-1704 ◽  
Author(s):  
Sebastian Wärmländer ◽  
Ann Tiiman ◽  
Axel Abelein ◽  
Jinghui Luo ◽  
Jyri Jarvet ◽  
...  
Keyword(s):  
Metal Ions ◽  
Small Molecules ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Peptide Interactions ◽  
Biophysical Studies

scholarly journals Peptide-tags for site-specific protein labelling in vitro and in vivo

2016 ◽  
Vol 12 (6) ◽  
pp. 1731-1745 ◽  
Author(s):  
Jonathan Lotze ◽  
Ulrike Reinhardt ◽  
Oliver Seitz ◽  
Annette G. Beck-Sickinger
Keyword(s):  
Metal Ions ◽  
Small Molecules ◽  
Protein Localization ◽  
Specific Protein ◽  
Site Specific ◽  
Protein Labelling ◽  
Peptide Interactions ◽  
Peptide Tags

Peptide-tag based labelling can be achieved by (i) enzymes (ii) recognition of metal ions or small molecules and (iii) peptide–peptide interactions and enables site-specific protein visualization to investigate protein localization and trafficking.

scholarly journals Conformational Regulation of Amyloid β-peptide by Lipid Membranes and Metal Ions

2010 ◽  
Vol 130 (4) ◽  
pp. 495-501 ◽  
Author(s):  
Takashi MIURA ◽  
Mayumi YODA ◽  
Chihiro TSUTSUMI ◽  
Kiyoko MURAYAMA ◽  
Hideo TAKEUCHI
Keyword(s):  
Metal Ions ◽  
Lipid Membranes ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Conformational Regulation

NMR Investigations of Amyloid-β Peptide Interactions with Propofol at Clinically Relevant Concentrations with and without Aqueous Halothane Solution

2010 ◽  
Vol 21 (4) ◽  
pp. 1303-1309 ◽  
Author(s):  
Pravat K. Mandal ◽  
Neel Sarovar Bhavesh ◽  
Virender S. Chauhan ◽  
Vincenzo Fodale
Keyword(s):  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Peptide Interactions

The Amyloid-β Peptide in Amyloid Formation Processes: Interactions with Blood Proteins and Naturally Occurring Metal Ions

2016 ◽  
Vol 57 (7-8) ◽  
pp. 674-685 ◽  
Author(s):  
Cecilia Wallin ◽  
Jinghui Luo ◽  
Jüri Jarvet ◽  
Sebastian K. T. S. Wärmländer ◽  
Astrid Gräslund
Keyword(s):  
Metal Ions ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Amyloid Formation ◽  
Formation Processes ◽  
Blood Proteins ◽  
Naturally Occurring

scholarly journals Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers

2021 ◽  
Vol 15 ◽  
Author(s):  
Ryan Limbocker ◽  
Roxine Staats ◽  
Sean Chia ◽  
Francesco S. Ruggeri ◽  
Benedetta Mannini ◽  
...  
Keyword(s):  
Small Molecules ◽  
Neuroblastoma Cells ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Human Neuroblastoma Cells ◽  
Human Neuroblastoma ◽  
Parkinson’S Diseases ◽  
Wide Range ◽  
Opposing Effects

The aberrant aggregation of proteins is a key molecular event in the development and progression of a wide range of neurodegenerative disorders. We have shown previously that squalamine and trodusquemine, two natural products in the aminosterol class, can modulate the aggregation of the amyloid-β peptide (Aβ) and of α-synuclein (αS), which are associated with Alzheimer’s and Parkinson’s diseases. In this work, we expand our previous analyses to two squalamine derivatives, des-squalamine and α-squalamine, obtaining further insights into the mechanism by which aminosterols modulate Aβ and αS aggregation. We then characterize the ability of these small molecules to alter the physicochemical properties of stabilized oligomeric species in vitro and to suppress the toxicity of these aggregates to varying degrees toward human neuroblastoma cells. We found that, despite the fact that these aminosterols exert opposing effects on Aβ and αS aggregation under the conditions that we tested, the modifications that they induced to the toxicity of oligomers were similar. Our results indicate that the suppression of toxicity is mediated by the displacement of toxic oligomeric species from cellular membranes by the aminosterols. This study, thus, provides evidence that aminosterols could be rationally optimized in drug discovery programs to target oligomer toxicity in Alzheimer’s and Parkinson’s diseases.

scholarly journals Erratum to: Probing of Various Physiologically Relevant Metals–Amyloid-β Peptide Interactions with a Lipid Membrane-Immobilized Protein Nanopore

2014 ◽  
Vol 247 (6) ◽  
pp. 531-531
Author(s):  
Alina Asandei ◽  
Sorana Iftemi ◽  
Loredana Mereuta ◽  
Irina Schiopu ◽  
Tudor Luchian
Keyword(s):  
Lipid Membrane ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Peptide Interactions
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