Spectral and Structural Characterization of Two Ferric Coordination Modes of a Simple Bis(catecholamide) Ligand:  Metal-Assisted Self-Assembly in a Siderophore Analog

1996 ◽  
Vol 35 (10) ◽  
pp. 2719-2720 ◽  
Author(s):  
Eric J. Enemark ◽  
T. D. P. Stack
Keyword(s):  
Structural Characterization ◽  
Self Assembly ◽  
Coordination Modes ◽  
Siderophore Analog

Structural Characterization of a New Collagen Biomimetic Octapeptide with Nanoscale Self‐assembly Potential: Experimental and Theoretical Approaches

ChemPlusChem ◽  
2021 ◽  
Author(s):  
Cosmin Stefan Mocanu ◽  
Brindusa Alina Petre ◽  
Laura Darie Ion ◽  
Gabi Drochioiu ◽  
Marius Niculaua ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Self Assembly ◽  
Theoretical Approaches

scholarly journals Structural Characterization of the Hydrophobin SC3, as a Monomer and after Self-Assembly at Hydrophobic/Hydrophilic Interfaces

1998 ◽  
Vol 74 (4) ◽  
pp. 2059-2068 ◽  
Author(s):  
Marcel L. de Vocht ◽  
Karin Scholtmeijer ◽  
Eric W. van der Vegte ◽  
Onno M.H. de Vries ◽  
Nathalie Sonveaux ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Self Assembly

scholarly journals Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation

2015 ◽  
Vol 112 (16) ◽  
pp. E1994-E2003 ◽  
Author(s):  
Serene W. Chen ◽  
Srdja Drakulic ◽  
Emma Deas ◽  
Myriam Ouberai ◽  
Francesco A. Aprile ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Self Assembly ◽  
Protein Misfolding ◽  
Amyloid Fibril ◽  
Amyloid Formation ◽  
Image Reconstruction Techniques ◽  
Cryo Electron Microscopy ◽  
Amyloid Oligomers ◽  
Β Sheet

We describe the isolation and detailed structural characterization of stable toxic oligomers of α-synuclein that have accumulated during the process of amyloid formation. Our approach has allowed us to identify distinct subgroups of oligomers and to probe their molecular architectures by using cryo-electron microscopy (cryoEM) image reconstruction techniques. Although the oligomers exist in a range of sizes, with different extents and nature of β-sheet content and exposed hydrophobicity, they all possess a hollow cylindrical architecture with similarities to certain types of amyloid fibril, suggesting that the accumulation of at least some forms of amyloid oligomers is likely to be a consequence of very slow rates of rearrangement of their β-sheet structures. Our findings reveal the inherent multiplicity of the process of protein misfolding and the key role the β-sheet geometry acquired in the early stages of the self-assembly process plays in dictating the kinetic stability and the pathological nature of individual oligomeric species.

Influence of dicarboxylic acids on self-assembly process: Syntheses and structural characterization of new Ag(I) complexes derived from mixed ligands

Polyhedron ◽  
2009 ◽  
Vol 28 (14) ◽  
pp. 2983-2988 ◽  
Author(s):  
Di Sun ◽  
Geng-Geng Luo ◽  
Na Zhang ◽  
Jian-Hua Chen ◽  
Rong-Bin Huang ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Self Assembly ◽  
Dicarboxylic Acids ◽  
Assembly Process ◽  
Mixed Ligands

Synthesis and structural characterization of new dinuclear silver(I) complexes: Different coordination modes of substituted 1,2,4-triazine ligands

2011 ◽  
Vol 1006 (1-3) ◽  
pp. 324-329 ◽  
Author(s):  
Farzin Marandi ◽  
Nayyereh Hosseini ◽  
Harald Krautscheid ◽  
Daniel Lässig ◽  
Jörg Lincke ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Coordination Modes

scholarly journals Modulation of Amyloidogenic Protein Self-Assembly Using Tethered Small Molecules

2020 ◽  
Author(s):  
Emma Cawood ◽  
Nicolas Guthertz ◽  
Jessica Ebo ◽  
Theodoros Karamanos ◽  
Sheena E. Radford FRS ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Structural Characterization ◽  
Self Assembly ◽  
Molecular Mechanisms ◽  
Amyloid Fibrils ◽  
Fibril Formation ◽  
X Ray Crystallography ◽  
Starting Point ◽  
Amyloid Assembly

<p></p><p>Protein-protein interactions (PPIs) are involved in many of life’s essential biological functions yet are also an underlying cause of several human diseases, including amyloidosis. The modulation of PPIs presents opportunities to gain mechanistic insights into amyloid assembly, particularly through the use of methods which can trap specific intermediates for detailed study. Such information can also provide a starting point for drug discovery. Here, we demonstrate that covalently tethered small molecule fragments can be used to stabilize specific oligomers during amyloid fibril formation, facilitating the structural characterization of these assembly intermediates. We exemplify the power of covalent tethering using the naturally occurring truncated variant (ΔN6) of the human protein β2-microglobulin (β2m), which assembles into amyloid fibrils associated with dialysis-related amyloidosis. Using this approach, we have trapped tetramers formed by ΔN6 under conditions which would normally lead to fibril formation and found that the degree of tetramer stabilization depends on the site of the covalent tether and the nature of the protein-fragment interaction. The covalent protein-ligand linkage enabled structural characterization of these trapped oligomeric species using X-ray crystallography and NMR, providing insight into why tetramer stabilization inhibits amyloid assembly. Our findings highlight the power of “post-translational chemical modification" as a tool to study biological molecular mechanisms. </p><br><p></p>

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