Biomolecular interfaces based on self-assembly and self-recognition form biosensors capable of recording molecular binding and release

Nanoscale ◽  
2019 ◽  
Vol 11 (11) ◽  
pp. 4987-4998 ◽  
Author(s):  
Xiao Hu ◽  
Anthony Guiseppi-Elie ◽  
Cerasela Zoica Dinu

Cellular components manipulated in a synthetic environment form a biosensor capable of evaluating association and dissociation as related to molecular self-recognition and self-assembly.

Author(s):  
Maarten C Hardenberg ◽  
Tessa Sinnige ◽  
Sam Casford ◽  
Samuel Dada ◽  
Chetan Poudel ◽  
...  

Abstract Misfolded α-synuclein is a major component of Lewy bodies, which are a hallmark of Parkinson’s disease. A large body of evidence shows that α-synuclein can aggregate into amyloid fibrils, but the relationship between α-synuclein self-assembly and Lewy body formation remains unclear. Here we show, both in vitro and in a Caenorhabditis elegans model of Parkinson’s disease, that α-synuclein undergoes liquid‒liquid phase separation by forming a liquid droplet state, which converts into an amyloid-rich hydrogel with Lewy-body-like properties. This maturation process towards the amyloid state is delayed in the presence of model synaptic vesicles in vitro. Taken together, these results suggest that the formation of Lewy bodies may be linked to the arrested maturation of α-synuclein condensates in the presence of lipids and other cellular components.


Langmuir ◽  
2020 ◽  
Vol 36 (35) ◽  
pp. 10519-10527
Author(s):  
Jiahui Chen ◽  
Kun Qian ◽  
Kexing Xiao ◽  
Jiancheng Luo ◽  
Hui Li ◽  
...  

2007 ◽  
Vol 9 (8) ◽  
pp. 1561-1564 ◽  
Author(s):  
Hai-Bo Yang ◽  
Koushik Ghosh ◽  
Brian H. Northrop ◽  
Peter J. Stang

1994 ◽  
Vol 116 (16) ◽  
pp. 7064-7071 ◽  
Author(s):  
Federica Ciuchi ◽  
Giovanni Di Nicola ◽  
Hermann Franz ◽  
Giovanni Gottarelli ◽  
Paolo Mariani ◽  
...  

2014 ◽  
Vol 70 (a1) ◽  
pp. C546-C546
Author(s):  
Anna Kupka ◽  
Hermann Gies ◽  
Klaus Merz

The famous Miller experiment to model the primordial soup demonstrated that amino acids can form spontaneously as the essential building blocks of life in solutions. It is, however, still an open question how self-recognition processes influence the transformation of these spontaneously formed amino acids in solvents into higher ordered structures in the solid state, thereby creating chiral materials and catalytically competent structures. The understanding of the first steps of molecular self-assembly processes in such environments will thus give important clues towards the understanding of biological evolution. Most of intermolecular interactions are not very strong and their formation is related to and affected by small changes in the molecular structure and the crystallisation conditions. Continuing our investigations on aggregation of substituted aromatic molecules in the solid state, we studied the influence and boundaries of weak directing substituents like deuterium on the aggregation of small molecules. Hydrogen/deuterium (H/D)-exchange, the smallest possible modification of a molecule, is generally seen as a non dominating parameter in the formation of crystal structures of chemical compounds. On the other hand, it could already be shown that the aggregation of molecules in the solid state of polymorphic N-heterocycle systems like pyridine-N-oxide or acridine can be very sensitive to small changes of the isotopic substitution pattern of the selected molecules. Within our project, the molecular aggregation of amino acids in solution with the formation of molecular aggregates and pre-nucleation clusters in deuterated and non-deuterated systems, and in particular the role of the solvent in these processes, will be studied in both experiment and theory.


Molecules ◽  
2021 ◽  
Vol 26 (5) ◽  
pp. 1219
Author(s):  
Andrea Caporale ◽  
Simone Adorinni ◽  
Doriano Lamba ◽  
Michele Saviano

The self-recognition and self-assembly of biomolecules are spontaneous processes that occur in Nature and allow the formation of ordered structures, at the nanoscale or even at the macroscale, under thermodynamic and kinetic equilibrium as a consequence of specific and local interactions. In particular, peptides and peptidomimetics play an elected role, as they may allow a rational approach to elucidate biological mechanisms to develop new drugs, biomaterials, catalysts, or semiconductors. The forces that rule self-recognition and self-assembly processes are weak interactions, such as hydrogen bonding, electrostatic attractions, and van der Waals forces, and they underlie the formation of the secondary structure (e.g., α-helix, β-sheet, polyproline II helix), which plays a key role in all biological processes. Here, we present recent and significant examples whereby design was successfully applied to attain the desired structural motifs toward function. These studies are important to understand the main interactions ruling the biological processes and the onset of many pathologies. The types of secondary structure adopted by peptides during self-assembly have a fundamental importance not only on the type of nano- or macro-structure formed but also on the properties of biomaterials, such as the types of interaction, encapsulation, non-covalent interaction, or covalent interaction, which are ultimately useful for applications in drug delivery.


ChemInform ◽  
2010 ◽  
Vol 31 (21) ◽  
pp. no-no
Author(s):  
Moshe Greenwald ◽  
Dana Wessely ◽  
Eugenii Katz ◽  
Itamar Willner ◽  
Yoram Cohen

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