The origin and reason for the homochirality of living cells go with the problem of a relatively narrow spectrum of the actual biological monomers compared to the whole theoretically possible spectrum of amino acids or carbohydrates. A limited number of bio-monomers implies some special feature differing from all other similar molecules that are not present in the living cell. Here we propose one of the candidates for such a peculiarity: the ability to form highly elongated helical supramolecular structures (strings) when precipitating from homochiral solutions. The strings' forming can be accompanied by spontaneous splitting and/or chiral purification of the initially racemic mixture. Our previous theoretical reasoning was based mainly on the biomimetic systems, while now we describe the strings forming in homochiral amino acid solutions.
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http://dx.doi.org/10.1007/s11084-022-09620-z | DOI Listing |
Sci Total Environ
January 2025
Department of Chemical Engineering, Tennessee Technological University, Cookeville, TN, United States. Electronic address:
The overall objective of the present work was to quantify how shear, coupled with varying salt concentration, affected the particle size distribution and relaxation/aggregation behavior for various organic sources of nonliving natural organic matter (NNOM) in surface water. NNOM has been implicated as a conditioning agent leading to the formation of biofilms such as algae. NNOM is also a responsible in surface waters for facilitated transport of a variety of anthropogenic pollutants.
View Article and Find Full Text PDFAdv Colloid Interface Sci
January 2025
Pharmaceutical Sciences Laboratory, Faculty of Science and Engineering, Åbo Akademi University, Biocity (3rd fl.), Tykistökatu 6A, 20520 Turku, Finland; Turku Bioscience Centre, University of Turku and Åbo Akademi University, Biocity (5th fl.), Tykistökatu 6A, 20520 Turku, Finland. Electronic address:
In the realm of hybrid nanomaterials, the construction of core/shell nanoparticles offer an effective strategy for encompassing a particle by a polymeric or other suitable material, leading to a nanocomposite with distinct features within its structure. The polymer shell can be formed via nanoprecipitation, optimized by manipulating fluid flow, fluid mixing, modulating device features in microfluidics. In addition to the process optimization, success of polymer assembly in encapsulation strongly lies upon the favorable molecular interactions originating from the diverse chemical environment shared between core and shell materials facilitating formation of core/shell nanostructure.
View Article and Find Full Text PDFJ Am Chem Soc
January 2025
Department of Chemistry and Chemical Biology, TU Dortmund University, Otto-Hahn Str. 6, 44227 Dortmund, Germany.
Dynamically interconvertible metallo-supramolecular multicomponent assemblies, coexisting orthogonally in solution, serve as simplified mimics for complex networks found in biological systems. Building on recent advances in controlling the nonstatistical self-assembly of heteroleptic coordination cages and heteromeric completive self-sorting, i.e.
View Article and Find Full Text PDFNano Lett
January 2025
Zhejiang Engineering Research Center for Tissue Repair Materials and Wenzhou Key Laboratory of Biomaterials and Engineering and Wenzhou Key Laboratory of Biophysics, Wenzhou Institute, University of Chinese Academy of Sciences, Wenzhou 325001, China.
Saccharides and peptides with markedly disparate stereochemical features serve as pivotal chiral molecular partners in living systems. The importance of glycosylation in influencing glycopeptide self-assembly has been recognized. However, how different chiral combinations of saccharides and peptides influence the macroscopic hydrogel mechanics, fiber nanomechanics, asymmetric molecular packing, and thermodynamic changes during glycopeptide self-assembly remains unknown.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
January 2025
Technische Universität München, Division of Peptide Biochemistry, Emil-Erlenmeyer-Forum 5, 85354, Freising, GERMANY.
Amyloid self-assembly of α-synuclein (αSyn) is linked to the pathogenesis of Parkinson's disease (PD). Type 2 diabetes (T2D) has recently emerged as a risk factor for PD. Cross-interactions between their amyloidogenic proteins may act as molecular links.
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