Hypothesis: Crystalline self-assemblies of diphenylalanine (FF) are since long back considered to be related to Alzheimer's disease. An improved understanding of the mechanism behind the formation of such structures can lead to strategies for investigating the dynamic processes of assembly and disassembly of FF.
Experiment: The assembly, disassembly and reassembly of FF crystals are influenced by the solvent composition and can be triggered by evaporation of solvent. In this work these processes are directly monitored, and the structures obtained are analyzed.
Findings: The role of the solvent for assembly, disassembly and reassembly of diphenylalanine crystals has been demonstrated. The initial crystal structure formed via self-assembly of FF monomers can be transformed into needle-like crystals and further to hollow hexagonal microtubes through evaporation of the solvent. It is shown that all the assembly-disassembly processes are spontaneous and driven by thermodynamics. It is also found that some of the crystalline structures exhibit optical waveguiding properties.
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http://dx.doi.org/10.1016/j.jcis.2021.04.062 | DOI Listing |
Dev Biol
December 2024
Stowers Institute for Medical Research, Kansas City, MO, 64110, USA; Howard Hughes Medical Institute, Stowers Institute for Medical Research, Kansas City, MO, 64110, USA. Electronic address:
The cell nuclei of Ophisthokonts, the eukaryotic supergroup defined by fungi and metazoans, is remarkable in the constancy of their double-membraned structure in both somatic and germ cells. Such remarkable structural conservation underscores common and ancient evolutionary origins. Yet, the dynamics of disassembly and reassembly displayed by Ophisthokont nuclei vary extensively.
View Article and Find Full Text PDFThe disassembly and reassembly of nucleosomes by histone chaperones is an essential activity during eukaryotic transcription elongation. This highly conserved process maintains chromatin integrity by transiently removing nucleosomes as barriers and then restoring them in the wake of transcription. While transcription elongation requires multiple histone chaperones, there is little understanding of how most of them function and why so many are required.
View Article and Find Full Text PDFAdv Exp Med Biol
November 2024
Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL, USA.
Eukaryotic genome is packaged into chromatin. Thus, transcription takes place in the context of chromatin that is an array of nucleosomes. Nucleosome poses a barrier for the gene regulatory factors to access DNA for transcription to occur.
View Article and Find Full Text PDFJ Mater Chem B
December 2024
Department of Chemical and Pharmaceutical Sciences, University of Trieste, Via. Giorgieri 1, 34127 Trieste, Italy.
Biochem Biophys Res Commun
November 2024
School of Life Science and Technology, ShanghaiTech University, Shanghai, China. Electronic address:
In mammalian cells, the Golgi apparatus undergoes fragmentation for its correct partition into two daughter cells during mitosis. Several Golgi structural proteins have been demonstrated to regulate Golgi disassembly/reassembly and spindle formation. However, it is largely unknown whether Golgi proteins mediate other major events in mitosis.
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