Molecular nucleation mechanism and control strategy of crystal polymorphic selection.

Many human diseases are associated with the formation of protein coagulation, such as eye cataracts, amyotrophic lateral sclerosis, sickle cell anemia, and Alzheimer's disease.
, however, concentrated proteins have their uses: as crystals, they are used by structural biologists to clarify protein structures, or as delivery vehicles for drug applications. the physicochemical properties of
crystals vary significantly between the different forms or structures of the same macromolecules ("polymorphics") and determine their availability in a scientific or industrial environment.
in order to control emerging polymorphics, it is necessary to be familiar with the molecular level of the pathways that lead to various macro states and the mechanisms of control path selection.
, April 5, 2018, Beijing time, Nature published an article by Mike Sleutel of the Belgian Center for Structural Biology Research and Alexander E. S. Van Driesche of the University of The Alps in Grenoble , among others, entitled "Molecular nucleation mechanisms and control sstrategies for crystal polymorph"
team showed the polymorphic selectionthat that occurred in the initial stages of structure formation, as well as specific blocks based on each spatial group.
, the study demonstrated the control of the system by selectively forming the required polymorphics through fixed-point mutagenesis, in particular by adjusting intermolecular bonding or gel inoculation.
results are different from the current protein nucleation images because sub-stabilized dense liquids are not identified as crystalline precursors.
, on the contrary, the study observed a nucleated event driven by directional connections between subcritical clusters that have shown a degree of crystallization.
these insights demonstrate ways to control macromolecular phase changes, helping to develop protein-based drug delivery systems and macromolecular crystalology.
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