V. K. Rumyantseva, S. N. Morozkina, M. V. Uspenskaya, M. G. Petukhov
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引用次数: 0
Abstract
Using the results of virtual ligand screening (VLS) of a representative set of 66834 commercially available drug-like ligands and 8400 di- and tripeptides in the central cavity of Transthyretin (TTR) amyloid fibrils, it has been shown that despite the great chemical diversity, among commercially available drug-like organic compounds and ultrashort peptides (USPs), only 7 USPs are able to bind in the central cavity of TTR amyloid fibrils, thus preventing the growth of amyloid fibrils. The results of VLS also show that the relaxation of ligand steric strains in the obtained complexes not only significantly improves docking scores but also radically (>50%) changes the main result of VLS, the molecular composition of 1% of the best ligands. Thus, the relaxation of steric strains after VLS can more than double the effectiveness of VLS in the development of new drugs.
期刊介绍：
The journal publishes papers on vast aspects of cell research, including morphology, biochemistry, biophysics, genetics, molecular biology, immunology. The journal accepts original experimental studies, theoretical articles suggesting novel principles and approaches, presentations of new hypotheses, reviews highlighting major developments in cell biology, discussions. The main objective of the journal is to provide a competent representation and integration of research made on cells (animal and plant cells, both in vivo and in cell culture) offering insight into the structure and functions of live cells as a whole. Characteristically, the journal publishes articles on biology of free-living and parasitic protists, which, unlike Metazoa, are eukaryotic organisms at the cellular level of organization.
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