Structural Fractal Analysis of the Active Site of Acetylcholinesterase in Complexes with Huperzine A, Galantamine, and Donepezil. Issue 11 (6th August 2021)

• Record Type: Journal Article
• Authors: Grigorev, Veniamin Y.; Rasdolsky, Alexander N.; Grigoreva, Ludmila D.; Tinkov, Oleg V.
• Is Part Of: Molecular informatics. Volume 40:Issue 11(2021)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2021-08-06
• Subjects: AChE -- fractal dimension; Cheminformatics -- Periodicals; QSAR (Biochemistry) -- Periodicals; Structure-activity relationships (Biochemistry) -- Periodicals; Drugs -- Structure-activity relationships -- Periodicals; 615.19
• DOI: 10.1002/minf.202100127
• Languages: English
• ISSNs: 1868-1743

Abstract

Abstract: The fractal dimension (D) of the active site of hAChE in the unliganded state and as part of complexes with hyperzine A, galantamine, and donepezil is calculated using molecular interatomic‐distance histograms. Fractal matrices of structural changes (FMSCs) are formed by pairwise comparison of the values of D and by revealing the significance of their differences. FMSCs are found to be used to quantitatively estimate the changes in the structures of the molecules in various states. When analyzing FMSCs, we found that the most significant structural changes are related to the Glu202 amino acid residue. No structural perturbations are revealed in the case of Trp86, Gly122, Ala204, Phe338, Tyr341, Gly448, and Ile451. Abstract :