NDLI: Quantum chemical study of silanediols as metal binding groups for metalloprotease inhibitors

Content Provider	Springer Nature Link
Author	Ignatyev, Igor S. Montejo, Manuel Rodríguez Ortega, Pilar Gema González, Juan Jesús López
Copyright Year	2013
Abstract	DFT (B3LYP and M06L) as well as ab initio (MP2) methods with Dunning cc-pVnZ (n = 2,3) basis sets are employed for the study of the binding ability of the new class of protease inhibitors, i.e., silanediols, in comparison to the well-known and well-studied class of inhibitors with hydroxamic functionality (HAM). Active sites of metalloproteases are modeled by [R3M-OH2]2+ complexes, where R stands for ammonia or imidazole molecules and M is a divalent cation, namely zinc, iron or nickel (in their different spin states). The inhibiting activity is estimated by calculating Gibbs free energies of the water displacement by metal binding groups (MBGs) according to: [R3M-OH2]2+ + MBG → [R3M-MBG]2+ + H2O. The binding energy of silanediol is only a few kcal mol−1 inferior to that of HAM for zinc and iron complexes and is even slightly higher for the triplet state of the (NH3)3Ni2+ complex. For both MBGs studied in the ammonia model the binding ability is nearly the same, i.e., Fe2+(t) > Ni2+(t) > Fe2+(q) > Ni2+(s) > Zn2+. However, for the imidazole model the order is slightly different, i.e., Ni2+(t) > Fe2+(t) > Fe2+(q) > Ni2+(s) ≥ Zn2+. Equilibrium structures of the R3Zn 2+ complexes with both HAM and silanediol are characterized by the monodentate binding, but the bidentate character of binding increases on going to iron and nickel complexes. Two types of intermediates of the water displacement reactions for [(NH3)3M-OH2]2+ complexes were found which differ by the direction of the attack of the MBG. Hexacoordinated complexes exhibit bidentate bonding of MBGs and are lower in energy for M=Ni and Fe. For Zn penta- and hexacoordinated complexes have nearly the same energy. Intermediate complexes with imidazole ligands have only octahedral structures with bidentate bonding of both HAM and dimethylsilanediol molecules.
Starting Page	1819
Ending Page	1834
Page Count	16
File Format	PDF
ISSN	16102940
Journal	Journal of Molecular Modeling
Volume Number	19
Issue Number	4
e-ISSN	09485023
Language	English
Publisher	Springer-Verlag
Publisher Date	2013-01-15
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	ab initio Binding energy DFT Metal binding groups Metalloproteases inhibitors Silanediol functionality Computer Applications in Chemistry Molecular Medicine Computer Application in Life Sciences Characterization and Evaluation of Materials Theoretical and Computational Chemistry
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Physical and Theoretical Chemistry Computational Theory and Mathematics Catalysis Inorganic Chemistry Computer Science Applications

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