The Cumulative Electrostatic Effect of Aromatic Stacking Interactions and the Negative Electrostatic Environment of the Flavin Mononucleotide Binding Site Is a Major Determinant of the Reduction Potential for the Flavodoxin fromDesulfovibrio vulgaris[Hildenborough]†

Biochemistry ◽  
1996 ◽  
Vol 35 (50) ◽  
pp. 15980-15988 ◽  
Author(s):  
Zhimin Zhou ◽  
Richard P. Swenson
Keyword(s):  
Binding Site ◽  
Reduction Potential ◽  
Major Determinant ◽  
Flavin Mononucleotide ◽  
Stacking Interactions ◽  
Aromatic Stacking ◽  
Electrostatic Effect

A Chemical Perspective to the Anti-Amyloid Action of Compounds and a Nanoparticle Based Assay for Screening Amyloid Inhibitors

2020 ◽  
Author(s):  
Nidhi Gour ◽  
Bharti Koshti
Keyword(s):  
Memory Loss ◽  
Cost Effective ◽  
Structural Motif ◽  
Rapid Screening ◽  
Stacking Interactions ◽  
Aromatic Rings ◽  
Amyloid Fibers ◽  
Aromatic Stacking ◽  
Cost Effective Technique ◽  
The Brain

Aggregation of amyloid beeta 1-42 (Aβ<sub>42</sub>) peptide causes the formation of clustered deposits knows as amyloid plaques in the brain which leads to neuronal dysfunction and memory loss and associated with many neurological disorders including Alzheimer’s and Parkinson’s. Aβ<sub>42</sub> has core structural motif with phenylalanine at the 19 and 20 positions. The diphenylalanine (FF) residue plays a crucial role in the formation of amyloid fibers and serves as model peptide for studying Aβ<sub>42 </sub>aggregation. FF self-assembles to well-ordered tubular morphology via aromatic pi-pi stackings. Our studies, suggest that the aromatic rings present in the anti-amyloidogenic compounds may interact with the pi-pi stacking interactions present in the FF. Even the compounds which do not have aromatic rings, like cyclodextrin and cucurbituril show anti-amyloid property due to the binding of aromatic ring inside the guest cavity. Hence, our studies also suggest that compounds which may have a functional moiety capable of interacting with the aromatic stacking interactions might be tested for their anti-amyloidogenic properties. Further, in this manuscript, we have proposed two novel nanoparticle based assays for the rapid screening of amyloid inhibitors. In the first assay, interaction between biotin-tagged FF peptide and the streptavidin labelled gold nanoparticles (s-AuNPs) were used. In another assay, thiol-Au interactions were used to develop an assay for detection of amyloid inhibitors. It is envisaged that the proposed analytical method will provide a simple, facile and cost effective technique for the screening of amyloid inhibitors and may be of immense practical implications to find the therapeutic remedies for the diseases associated with the protein aggregation.

scholarly journals Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase

FEBS Journal ◽  
2015 ◽  
Vol 282 (16) ◽  
pp. 3091-3106 ◽  
Author(s):  
Patricia Ferreira ◽  
Aitor Hernández-Ortega ◽  
Fátima Lucas ◽  
Juan Carro ◽  
Beatriz Herguedas ◽  
...  
Keyword(s):  
Alcohol Oxidase ◽  
Stacking Interactions ◽  
Aromatic Stacking

A Supramolecular System for Quantifying Aromatic Stacking Interactions

2001 ◽  
Vol 7 (22) ◽  
pp. 4863-4877 ◽  
Author(s):  
Harry Adams ◽  
Christopher A. Hunter ◽  
Kevin R. Lawson ◽  
Julie Perkins ◽  
Sharon E. Spey ◽  
...  
Keyword(s):  
Supramolecular System ◽  
Stacking Interactions ◽  
Aromatic Stacking

scholarly journals Specific Features for the Competent Binding of Substrates at the FMN Adenylyltransferase Site of FAD Synthase from Corynebacterium ammoniagenes

2019 ◽  
Vol 20 (20) ◽  
pp. 5083 ◽  
Author(s):  
Sonia Arilla-Luna ◽  
Ana Serrano ◽  
Milagros Medina
Keyword(s):  
Binding Site ◽  
Thermodynamic Parameters ◽  
Spectroscopic Properties ◽  
Open Cavity ◽  
Flavin Mononucleotide ◽  
Kinetic Properties ◽  
Biophysical Properties ◽  
Conserved Motif ◽  
Corynebacterium Ammoniagenes ◽  
Optimal Geometry

Bifunctional FAD synthases (FADSs) catalyze FMN (flavin mononucleotide) and FAD (flavinadenine dinucleotide) biosynthesis at their C-riboflavin kinase (RFK) and N-FMN:adenylyltransferase (FMNAT) modules, respectively. Biophysical properties and requirements for their FMNAT activity differ among species. Here, we evaluate the relevance of the integrity of the binding site of the isoalloxazine of flavinic substrates for FMNAT catalysis in Corynebacterium ammoniagenes FADS (CaFADS). We have substituted P56 and P58, belonging to a conserved motif, as well as L98. These residues shape the isoalloxazine FMNAT site, although they are not expected to directly contact it. All substitutions override enzyme ability to transform substrates at the FMNAT site, although most variants are able to bind them. Spectroscopic properties and thermodynamic parameters for the binding of ligands indicate that mutations alter their interaction modes. Substitutions also modulate binding and kinetic properties at the RFK site, evidencing the crosstalk of different protomers within CaFADS assemblies during catalysis. In conclusion, despite the FMNAT site for the binding of substrates in CaFADS appearing as a wide open cavity, it is finely tuned to provide the competent binding conformation of substrates. In particular, P56, P58 and L98 shape the isoalloxazine site to place the FMN- and FAD-reacting phosphates in optimal geometry for catalysis.

Metal ion clip: fine-tuning aromatic stacking interactions in the multistep formation of carbazole-bridged zinc(ii) complexes

2015 ◽  
Vol 51 (50) ◽  
pp. 10103-10106 ◽  
Author(s):  
Yuki Imai ◽  
Tsuyoshi Kawai ◽  
Junpei Yuasa
Keyword(s):  
Metal Ion ◽  
Fine Tuning ◽  
Stacking Interactions ◽  
Aromatic Stacking ◽  
Bridging Ligand

A carbazole-based triple bridging ligand (LH) consisting of two imidazole moieties with a diketone unit forms carbazole-bridged zinc(ii) complexes with structures of [(L−)4(Zn2+)n] (n = 2–6), where the strength of aromatic stacking interactions between the carbazole rings increases with an increase in the number of Zn2+ ions bridged.

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