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Inhibitors of the M2 Proton Channel Engage and Disrupt Transmembrane Networks of Hydrogen-Bonded Waters.
- J. Thomaston, N. Polizzi, Athina Konstantinidi, Jun Wang, A. Kolocouris, W. DeGrado
- Biology, ChemistryJournal of the American Chemical Society
- 30 August 2018
X-ray crystal structures of the M2 proton channel with bound inhibitors reveal that ammonium groups bind to water-lined sites that are hypothesized to stabilize transient hydronium ions formed in the proton-conduction mechanism.
X-ray crystal structures of the influenza M2 proton channel drug-resistant V27A mutant bound to a spiro-adamantyl amine inhibitor reveal the mechanism of adamantane resistance.
It is observed that the channel pore is wider at its N-terminus as a result of the V27A mutation and that this removes V27 side chain hydrophobic interactions that are important for binding of amantadine and rimantadines.
Unraveling the Binding, Proton Blockage, and Inhibition of Influenza M2 WT and S31N by Rimantadine Variants.
- Antonios Drakopoulos, Christina Tzitzoglaki, A. Kolocouris
- BiologyACS medicinal chemistry letters
- 29 January 2018
It was shown that resistance of M2 S31N to rimantadine analogues compared to M2 WT resulted from their higher koff rates compared to the kon rates according to electrophysiology (EP) measurements, and it was also shown that a small change in an amino acid at site 28 of M 2 WT, which does not line the pore, seriously affects M2WT blockage kinetics.
Comparative Perturbation Effects Exerted by the Influenza A M2 WT Protein Inhibitors Amantadine and the Spiro[pyrrolidine-2,2'-adamantane] Variant AK13 to Membrane Bilayers Studied Using Biophysical…
- Athina Konstantinidi, N. Naziris, A. Kolocouris
- Chemistry, BiologyThe journal of physical chemistry. B
- 4 October 2018
The comparative effects of amantadine and its synthetic spiro[pyrrolidine-2,2'-adamantane] (AK13) analogue in dimyristoylphosphatidylcholine (DMPC) bilayers were studied and it was pointed out that the two analogues perturbed drastically the DMPC bilayers with AK13 to be more effective at high concentrations.
1,2-Αnnulated Adamantane Heterocyclic Derivatives as Anti-Influenza Α Virus Agents
- Vasiliki Pardali, Erofili Giannakopoulou, Athina Konstantinidi, A. Kolocouris, Grigoris Zoidis
- ChemistryCroatica chemica acta
- 29 July 2019
In this report we review our results on the development of 1,2-annulated adamantane heterocyclic derivatives and we discuss the structure-activity relationships obtained from their biological…
Chemical Probes for Blocking of Influenza A M2 WT and S31N Channels.
- Christina Tzitzoglaki, K. McGuire, A. Kolocouris
- Biology, ChemistryACS chemical biology
- 12 August 2020
In the active M2 S31N blockers 1 and 6, the phenyl and isoxazolyl head groups achieve a deeper binding position, corresponding to high kon / low koff and high koff measured rate constants, compared to inactive 2-5, which have much lower kon and higher koff.
Rimantadine Binds to and Inhibits the Influenza A M2 Proton Channel without Enantiomeric Specificity.
It is concluded that the slight differences in hydration for the (R)- and (S)-rimantadine enantiomers are not relevant to drug binding or channel inhibition, and the water structure was evaluated by grand canonical ensemble molecular dynamics simulations as a function of the chemical potential of the water.
Molecular investigation of artificial and natural sweeteners as potential anti-inflammatory agents.
- Eleni Chontzopoulou, Christina D. Papaemmanouil, T. Mavromoustakos
- Biology, ChemistryJournal of biomolecular structure & dynamics
- 9 September 2021
The in silico methods indicated that aspartame could serve as a novel starting point for drug design against LOX enzyme, an enzyme participating in the inflammation pathway.
The boundary lipid around DMPC-spanning influenza A M2 transmembrane domain channels: Its structure and potential for drug accommodation.