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Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide
Published on: December 19, 2020
Cyclodepsipeptides as chemical tools for studying ionic transport through membranes
M M Shemyakin1, Y A Ovchinnikov, V T Ivanov
1Institute for Chemistry of Natural Products, USSR Academy of Sciences, Moscow, USSR.
This study explores membrane-active depsipeptides like valinomycin, revealing their cation-binding abilities influence antimicrobial activity. These compounds can be chemically tailored as tools for studying biological membranes.
Area of Science:
- Biochemistry
- Biophysics
- Membrane Biology
Background:
- Valinomycin and enniatins are membrane-active depsipeptides.
- These compounds affect alkali metal ion permeability in biological and model membranes.
- Their antimicrobial activity is linked to cation-complexing ability.
Purpose of the Study:
- To investigate the chemistry of depsipeptides and their interaction with membranes.
- To correlate cation-complexing ability with antimicrobial activity and membrane effects.
- To elucidate the spatial structure and conformational properties of these cyclodepsipeptides.
Main Methods:
- Spectropolarimetry and conductimetry were used to study cation complexation.
- Nuclear magnetic resonance (NMR), optical rotatory dispersion (ORD), and infrared (IR) spectrophotometry were employed.
- Studies included interactions with phospholipid monolayers, bimolecular membranes, and biological membrane systems.
Main Results:
- Conformational analysis revealed coexisting conformers in solution.
- The spatial structures of valinomycin, enniatin B, and their K+ complexes were elucidated.
- Cyclodepsipeptide conformation impacts complexation efficiency, selectivity, and membrane interactions.
Conclusions:
- Depsipeptides can be designed as chemical tools for membrane research.
- Conformation-dependent cation binding via ion-dipole interactions may explain natural ion permeability mechanisms.
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