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Differences in Interactions of Benzoic Acid and Benzoate with Interfaces.

ABSTRACT: The interaction of benzoic acid and benzoate with model membrane systems was characterized to understand the molecular interactions of the two forms of a simple aromatic acid with the components of the membrane. The microemulsion system based on bis(2-ethylhexyl)sulfosuccinate (AOT) allowed determination of the molecular positioning using 1D NMR and 2D NMR spectroscopic methods. Benzoic acid and benzoate were both found to penetrate the membrane/water interfaces; however, the benzoic acid was able to penetrate much deeper and thus is more readily able to traverse a membrane. The Langmuir monolayer model system, using dipalmitoylphosphatidylcholine, was used as a generic membrane lipid for a cell. Compression isotherms of monolayers demonstrated a pH dependent interaction with a lipid monolayer and confirming the pH dependent observations shown in the reverse micellar model system. These studies provide an explanation for the antimicrobial activity of benzoic acid while benzoate is inactive. Furthermore, these studies form the framework upon which we are investigating the mode of bacterial uptake of pyrazinoic acid, the active form of pyrazinamide, a front line drug used to combat tuberculosis.

SUBMITTER: Peters BJ

PROVIDER: S-EPMC6168200 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature

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Differences in Interactions of Benzoic Acid and Benzoate with Interfaces.

Peters Benjamin J BJ Groninger Allison S AS Fontes Fabio L FL Crick Dean C DC Crans Debbie C DC

Langmuir : the ACS journal of surfaces and colloids 20160908 37

The interaction of benzoic acid and benzoate with model membrane systems was characterized to understand the molecular interactions of the two forms of a simple aromatic acid with the components of the membrane. The microemulsion system based on bis(2-ethylhexyl)sulfosuccinate (AOT) allowed determination of the molecular positioning using 1D NMR and 2D NMR spectroscopic methods. Benzoic acid and benzoate were both found to penetrate the membrane/water interfaces; however, the benzoic acid was ab ...[more]

PMID: 27482911

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Project description:ConspectusMolecular association of proteins with nucleic acids is required for many biological processes essential to life. Electrostatic interactions via ion pairs (salt bridges) of nucleic acid phosphates and protein side chains are crucial for proteins to bind to DNA or RNA. Counterions around the macromolecules are also key constituents for the thermodynamics of protein-nucleic acid association. Until recently, there had been only a limited amount of experiment-based information about how ions and ionic moieties behave in biological macromolecular processes. In the past decade, there has been significant progress in quantitative experimental research on ionic interactions with nucleic acids and their complexes with proteins. The highly negatively charged surfaces of DNA and RNA electrostatically attract and condense cations, creating a zone called the ion atmosphere. Recent experimental studies were able to examine and validate theoretical models on ions and their mobility and interactions with macromolecules. The ionic interactions are highly dynamic. The counterions rapidly diffuse within the ion atmosphere. Some of the ions are released from the ion atmosphere when proteins bind to nucleic acids, balancing the charge via intermolecular ion pairs of positively charged side chains and negatively charged backbone phosphates. Previously, the release of counterions had been implicated indirectly by the salt-concentration dependence of the association constant.Recently, direct detection of counterion release by NMR spectroscopy has become possible and enabled more accurate and quantitative analysis of the counterion release and its entropic impact on the thermodynamics of protein-nucleic acid association. Recent studies also revealed the dynamic nature of ion pairs of protein side chains and nucleic acid phosphates. These ion pairs undergo transitions between two major states. In one of the major states, the cation and the anion are in direct contact and form hydrogen bonds. In the other major state, the cation and the anion are separated by water. Transitions between these states rapidly occur on a picosecond to nanosecond time scale. When proteins interact with nucleic acids, interfacial arginine (Arg) and lysine (Lys) side chains exhibit considerably different behaviors. Arg side chains show a higher propensity to form rigid contacts with nucleotide bases, whereas Lys side chains tend to be more mobile at the molecular interfaces. The dynamic ionic interactions may facilitate adaptive molecular recognition and play both thermodynamic and kinetic roles in protein-nucleic acid interactions.

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Differences in Interactions of Benzoic Acid and Benzoate with Interfaces.

Publications

Differences in Interactions of Benzoic Acid and Benzoate with Interfaces.

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