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Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
Published on: December 16, 2021
Modulation of small molecule solubility and protein binding by arginine
Tsutomu Arakawa1, Misao Uozaki, A Hajime Koyama
1Alliance Protein Laboratories, 3957 Corte Cancion, Thousand Oaks, CA 91360, USA.
Molecular Medicine Reports
|April 8, 2011
Summary
Arginine significantly enhances the aqueous solubility of acycloguanosine (ACV), an antiviral drug. This amino acid also affects how OG binds to proteins, suggesting a role in drug formulation.
Area of Science:
- Pharmaceutical Sciences
- Physical Chemistry
- Biochemistry
Background:
- Arginine is known to increase the aqueous solubility of certain low molecular weight aromatic compounds.
- Acycloguanosine (ACV) is an antiherpetic agent with moderate aqueous solubility, posing formulation challenges.
Purpose of the Study:
- To investigate the effect of arginine on the aqueous solubility of acycloguanosine (ACV) at neutral pH.
- To compare the protein binding behavior of ACV and octyl-gallate (OG) in the presence of arginine.
Main Methods:
- Solubility of ACV was measured in aqueous solutions containing varying concentrations of arginine (0.1 M to 2 M) at neutral pH.
- Binding of ACV and OG to bovine serum albumin (BSA) was assessed to understand protein-ligand interactions.
Main Results:
- ACV solubility increased approximately 1.9-fold and 2.6-fold with 1 M and 2 M arginine, respectively.
- No significant solubility enhancement was observed below 0.1 M arginine.
- While ACV showed no binding to BSA, OG exhibited substantial binding, which was partially inhibited by arginine.
Conclusions:
- Arginine effectively enhances the aqueous solubility of acycloguanosine (ACV) in a dose-dependent manner at neutral pH.
- Differential protein binding observed between ACV and OG suggests distinct interaction mechanisms.
- Arginine's ability to modulate protein binding may influence drug delivery and formulation strategies.
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