The solubility of N-acetyl amino acid amides in organic acid and alcohol solutions: Mechanistic insight into structural protein solubilization
| Autor: | Momoyo Wada, Atsushi Hirano, Tomoshi Kameda, Takehiro K. Sato |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Formates
Formic acid 02 engineering and technology Biochemistry 2-Propanol 03 medical and health sciences chemistry.chemical_compound Acetic acid Structural Biology Amide Side chain Organic chemistry Solubility Amino Acids Molecular Biology Peptide sequence 030304 developmental biology chemistry.chemical_classification 0303 health sciences Proteins General Medicine 021001 nanoscience & nanotechnology Amides Amino acid chemistry Solvents 0210 nano-technology Organic acid |
| Zdroj: | International journal of biological macromolecules. 178 |
| ISSN: | 1879-0003 |
| Popis: | Structural proteins such as spider silk and silkworm silk are generally poorly soluble in aqueous and organic solutions, making them difficult to manipulate in manufacturing processes. Although some organic acids and alcohols, such as formic acid and hexafluoroisopropanol (HFIP), effectively solubilize poorly soluble proteins, little is known about their protein solubilization mechanism. In this study, the solubility of N-acetyl amino acid amide compounds in organic solvents-formic acid, acetic acid, HFIP and isopropanol-was measured to clarify the protein solubilization mechanism at the amino acid residue level. On the basis of thermodynamic analyses of the solubility in terms of the transfer free energy (from water to organic solvents), every organic solvent was found to be effective in thermodynamically stabilizing hydrophobic amino acid side chains in the liquid phase. Formic acid and HFIP were comparably effective in the stabilization of the polypeptide backbone, whereas acetic acid and isopropanol were ineffective. Therefore, the significant solubilizing effect of formic acid and HFIP on the structural proteins was attributed to their favorable interactions with hydrophobic amino acid side chains and with the polypeptide backbone of the proteins. The present findings are useful for the optimization of protein manipulation and amino acid sequence design. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect