Cooperative effect of hydrophobic and electrostatic forces on alcohol-induced alpha-helix formation of alpha1-acid glycoprotein |
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| Authors: | Nishi Koji Komine Yoshio Sakai Norifumi Maruyama Toru Otagiri Masaki |
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| Affiliation: | Department of Biopharmaceutics, Graduate School of Pharmaceutical Science, Kumamoto University 5-1 Oe-honmachi, Kumamoto 862-0973, Japan. |
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| Abstract: | Alpha1-acid glycoprotein (AGP) is a serum glycoprotein that mainly binds basic drugs. Previous reports have shown that AGP converts from a beta-sheet to an alpha-helix upon interaction with biomembranes. In the current studies, we found that alkanols, diols, and halogenols all induce this conformational change. Increased length and bulkiness of the hydrocarbon group and the presence of a halogen atom promoted this conversion, whereas the presence of a hydroxyl group inhibited it. Moreover, the effect was dependent on the hydrophobic and electrostatic properties of the alcohols. These results indicate that, in a membrane environment, hydrophobic and electrostatic factors cooperatively induce the transition of AGP from a beta-sheet to an alpha-helix. |
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| Keywords: | The abbreviations used for the alcohols are summarized in Table 1 α1-acid glycoprotein CD, circular dichroism ASA, solvent-accessible surface area ASA (T), total ASA rASA (H), relative ASA of hydrophobic region rASA (N), relative ASA of negative charge region rASA (P), relative ASA of positive charge region HE50, concentration of alcohol needed to form 50% α-helix structure |
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