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Cooperative effect of hydrophobic and electrostatic forces on alcohol‐induced α‐helix formation of α 1 ‐acid glycoprotein
Author(s) -
Nishi Koji,
Komine Yoshio,
Sakai Norifumi,
Maruyama Toru,
Otagiri Masaki
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.05.044
Subject(s) - chemistry , hydrophobic effect , glycoprotein , alcohol , helix (gastropod) , biophysics , membrane , electrostatics , static electricity , halogen , conformational change , stereochemistry , biochemistry , organic chemistry , alkyl , ecology , snail , electrical engineering , biology , engineering
α 1 ‐Acid glycoprotein (AGP) is a serum glycoprotein that mainly binds basic drugs. Previous reports have shown that AGP converts from a β‐sheet to an α‐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 β‐sheet to an α‐helix.