pK shift of functional group in mechanochemical coupling due to hydrophobic effect: evidence for an apolar-polar repulsion free energy in water.
In the sequential polypeptide poly[4(VPGVG),(VPGEG)] and its more hydrophobic analog poly[4(IPGVG),(IPGEG)] when the material is gamma-irradiation cross-linked to form an elastomeric matrix, mechanochemical coupling occurs on changing the pH, that is, motion and mechanical work are achieved by a change in proton chemical potential. The temperature dependence of aggregation at different pH values in phosphate buffered saline demonstrates the pK to be shifted approximately one pH unit higher for the more hydrophobic sequential polypeptide. The pH dependence of contraction or relaxation for each elastomer shows a similar shift. Data are reviewed and 2D-NMR data are presented which argue that the pK shift is not due to different conformations of the polypentapeptides. Specifically it is proposed that there exist a competition between carboxylates and hydrophobic side chains for mutually incompatible water structures; this results in an apolar-polar repulsion free energy in water with the difference in free energy reflecting the difference in the lle and Val hydrophobicities.
Urry
D W
DW
Laboratory of Molecular Biophysics, School of Medicine, University of Alabama, Birmingham 35294.
Chang
D K
DK
Zhang
H
H
Prasad
K U
KU
D004549:Elastin; D006863:Hydrogen-Ion Concentration; D007532:Isoleucine; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D009842:Oligopeptides; D012995:Solubility; D013329:Structure-Activity Relationship; D013696:Temperature; D013816:Thermodynamics; D014633:Valine; D014867:Water
D009842:Oligopeptides; D007532:Isoleucine; D014867:Water; D004549:Elastin; D014633:Valine