Role of Hydrophobic Interactions in Enzyme Inhibition by Drugs

1970 ◽  
Vol 59 (6) ◽  
pp. 865-868 ◽  
Author(s):  
Eric J. Lien ◽  
Mehdi Hussain ◽  
George L. Tong
Keyword(s):  
Enzyme Inhibition ◽  
Hydrophobic Interactions

The role of hydrophobic interactions in binding of polyamines to non NMDA receptor ion channels

1998 ◽  
Vol 37 (10-11) ◽  
pp. 1381-1391 ◽  
Author(s):  
Changhai Cu ◽  
Robert Bähring ◽  
Mark L. Mayer
Keyword(s):  
Ion Channels ◽  
Nmda Receptor ◽  
Hydrophobic Interactions

Some Considerations on Confined Water: The Thermal Behavior of Transport Properties in Water-Glycerol and Water-Methanol Mixtures

MRS Advances ◽  
2016 ◽  
Vol 1 (26) ◽  
pp. 1891-1902 ◽  
Author(s):  
Francesco Mallamace ◽  
Carmelo Corsaro ◽  
Domenico Mallamace ◽  
Cirino Vasi ◽  
Sebastiano Vasi ◽  
...  
Keyword(s):  
Hydrophobic Interactions ◽  
Molar Fraction ◽  
Relaxation Times ◽  
Confined Water ◽  
Self Diffusion ◽  
Excess Value ◽  
Water Glycerol ◽  
System Properties ◽  
Dynamical Crossover

ABSTRACTWe discuss recent literature data on the relaxation times (the primary tα), viscosity, and self-diffusion in water-glycerol and water-methanol mixtures across a wide temperature range from the stable water phase to the deep supercooled regime (373–147K). In particular, to clarify the role of hydrophilicity interactions (the hydrogen bonds) and hydrophobic interactions we study the mixture in terms of the water molar fraction (XW) with fixed temperatures at 5K steps across the entire composition range, and we find a marked deviation from the ideal thermodynamic behavior of the transport functions. This deviation is strongly T and XW dependent and spans values that range from two orders of magnitude at the highest temperature to more than five in the deeply supercooled regime (more precisely, at ≃200K). We analyze these deviations in terms of how the measured values differ from ideal values and find that the hydrogen-bonding water network dominates system properties up to XW = 0.3. We also examine an Arrhenius plot of the maximum excess value (Δtα(T) vs. 1/T) and find two significant changes due to water: one at the dynamical crossover temperature (TL ≃ 225K, i.e., the locus of the Widom line), and one at T ≃ 315K (the water isothermal compressibility χT minimum).

Brain angiotensin receptors and sympathoadrenal regulation during insulin-induced hypoglycemia

2001 ◽  
Vol 280 (4) ◽  
pp. R1162-R1168 ◽  
Author(s):  
René H. Worck ◽  
Dennis Staahltoft ◽  
Thomas E. N. Jonassen ◽  
Erik Frandsen ◽  
Hans Ibsen ◽  
...  
Keyword(s):  
Blood Pressure ◽  
Enzyme Inhibition ◽  
Blood Pressure Response ◽  
Pressure Response ◽  
Angiotensin Receptors ◽  
Converting Enzyme ◽  
Reflex Regulation ◽  
Conscious Rats ◽  
Converting Enzyme Inhibition

Simultaneous blockade of systemic AT1 and AT2 receptors or converting enzyme inhibition (CEI) attenuates the hypoglycemia-induced reflex increase of epinephrine (Epi). To examine the role of brain AT1 and AT2 receptors in the reflex regulation of Epi release, we measured catecholamines, hemodynamics, and renin during insulin-induced hypoglycemia in conscious rats pretreated intracerebroventricularly with losartan, PD-123319, losartan and PD-123319, or vehicle. Epi and norepinephrine (NE) increased 60-and 3-fold, respectively. However, the gain of the reflex increase in plasma Epi (Δplasma Epi/Δplasma glucose) and the overall Epi and NE responses were similar in all groups. The ensuing blood pressure response was similar between groups, but the corresponding bradycardia was augmented after PD-123319 ( P < 0.05 vs. vehicle) or combined losartan and PD-123319 ( P < 0.01 vs. vehicle). The findings indicate 1) brain angiotensin receptors are not essential for the reflex regulation of Epi release during hypoglycemia and 2) the gain of baroreceptor-mediated bradycardia is increased by blockade of brain AT2 receptors in this model.

The Role of Hydrophobic Interactions in Amyloidogenesis: Example of Prion-Related Polypeptides

2003 ◽  
Vol 21 (3) ◽  
pp. 353-365 ◽  
Author(s):  
Olga Tcherkasskaya ◽  
William Sanders ◽  
Veeradej Chynwat ◽  
Eugene A. Davidson ◽  
Cindy S. Orser
Keyword(s):  
Hydrophobic Interactions

scholarly journals Electrostatic and Hydrophobic Interactions Differentially Tune Membrane Binding Kinetics of the C2 Domain of Protein Kinase Cα

2013 ◽  
Vol 288 (23) ◽  
pp. 16905-16915 ◽  
Author(s):  
Angela M. Scott ◽  
Corina E. Antal ◽  
Alexandra C. Newton
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Rate Constants ◽  
Electrostatic Interactions ◽  
Hydrophobic Interactions ◽  
Dissociation Rate ◽  
C2 Domain ◽  
Pkc Isozymes ◽  
Dissociation Rate Constants

The cellular activation of conventional protein kinase C (PKC) isozymes is initiated by the binding of their C2 domains to membranes in response to elevations in intracellular Ca2+. Following this C2 domain-mediated membrane recruitment, the C1 domain binds its membrane-embedded ligand diacylglycerol, resulting in activation of PKC. Here we explore the molecular mechanisms by which the C2 domain controls the initial step in the activation of PKC. Using stopped-flow fluorescence spectroscopy to measure association and dissociation rate constants, we show that hydrophobic interactions are the major driving force in the binding of the C2 domain to anionic membranes, whereas electrostatic interactions dominate in membrane retention. Specifically, mutation of select hydrophobic or select basic residues in the Ca2+-binding loops reduces membrane affinity by distinct mechanisms; mutation of hydrophobic residues primarily alters association rate constants, whereas mutation of charged residues affects dissociation rate constants. Live cell imaging reveals that introduction of these mutations into full-length PKCα not only reduces the Ca2+-dependent translocation to plasma membrane but, by impairing the plasma membrane-sensing role of the C2 domain, causes phorbol ester-triggered redistribution of PKCα to other membranes, such as the Golgi. These data underscore the key role of the C2 domain in driving conventional PKC isozymes to the plasma membrane and reveal that not only the amplitude but also the subcellular location of conventional PKC signaling can be tuned by altering the affinity of this module for membranes.

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