Studies of ligand diffusion pathways over a protein surface.
Studies were conducted on the behavior of simulated molecules diffusing within organized water, postulated to form from the hydropathic states of protein surface amino acid side chains. This organization is postulated to facilitate the diffusion of ligands across the protein surface to their effector. These studies reveal that the organized water can be disrupted in their diffusion facilitating function by the presence of some other solute in high concentration. It was also found from cellular automata simulations that chiral isomers behaved in a slightly different manner when in an asymmetric enclosure simulating a fragment of the organized water pathway. These findings have relevance to observations about the mechanism of action of nonspecific anesthetic agents.
Kier
Lemont B
LB
Institute of Medicinal Chemistry, University of Lausanne, CH-1015 Lausanne, Switzerland. kier@hsc.vcu.edu
Cheng
Cho-Kung
CK
Testa
Bernard
B
D000596:Amino Acids / Q000737:chemistry; D000777:Anesthetics / Q000494:pharmacology; D001665:Binding Sites; D003198:Computer Simulation; D004058:Diffusion; D008024:Ligands; D008956:Models, Chemical; D011506:Proteins / Q000737:chemistry*; D013499:Surface Properties; D014867:Water / Q000737:chemistry
D000596:Amino Acids; D000777:Anesthetics; D008024:Ligands; D011506:Proteins; D014867:Water