英语科普小知识 药物的副作用不可避免.docVIP

A new study of both computer-created and natural proteins suggests that the number of unique pockets -- sites where small molecule pharmaceutical compounds can bind to proteins -- is surprisingly small, meaning drug side effects may be impossible to avoid. The study also found that the fundamental biochemical processes needed for life could have been enabled by the simple physics of protein folding. Studying a set of artificial proteins and comparing them to natural proteins, researchers at the Georgia Institute of Technology have concluded that there may be no more than about 500 unique protein pocket configurations that serve as binding sites for small molecule?ligands（配体）. Therefore, the likelihood that a molecule intended for one protein target will also bind with an unintended target is significant, said Jeffrey Skolnick a professor in the School of Biology at Georgia Tech. ? Our study provides a rationalization for why a lot of drugs have significant side effects -- because that is?intrinsic（本质的）?to the process, said Skolnick. There are only a relatively small number of different ligand binding pockets. The likelihood of having geometry in an amino acid composition that will bind the same ligand turns out to be much higher than anyone would have anticipated. This means that the idea that a small molecule could have just one protein target cant be supported. ? Research on the binding pockets was scheduled to be published May 20 in the early online edition of the journal Proceedings of the National Academy of Sciences. The research was supported by the National Institutes of Health (NIH). ? Skolnick and collaborator Mu Gao have been studying the effects of physics on the activity of protein binding and contrasting the original conditions created by the folding of amino acid residues against the role played by evolution in optimizing the process. ? The basic physics of the system provides the mechanism for molecules to bind to proteins, said Skolnick, who is d