Vasudevan, TK and Ran, VSR (1982) Preferred conformations and flexibility of aminoacyl side chain of penicillins. In: International Journal of Biological Macromolecules, 4 (6). pp. 347-351.
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Possible conformations of penicillin G; d and l isomers of ampicillin; α-amino-α-methyl-benzyl penicillins and 3- pyridyl methyl penicillin have been studied by an energy minimization procedure using empirical potential functions. The preferred conformations of these antibiotics have been correlated with their biological activity. The conformational requirement of the antibiotic to be active against Gram-positive and Gram-negative (β-lactamase-negative) bacterial strains seems to be the same. The reduced activity of penicillin G against Gram-negative bacteria has been attributed to its lower ability to permeate the outer membrane. The flexibility of the sidechains of these antibiotics is also shown to be important for the desired biological activity.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Elsevier Science.|
|Keywords:||Penicillin; conformation; side chain flexibility; β-lactam antibiotics; structure-activity relationships|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||31 Dec 2009 10:34|
|Last Modified:||19 Sep 2010 05:41|
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