AI Article Synopsis
- Molecular graphics and modeling techniques helped clarify the chemical basis of the a priori approach and visualize enzyme-inhibitor interactions for compound 34 and its derivatives.
- The overlap of electron density between the enzyme and inhibitor is significant at distances of 1.5-5.5 Å, which is beyond typical van der Waals radii.
- The derivatives of compound 34 show a linear correlation between their biological activity, molecular size, and the amount of intermolecular interactions they exhibit.
Article Abstract
Molecular graphics and modeling methods illustrated the chemical background of the a priori approach from part I, and visualized steric and electronic enzyme-inhibitor relationships at qualitative and quantitative level for 34 and its derivatives. The enzyme-inhibitor electron density overlap occurs at 1.5-5.5A cut-off distance, beyond van der Waals radii. Derivatives of 34 exhibit linear relationships between biological activity, molecular size and number of intermolecular interactions.
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| http://dx.doi.org/10.1016/S1093-3263(02)00202-4 | DOI Listing |
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