We combined metadynamics, docking and molecular mechanics/generalised born surface area (MM/GBSA) re-scoring methods to investigate the impact of single and multiple N-methylation on a set of RGD cyclopeptides displaying different affinity for integrin αIIbβ3. We rationalised the conformational effects induced by N-methylation and its interplay with receptor affinity, obtaining good agreement with experimental data. This approach can be exploited before entering time-consuming and expensive synthesis and binding experiments.
Metadynamics simulations rationalize the conformational effects induced by N-methylation of RGD cyclic hexapeptides / C. Paissoni, M. Ghitti, L. Belvisi, A. Spitaleri, G. Musco. - In: CHEMISTRY-A EUROPEAN JOURNAL. - ISSN 0947-6539. - 21:40(2015 Sep 28), pp. 14165-14170.
Metadynamics simulations rationalize the conformational effects induced by N-methylation of RGD cyclic hexapeptides
C. Paissoni;L. Belvisi;A. Spitaleri;
2015
Abstract
We combined metadynamics, docking and molecular mechanics/generalised born surface area (MM/GBSA) re-scoring methods to investigate the impact of single and multiple N-methylation on a set of RGD cyclopeptides displaying different affinity for integrin αIIbβ3. We rationalised the conformational effects induced by N-methylation and its interplay with receptor affinity, obtaining good agreement with experimental data. This approach can be exploited before entering time-consuming and expensive synthesis and binding experiments.File | Dimensione | Formato | |
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