Biomolecular NMR Unit

Milano, Italy

Biomolecular NMR Unit

Milano, Italy
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Paissoni C.,University of Milan | Ghitti M.,Biomolecular NMR Unit | Belvisi L.,University of Milan | Spitaleri A.,Italian Institute of Technology | Musco G.,Biomolecular NMR Unit
Chemistry (Weinheim an der Bergstrasse, Germany) | Year: 2015

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. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.


Paissoni C.,Biomolecular NMR Unit | Paissoni C.,University of Milan | Ghitti M.,Biomolecular NMR Unit | Belvisi L.,University of Milan | And 2 more authors.
Chemistry - A European Journal | Year: 2015

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. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.


PubMed | Italian Institute of Technology, Biomolecular NMR Unit and University of Milan
Type: Journal Article | Journal: Chemistry (Weinheim an der Bergstrasse, Germany) | Year: 2015

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 IIb3. 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.

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