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Magdalena J. Ślusarz, Emilia Sikorska and Rafał Ślusarz Interactions of vasopressin and oxytocin receptors with vasopressin analogues substituted in position 2 with 3,3′-diphenylalanine – a molecular docking study Journal of Peptide Science 19

Article first published online: 10 JAN 2013 | DOI: 10.1002/psc.2485

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Four vasopressin analogues substituted at position 2 with 3,3′-diphenylalanine have been docked into partially flexible vasopressin/oxytocin receptors. The bulky residue at position 2 acts as a structural restraint much stronger in the oxytocin receptor than in the vasopressin V2 receptor. A weak activity at V1a vasopressin receptor appears to be caused by weak receptor–ligand interactions. Results of this study may facilitate a rational design of new analogues with the highest activity/selectivity at vasopressin and oxytocin receptors.

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