The pH-Dependent Conformational States of Kyotorphin: A Constant-pH Molecular Dynamics Study

摘要: An extensive conformational study of the analgesic dipeptide kyotorphin (L-Tyr-L-Arg) at different pH values was performed using a constant-pH molecular dynamics method. This showed remarkable pH-dependent variety. The protonation N-terminal amine identified as key element in transition between more extended and packed states, monitored by dihedral angle defined atoms 1Cβ-1Cα-2Cα-2Cβ. principal-component analysis two major populations (the trans cis) together with conformations that occur exclusively extreme values. Other, less stable were also identified, which help us to understand transitions predominant populations. fitting kyotorphin's space structure morphine resulted set conformers able fulfill most constraints for μ-receptor. These results suggest there may be strong similarities receptor structural family opioid receptors.