Abstract
AbstractIn the Arginine Vasopressin (CYFQNCPRG–NH2, AVP) molecule, the disulfide bond between Cys1 and Cys6 forms a 20‐membered ring crucial for AVP activity. The activity could be enhanced by restraining the AVP structure with additional cyclic moiety. To reduce AVP conformational flexibility, a standard link has now been added between residues at position 4, substituted with different positively charged amino acids, and Gly at position 9. The resulting AVP analogues have subsequently been docked to the vasopressin and oxytocin receptors and relaxed/geometry optimized using a Constrained Simulated Annealing (CSA) procedure. The results of our modeling suggest that the size of the additional AVP cycle is crucial for the biological activity of the analogue.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
