Docking and Structural Validation of Analgesic Peptide Muteins with Opiod Receptors

  • Dr. J. Venkateshwara Rao

Abstract

The new age of opioid research began with identification of endogenous ligands in the brain for analgesic receptors, which led to identification and structure determination of enkephalins, dynorphins and endomorphins along with opioid receptors µ (MOR), δ (DOR), and k (KOR).  Only the possible variants were entered in the matrix. β-Endorphin, Dynorphin 32 and Peptide F were selected based on their high binding efficiency without cross-reaction. These peptides were further modified and necessary changes were done to prepare active models for the interaction studies. Two hybrid peptides were constructed by using three active peptides reported in literature linked with polyglycine linkers. Peptides1 shows 10 amino acids interacting with kappa1 receptor are Phe332, Lys338, Arg257, Val256, Arg274, Ser255, Arg270, Lys254, Leu253 and Ile250. Peptides 2 shows 12 amino acids interacting with kappa2 receptor are His162, Leu167, Val160, Ser255, Val256, Leu258, Leu259, Asp266, Arg270, Glu335, Lys349 and Ser262. This information is highly useful to develop modern analgesic peptide based drugs for future medical applications.

Published
2020-04-25
How to Cite
Dr. J. Venkateshwara Rao. (2020). Docking and Structural Validation of Analgesic Peptide Muteins with Opiod Receptors. International Journal of Advanced Science and Technology, 29(8s), 1117 - 1127. Retrieved from http://sersc.org/journals/index.php/IJAST/article/view/11529