Conformational Variation and Selectivity of Glycosylated PACAP23 Replacing the Fourth Residue by Beta-turn or Alpha-helix Inducers

Identifier:  TFG:3799

Handle: https://hdl.handle.net/20.500.11797/TFG3799

Authors:  Gilmartin, Thiago

Abstract:
Discussion of the variation in the conformation and affinity of the glycosylated neurohormone PACAP23 in function of the substitution of the fourth amino acid of the peptide chain by Glycine, Alanine, or Sarcosine; and their affinity towards the G protein-coupled receptors PAC1, VPAC1, and VPAC2. This substitution may cause the variation of the three-dimensional structure of the peptide, producing beta-turn or alpha-helix conformations. Beta-turns favor the affinity to PAC1 receptors, while alpha-helix conformations will rather interact with VPAC1 and VPAC2 receptors. This study has been centered on PAC1 affinity and activation, due to its neuroprotective and neuro-repairing activity.