Conformational studies of synthesized neuropeptide fragment hPP【17-24】by CD and NMR

• Main Authors: Ming-Ju Wu, 吳明儒
• Other Authors: Chang-Shin Lee
• Format: Others
• Language: zh-TW
• Published: 2008
• Online Access: http://ndltd.ncl.edu.tw/handle/96jee5

碩士 === 淡江大學 === 化學學系碩士班 === 96 === The human pancreatic polypeptide(hPP), a 36-residue, polypeptide hormone is a member of the neuropeptide Y(NPY)family. In the central nervous system PP promotes food intake and gastric emptying by activation of the Y4 and probably Y5 receptors. The C-terminal is a well-defined α-helical region and the N terminus is an extended polyproline helix which bent back onto the the C-terminalα-helix. The structural motif of pp has been named as the PP-fold. hPP in solution exists as a dimer and when bound to micelle, it exists as a monomer. Therefore, to elucidate the monomer structure is important. Short peptide fragment may avoid dimmer formation and reveal the folding dynamoics of hpp. We studied hPP[17-24] ,of α-helical region, and used SPPS method for synthesizing the residues17-24.Isolation and purification were performed by HPLC and the molecular weight were made sure by Mass. The conformation and dynamics of hPP[17-24] in different solvent condition is studied by CD and 2D NMR experiment. Conformation of hPP[17-24] exists as a random coil in 100%H2O and become more regular in 50%TFE / 50%H2O of hPP[17-24].