Identification of the Site of the Octanoic Acid Post-Translational Modification in Human Ghrelin Using Electron Transfer Dissociation

Ghrelin is a human peptide hormone containing 28 amino acid residues, which is primarily produced in the stomach. The biological function of Ghrelin is known to stimulate the brain to increase appetite and favor the accumulation of lipids in visceral fatty tissue. The amino acid residue at the third position (Ser3) needs to be octanoylated (modified with a moiety of 126 Da, C8H14O), in order to become biologically activ. The acylation is necessary for the peptide to bind and activate with its receptor, growth hormone secretagoue receptor (GHS-R).

This application note demonstrates the advantages of Electron Transfer Dissociation for the for site-specific peptide octanoylation in Human Ghrelin.

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