Biological activity of lipophilic derivatives of peptide 562–572 of rat luteinizing hormone receptor

A study investigated the biological activity of lipophilic derivatives of peptide 562-572 of the rat luteinizing hormone receptor. This is the first study to demonstrate that the modification of the peptide corresponding to the C terminal region of the third intracellular loop of LHR with lipophilic residues of decanoic and palmitic acids greatly enhances their ability to influence the basal and hCG stimulated activity of adenylyl cyclase signaling system in rat testes and that this modification is effective only if the hydrophobic radical is located at the C terminus of the peptide, mimicking the sixth transmembrane domain of LHR and being comparable to that domain in size and hydrophobicity.