Structure and Chemistry of the Peptide Hormones of the Intermediate Lobe

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Abstract
The peptide hormones of the intermediate lobe are derived from a common precursor protein and are therefore biogenetically and structurally related. They represent a group of linear, flexible peptides which elicit a variety of physiological response. Structure-activity studies have shown that different segments of adjacent amino acid residues have a specific function (e.g. address, message, potentiation) in the interaction of each of these hormones with its receptor(s). This kind of organization of hormonal information is called sychnologic; it is the basic for the pleiotropic action of the opiomelanocortin peptides, i.e. the ability of related peptides to interact with different types of receptors in different target cells. Labelled peptide hormones with radioactive, fluorescent, or photolabile groups at defined sites are a prerequisite for studying hormone-receptor interaction. Multi-labelled derivatives of alpha-MSH are suitable for degradation and intracellular incorporation studies. Photoaffinity labelling of melanophore receptors with azidophenyl-containing analogues of alpha-MSH produces an irreversible stimulation of pigment cells. Covalent conjugates between peptide hormone receptors. These conjugates exhibit remarkable properties such as superpotency, strongly enhanced receptor affinity and prolonged action.

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