The study and application of the molecular interactions governing how short chains of amino acids, acting as hormones or local mediators, bind to cell surface receptors to initiate intracellular cascades. This field examines the synthesis, degradation, receptor specificity, and downstream effector modulation unique to peptide-based communication systems. Understanding this chemistry is fundamental to comprehending rapid, localized endocrine responses.
Origin
Derived from biochemistry and molecular endocrinology, this term highlights the chemical nature of signaling molecules derived from proteolysis or specific gene transcription. Unlike steroid hormones which cross the membrane, peptides interact externally, necessitating specific receptor machinery. The chemistry dictates their short half-life and localized action profiles within the physiological milieu.
Mechanism
The mechanism involves the binding of the peptide ligand to its transmembrane G-protein coupled receptor or tyrosine kinase receptor, triggering conformational changes that activate intracellular second messengers like cAMP or calcium flux. These events rapidly modulate enzyme activity or gene transcription factors specific to the target cell type. Effective signaling requires precise stoichiometry between the peptide concentration and receptor density for accurate signal transduction.
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