Peptide Sequence Specificity describes the absolute requirement for a specific, ordered chain of amino acids within a signaling peptide to elicit a precise biological effect via its intended receptor. Even minor alterations in the sequence, such as a single amino acid substitution, can drastically reduce or entirely abolish its intended physiological action. This specificity underpins the reliability of peptide hormone function.
Origin
This term is derived directly from biochemistry and protein structure analysis, where the primary structure dictates the tertiary conformation and thus receptor binding affinity. Specificity is a core tenet of molecular recognition in endocrinology, distinguishing one signaling molecule from another. It is crucial when considering peptide therapeutics.
Mechanism
Specificity is maintained through precise three-dimensional folding that creates a binding pocket complementary to the receptor surface, much like a lock and key mechanism. Once bound, the peptide induces a conformational change in the receptor, initiating the downstream signaling cascade. Degradation by peptidases, which are also sequence-aware, further dictates the effective duration of action for the native peptide.
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