These are laboratory-created molecules that are structurally similar to, but not identical with, naturally occurring peptides in the human body. They are designed to mimic the biological function of the native peptide, often with enhanced properties such as greater stability, longer half-life, or more selective receptor targeting. Their clinical utility lies in their ability to provide a more effective or convenient therapeutic profile.
Origin
The term originates in medicinal chemistry and biotechnology, driven by the need to overcome the rapid degradation and poor pharmacokinetic properties of many natural peptides. The process of creating an ‘analog’ involves modifying the amino acid sequence or structure of the parent peptide. This innovation allows for more practical and effective dosing regimens.
Mechanism
These analogs bind to the same receptors as their endogenous counterparts, such as Growth Hormone Releasing Hormone Receptors, but their modified structure makes them resistant to degradation by proteases. This resistance extends their duration of action in the bloodstream, reducing the required frequency of administration. The mechanism provides sustained, precise biological signaling for conditions like growth hormone deficiency.
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