Peptide Sequencing is the analytical laboratory technique used to determine the exact order of amino acid residues in a peptide or protein. This process is foundational in molecular science and clinical endocrinology, as the specific sequence dictates the molecule’s three-dimensional structure, function, and receptor binding affinity. Accurate sequencing is essential for the quality control and development of bio-identical peptides and for identifying novel therapeutic targets within the body’s complex signaling network. It is the definitive method for molecular identification.
Origin
The methodology for peptide sequencing was pioneered by Frederick Sanger, who determined the sequence of insulin, marking a major breakthrough in biochemistry and establishing the foundation for protein chemistry. This technique has since been refined and automated, becoming a standard, indispensable tool in modern molecular biology and pharmaceutical development. The ability to read the amino acid code was a revolutionary step in understanding biological function.
Mechanism
The primary mechanism often involves Edman degradation, where amino acids are sequentially cleaved from the peptide chain and identified one by one. Modern methods also heavily rely on mass spectrometry, which fragments the peptide and measures the mass-to-charge ratio of the resulting fragments. By analyzing these data patterns, researchers can accurately reconstruct the full amino acid sequence, confirming the identity and purity of both endogenous and synthetically manufactured peptide compounds for clinical use.
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