3.4 Edman sequencing
In 1950, Pehr Edman pioneered Edman sequencing, a method to determine
protein amino acid sequences by reacting with and identifying N-terminal
residues of polypeptide chains. This technique has played a vital role
in biological drug development and quality control for therapeutic
proteins [10]. It continues to find applications in various life
science research fields. Edman’s PITC reaction was successfully used to
modify peptide amines and identify proteolytic protein cleavage in cell
signaling processes with high throughput [37]. It helped identify
the N-terminal tripeptide GTF262 of GP-2 in the Lassa virus, which
causes hemorrhagic fever [38].
In plant protein research, both MS and Edman sequencing were employed to
analyze rice leaf sheath proteins, revealing shared amino acid sequences
and showcasing their complementary use [39]. Moreover, Edman
degradation has contributed to the development of a photo thermally
responsive Nanoprobe. The probe releases the fluorescent dye Cy5.5 upon
exposure to an 808 nm laser, enhancing near-infrared (NIR) fluorescence
under slightly acidic conditions. This Nano probe enables fluorescence
imaging of v3 over-expressing U87MG cells in vitro and in vivo,
presenting a novel tool for biomedical imaging, drug delivery, and gene
administration [40].