Abstract
Elastin is present in the extracellular matrix of various tissues, most abundantly
in the aorta and major vascular vessels, and is formed by self-assembly followed by
concomitant crosslinkers of tropoelastin, an elastin precursor. Desmosine is a pyridinium-based
tetrafunctional amino acid that serves as an important crosslinker to bind the polymeric
chains of peptides in the 3D network of elastin. Despite its significance, the detailed
structure of elastin has not been elucidated. In this work, the synthesis of a cyclic
desmosine peptide designed to mimic elastin, which could serve as a compound for mass
spectrometric analysis to elucidate crosslinking structures is reported. The synthesis
involved stepwise and regioselective palladium-catalyzed cross-couplings, and inter-
and intramolecular condensations.
Key words
desmosine - cyclic peptide - cross-coupling - condensation
