Abstract
Collagen fibers, which make up 30% of all proteins in vertebrates, are extracellular
matrix proteins that provide mechanical strength to connective tissues such as skin
and bone, forming the structural foundation of the body. Deoxypyridinoline, a collagen
cross-linking amino acid first isolated from bovine bone in 1982, is released into
the bloodstream during bone metabolism alongside degraded bone tissue. This makes
it a promising biomarker for quantitatively assessing diseases associated with abnormal
bone resorption. In this study, we achieved the total synthesis of deoxypyridinoline
from commercially available amino acids in five steps with an overall yield of 20%.
This synthetic method provides a scalable alternative to isolating the compound from
natural sources. As part of ongoing research into its use as a biomarker, we also
synthesized isotopically labeled deoxypyridinoline-13C2,15N1, which can be used as an internal standard for quantitative analysis.
Key words
synthesis - amino acids - deoxypyridinoline - bone - collagen - isotopic labeling
