Premium
Photolysis of crosslinked peptides from elastin of porcine aorta
Author(s) -
Davril Monique,
Han Kia-Ki,
Guay Mireille,
Lamy François
Publication year - 1979
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(79)80168-4
Subject(s) - humanities , chemistry , microbiology and biotechnology , art , biology
Elastin, a fibrous protein found in connective tissue is a hydrophobic, highly crosslinked insoluble protein. The study of its primary structure has been greatly hindered because no specific enzymatic or chemical method is known which would release a finite number of homogeneous peptides. Since the major crosslinks are tetrasubstituted pyridinium compounds, the (iso)desmosines [l] (1, fig.1) we are exploring the possibility of breaking speci~c~y the aromatic ring byphotolysis. The photochemic~ decomposition of free (iso)desmosines has been studied [2] and it was found that the primary photochemical event is the formation of a tetrasubstituted azabicyclo compound 2, which is subsequently hydrolysed to give an open chain aminoaldehyde 3. This compound can either recyclise to give a novel isomer of (iso)desmosines, photodesmosine 5 (in preparation) or be further hydrolysed to give free lysine and a trisubstituted analogue of glutaconic aldehyde 4. In this paper we wish to report on the photochemi~~ behavior of (iso)de~os~es present in highly reticulated peptides obtained by non-specific cleavage of aortic elastin [3].