[Biosynthesis and properties of collagen forming in the cartilage of chick embryos in the presence of various proline analogs].

Effect of proline analogues on biosynthesis and properties of collagen in chick embryo cartilage was studied. Azethidine-2-carboxylic acid, 3,4-dehydroproline, cis-fluoro-proline, cis-hydroxyproline and thiazolidine-4-carboxylic acid were found to inhibit the incorporation of 14C-proline into proteins by 66-89%. Introduction of proline analogues, instead of the amino acid, into the polypeptide chains of collagen caused the impairment of the enzymatic hydroxylation of the proline residues (formation of hydroxyproline). 3,4-dehydroproline possessed the highest inhibitory effect (80%) on formation of hydroxyproline. When it was introduced into alpha-chains of protocollagen, 3,4-dehydroproline inhibited 1.5-6-fold the cleavage of the protein by bacterial collagenase.