New analysis of the phylogenetic change of collagen thermostability

Abstract

Recent data concerning the thermostability and the primary structure of type IV collagens, some invertebrate collagens, and for the stability of synthetic collagen‐like polypeptides, show that our earlier analysis of the phylogenetic change of thermostability has some shortcomings. The results of the analysis were corrected and it has been shown that the dependence of denaturation temperature Td on 4‐hydroxyproline content is hyperbolic and the total Gly‐Pro‐Hyp sequence content is a main, but not exclusive, factor influencing the change of collagen thermostability. It appears possible that the same mechanism underlies the thermostability of fibril‐forming collagens of all animal life, ranging from Antarctic ice fish to at least one annelid (Alvinella pompejana) living at very high temperatures at the bottom of the ocean near thermal vents. © 2000 John Wiley & Sons, Inc. Biopoly 53: 523–528, 2000

4‐Chloroprolines: Synthesis, conformational analysis, and effect on the collagen triple helix

“…15,16 Why is proline hydroxylation essential to the formation of a stable ECM? It is known that collagens containing a high fraction of Hyp in the Yaa position are particularly stable, 17,18 but the physicochemical basis for this stability was unclear.…”

O‐acylation of hydroxyproline residues: Effect on peptide‐bond isomerization and collagen stability

“…The thermal stability of collagen has a positive correlation with its Hyp content. 3,4 The effects of Hyp stereochemistry and sequence on collagen stability have been explored with peptide mimics. 5 ,6 In seminal work, Prockop and coworkers showed that [(ProHypGly) 10 ] 3 is more stable than [(ProProGly) 10 ] 3 , whereas (HypProGly) 10 does not exhibit triple helix formation.…”

Procollagen trafficking, processing and fibrillogenesis

“…Hydroxylation stabilizes the structure of the collagen triple helix and increases its denaturation temperature (Berg and Prockop, 1973;Jimenez et al, 1973;Rosenbloom et al, 1973). There is also a positive correlation between the melting temperature of the triple helix and the extent of hydroxylation of proline residues (Burjanadze, 1979;Burjanadze, 2000;Burjanadze and Veis, 1997), and with the physiological temperature of an organism (Privalov, 1982). Interestingly, a recent report indicates that the melting temperature of collagen might lie slightly below, rather than above, body temperature and be further modulated in vivo by interactions with surrounding proteins (Leikina et al, 2002;Persikov and Brodsky, 2002).…”