Der Einfluss der O-Acetylierung auf das konformative Verhalten des Kollagen-Modellpeptides (L-Pro-L-Hyp-Gly)10 und von Gelatine
✍ Scribed by Rolf W. Weber; Hans Nitschmann
- Publisher
- John Wiley and Sons
- Year
- 1978
- Tongue
- German
- Weight
- 542 KB
- Volume
- 61
- Category
- Article
- ISSN
- 0018-019X
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✦ Synopsis
The Influence of O‐Acetylation upon the Conformational Behaviour of the Collagen Model Peptide (L‐pro‐L‐Hyp‐Gly)~10~ and of Gelatin
(L‐Pro‐L‐Hyp‐Gly)~10~ which can be considered as a model peptide for collagen structure studies has been synthesized by the Merrifield technique. Subsequently, the hydroxyprolin residues have been acetylated by acetic acid anhydride in trifluoroacetic acid. In the same way, the hydroxyl groups of commercial bovine gelatin have been selectively acetylated. The influence of blocking the hydroxyl groups upon the thermal stability of the tripel helix formed by (L‐Pro‐L‐Hyp‐Gly)~10~ and upon the transition temperature and the gel stability of the gelatin has been investigated by the measurement of optical rotation, circular dichroism, molecular weights and gel melting points. The results show that O‐acetylation reduces the thermal stability of the collagen‐like tripel helices formed in solution by the synthetic peptide and during the gelation process of gelatin. Our experiments support data previously published by various authors indicating that the hydroxyl group of hydroxyprolin plays an important role in stabilizing the collagen tripel helix. The possibility to use O‐acetylated gelatin with its reduced gel forming capability for the preparation of plasma substitute solutions is discussed.