Imino acids and collagen triple helix stability: Characterization of collagen-like polypeptides containing Hyp-Hyp-Gly sequence repeats
Imino acids and collagen triple helix stability: Characterization of collagen-like polypeptides containing Hyp-Hyp-Gly sequence repeats
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DOI：
10.1021/ja047069h
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发表时间：
2004-09-22
影响因子：
15
通讯作者：
Zagari, A
中科院分区：
文献类型：
--
作者：
Berisio, R;Granata, V;Zagari, A
对影响蛋白质稳定性的因素的分析是一个激烈辩论的主题。特别具有挑战性的是对结构蛋白的研究，因为它们的功能就是它们的结构。其中包括胶原蛋白，它是骨骼、皮肤、软骨、肌腱和其他连接组织的关键结构成分。众所周知，胶原蛋白三螺旋的特征是含有羟基脯氨酸，其含量可根据宿主生物的需要调节三螺旋的热稳定性。由于胶原蛋白的复杂性和纤维性质，有关该蛋白的稳定性和结构的数据主要是通过使用类胶原蛋白多肽获得的。基于类胶原蛋白多肽的CD表征，我们在这里表明，在重复的三联体Hyp-Hyp-Gly的X位上的Hyp的存在显着地稳定了三螺旋。通过分子模拟，这种额外的稳定性被归因于属于相邻链的X和Y位置的Hyp残基之间形成的氢键。这份通讯还提供了关于含有脯氨酸衍生物的多肽的现有数据的综合解释。
The analysis of factors contributing to the stability of proteins is a subject of intense debate. Particularly challenging is the study of structural proteins, since their function is their structure. Among these is collagen, the key structural component of bones, skin, cartilage, tendons, and other connecting tissues. It is well established that the collagen triple helix is characterized by the presence of hydroxyproline, whose content modulates triple helix thermal stability according to the requirement of the host organism. Because of the complexity and the fibrous nature of collagen, data on the stability and structure of this protein have been mainly obtained by the use of collagen-like polypeptides. On the basis of CD characterization of collagen-like polypeptides we here show that the presence of Hyp at the X position of repeating triplets Hyp-Hyp-Gly stabilizes the triple helix significantly. This extra-stabilization has been ascribed, by using molecular modeling, to the formation of a hydrogen bond between Hyp residues belonging to the X and the Y positions of adjacent chains. This communication also provides a comprehensive interpretation of the ensemble of available data on polypeptides containing proline derivatives.