Synthesis of heterotrimeric collagen models containing Arg residues in Y-positions and analysis of their conformational stability
Synthesis of heterotrimeric collagen models containing Arg residues in Y-positions and analysis of their conformational stability
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DOI：
10.1016/j.bmcl.2003.10.005
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发表时间：
2004-01-05
影响因子：
2.7
通讯作者：
Takahara, Y
中科院分区：
文献类型：
--
作者：
Koide, T;Nishikawa, Y;Takahara, Y
据报道，掺入胶原性主-客体肽Ac-（Gly-Pro-Hyp）（3）-Gly-Pro-Y-（Gly-Pro-Hyp）（4）-Gly-Gly-NH 2的Y-位置的Arg残基以及4（R）-羟脯氨酸（Hyp）残基稳定三螺旋结构。在这里，我们合成了异源三聚体胶原模型含有精氨酸在Y-位置利用胱氨酸结策略。使用圆二色谱法分析它们的热转变温度表明，随着Arg数量的增加，三螺旋稳定性意外降低。所获得的结果表明，在Y-位置上的Arg残基并不总是Hyp残基的等价物，并且它具有潜在的螺旋不稳定效应。(C)2003爱思唯尔有限公司。保留所有权利。
An Arg residue incorporated into the Y-position of collagenous host-guest peptide Ac-(Gly-Pro-Hyp)(3)-Gly-Pro-Y-(Gly-Pro-Hyp)(4)-Gly-Gly-NH2 is reported to stabilize the triple helical structure as well as a 4(R)-hydroxyproline (Hyp) residue. Here, we synthesized heterotrimeric collagen models containing Arg in Y-positions utilizing the cystine knot strategy. Analysis of their thermal transition temperatures using circular dichroism spectrometry demonstrated unexpected decrease in the triple helical stability as the number of Arg increased. The obtained results indicated that an Arg residue in a Y-position is not always an equivalent of a Hyp residue, and that it possesses a potential helix destabilizing effect. (C) 2003 Elsevier Ltd. All rights reserved.