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Aggregation of Apolar Peptides in Organic Solvents. Concentration Dependence of 1H-NMR Parameters for Peptide NH Groups in $3_{10}$ Helical Decapeptide Fragment of Suzukacillin

机译:非极性肽在有机溶剂中的聚集。 Suzukacillin $ 3_ {10} $螺旋十肽片段中肽NH基的1H-NMR参数的浓度依赖性

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摘要

Peptide NH chemical shifts and their temperature dependences have been monitored as a function of concentration for the decapeptide, Boc-Aib-Pro-Val-Aib-Val-Ala- Aib-Ala-Aib-Aib-OMe in $CD{Cl}_3$ (0.001-0.06M) and ${({CD}_3)}_2SO$ (0.001-0.03M). The chemical shifts and temperature coefficients for all nine NH groups show no significant concentration dependence in ${({CD}_3)}_2SO$. Seven NH groups yield low values of temperature coefficients over the entire range, while one yields an intermediate value. In $CD{Cl}_3$, the Aib(1) NH group shows a large concentration dependence of both chemical shift and temperature coefficient, in contrast to the other eight NH groups. The data suggest that in ${({CD}_3)}_2SO$, the peptide adopts a $3_{10}$ helical conformation and is monomeric over the entire concentration range. In $CD{Cl}_3$, the $3_{10}$ helical peptide associates at a concentration of 0.01M, with the Aib(1) NH involved in an intermolecular hydrogen bond. Association does not disrupt the intramolecular hydrogen-bonding pattern in the decapeptide.
机译:已监测了$ CD {Cl} _3中十肽Boc-Aib-Pro-Val-Aib-Val-Ala-Aib-Ala-Aib-Aib-OMe的浓度变化对肽NH化学位移及其温度依赖性的影响。 $(0.001-0.06M)和$ {({CD} _3)} _ 2SO $(0.001-0.03M)。所有九个NH基团的化学位移和温度系数在$ {({CD} _3)} _ 2SO $中均无明显的浓度依赖性。七个NH基团在整个范围内产生较低的温度系数值,而一个则产生中间值。在$ CD {Cl} _3 $中,与其他八个NH组相反,Aib(1)NH组对化学位移和温度系数的浓度依赖性很大。数据表明,在$ {({CD} _3)} _ 2SO $中,该肽采用$ 3_ {10} $螺旋构象,并且在整个浓度范围内均为单体。在$ CD {Cl} _3 $中,$ 3_ {10} $螺旋肽以0.01M的浓度缔合,而Aib(1)NH参与分子间氢键。缔合不会破坏十肽中的分子内氢键模式。

著录项

  • 作者

    Iqbal M; Balaram P;

  • 作者单位
  • 年度 1982
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  • 原文格式 PDF
  • 正文语种 {"code":"en","name":"English","id":9}
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