BETA-STRUCTURE IN HUMAN AMYLIN AND 2 DESIGNER BETA-PEPTIDES - CD AND NMR SPECTROSCOPIC COMPARISONS SUGGEST SOLUBLE BETA-OLIGOMERS AND THE ABSENCE OF SIGNIFICANT POPULATIONS OF BETA-STRAND DIMERS
BETA-STRUCTURE IN HUMAN AMYLIN AND 2 DESIGNER BETA-PEPTIDES - CD AND NMR SPECTROSCOPIC COMPARISONS SUGGEST SOLUBLE BETA-OLIGOMERS AND THE ABSENCE OF SIGNIFICANT POPULATIONS OF BETA-STRAND DIMERS
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DOI：
10.1006/bbrc.1994.2574
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发表时间：
1994-11-15
影响因子：
3.1
通讯作者：
ANDERSEN, NH
中科院分区：
文献类型：
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作者：
CORT, J;LIU, ZH;ANDERSEN, NH
对于三种“β折叠”肽，观察到阳性远UV CD带的强度变化。在6% HFIP中，淀粉样物质（人胰腺胰淀素）在静置时显示出极强的192 nm条带，该条带在物理搅拌时减弱。在274 nm处同时形成的Tyr侧链带在搅拌下完全消失，将192 nm带的增强与β-片层的高度有序堆叠联系起来。核磁共振研究表明，这三种肽的β状态是低聚体，而不是β二聚体。由于与β-低聚物缓慢平衡的低浓度“无规卷曲”单体，成膜EAK肽显示NMR峰;显示强烈的195 nm带的更疏水的ELKA肽的溶液仅含有低聚物物质。在25%HFIP下的NMR研究揭示了抑制β-寡聚体形成的结构要求。(C)1994年出版社出版。
Intensity variation for the positive far UV CD band was observed for three 'beta-sheet' peptides. In 6% HFIP, an amyloidogenic species (human pancreatic amylin) displays, on standing, an extremely intense 192-nm band which diminishes upon physical agitation. A concurrently formed Tyr sidechain band at 274nm disappears completely with agitation, linking the enhancement of the 192-nm band to the highly ordered stacking of beta-sheets. NMR studies indicate that the beta-states of the three peptides are oligomeric, not beta dimers. A membrane-forming EAK peptide displays NMR peaks due to the low concentration of 'random coil' monomers present in slow equilibrium with beta-oligomers; solutions of a more hydrophobic ELKA peptide, which displays an intense 195-nm band, contain only oligomeric species. NMR studies at 25% HFIP revealed the structural requirements for inhibition of beta-oligomer formation. (C) 1994 Academic Press, Inc.