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抗衡离子对蜂毒肽聚集的影响。

The effect of counterions on melittin aggregation.

作者信息

Tatham A S, Hider R C, Drake A F

出版信息

Biochem J. 1983 Jun 1;211(3):683-6. doi: 10.1042/bj2110683.

DOI:10.1042/bj2110683
PMID:6882364
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1154414/
Abstract

Melittin, a surface-active polypeptide from bee venom, has an overall hydrophobic N-terminus, with basic residues clustered at the C-terminus. In aqueous solution melittin exists as a mixture of monomer and tetramer, the monomer adopting a predominantly random-coil configuration, whereas the tetramer is rich in alpha-helix. The tendency of melittin to aggregate is dependent on the counter-anions present in solution, the effect being most marked with phosphate, decreasing in the order HPO4(2-) greater than SO4(2-) greater than ClO4- greater than Cl-.

摘要

蜂毒肽是一种来自蜂毒的表面活性多肽,其N端总体呈疏水性,碱性残基聚集在C端。在水溶液中,蜂毒肽以单体和四聚体的混合物形式存在,单体主要呈无规卷曲构象,而四聚体富含α-螺旋。蜂毒肽的聚集倾向取决于溶液中存在的抗衡阴离子,其中磷酸根的影响最为显著,按HPO4(2-)>SO4(2-)>ClO4->Cl-的顺序递减。

相似文献

1
The effect of counterions on melittin aggregation.抗衡离子对蜂毒肽聚集的影响。
Biochem J. 1983 Jun 1;211(3):683-6. doi: 10.1042/bj2110683.
2
Dependence of melittin structure on its interaction with multivalent anions and with model membrane systems.蜂毒肽结构对其与多价阴离子及模型膜系统相互作用的依赖性。
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Thermodynamics of melittin tetramerization determined by circular dichroism and implications for protein folding.通过圆二色性测定的蜂毒肽四聚化的热力学及其对蛋白质折叠的影响。
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Conformation and aggregation of melittin: dependence on pH and concentration.蜂毒肽的构象与聚集:对pH值和浓度的依赖性。
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The structure of melittin in lipid bilayer membranes.
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Biochemistry. 1989 Oct 17;28(21):8614-23. doi: 10.1021/bi00447a052.
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3
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Circular-dichroism and fluorescence studies on melittin: effects of C-terminal modifications on tetramer formation and binding to phospholipid vesicles.蜂毒肽的圆二色性和荧光研究:C 端修饰对四聚体形成及与磷脂囊泡结合的影响
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Malonate transport in human red blood cells.
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The role of the phosphate group for the structure of phosphopeptide products of adenosine 3',5'-cyclic monophosphate-dependent protein kinase.磷酸基团在3',5'-环磷酸腺苷依赖性蛋白激酶磷酸肽产物结构中的作用。
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本文引用的文献

1
Secondary structure prediction of fish protamines.
Biochim Biophys Acta. 1980 Aug 21;624(2):420-7. doi: 10.1016/0005-2795(80)90083-5.
2
High-resolution 1H-NMR studies of self-aggregation of melittin in aqueous solution.蜂毒肽在水溶液中自聚集的高分辨率1H核磁共振研究。
Biochim Biophys Acta. 1980 Apr 25;622(2):231-44. doi: 10.1016/0005-2795(80)90034-3.
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High-resolution 1H-NMR studies of monomeric melittin in aqueous solution.水溶液中单体蜂毒素的高分辨率1H-NMR研究。
Biochim Biophys Acta. 1980 Apr 25;622(2):219-30. doi: 10.1016/0005-2795(80)90033-1.
4
Melittin forms crystals which are suitable for high resolution X-ray structural analysis and which reveal a molecular 2-fold axis of symmetry.蜂毒肽形成的晶体适合进行高分辨率X射线结构分析,并且揭示了分子的二重对称轴。
J Biol Chem. 1980 Mar 25;255(6):2578-82.
5
Melittin bound to dodecylphosphocholine micelles. H-NMR assignments and global conformational features.蜂毒素与十二烷基磷酸胆碱胶束结合。氢核磁共振谱归属及整体构象特征。
Biochim Biophys Acta. 1981 Sep 21;647(1):95-111. doi: 10.1016/0005-2736(81)90298-4.
6
Melittin-phospholipid interaction: evidence for melittin aggregation.蜂毒肽与磷脂的相互作用:蜂毒肽聚集的证据。
Biochim Biophys Acta. 1981 Apr 6;642(2):429-32. doi: 10.1016/0005-2736(81)90458-2.
7
Dependence of melittin structure on its interaction with multivalent anions and with model membrane systems.蜂毒肽结构对其与多价阴离子及模型膜系统相互作用的依赖性。
Int J Pept Protein Res. 1982 May;19(5):514-27. doi: 10.1111/j.1399-3011.1982.tb02637.x.
8
Infrared spectroscopic study of the secondary structure of melittin in water, 2-chloroethanol, and phospholipid bilayer dispersions.蜂毒肽在水、2-氯乙醇和磷脂双层分散体系中二级结构的红外光谱研究
Biochemistry. 1982 May 11;21(10):2305-12. doi: 10.1021/bi00539a006.
9
Conformation and aggregation of melittin: dependence on pH and concentration.蜂毒肽的构象与聚集:对pH值和浓度的依赖性。
Biochemistry. 1982 Feb 2;21(3):461-5. doi: 10.1021/bi00532a007.
10
Kinetics and mechanism of hemolysis induced by melittin and by a synthetic melittin analogue.蜂毒肽及一种合成蜂毒肽类似物诱导溶血的动力学和机制
Biophys J. 1982 Jan;37(1):329-38. doi: 10.1016/S0006-3495(82)84681-X.