重金属与含有半胱氨酸的卷曲螺旋肽结合的差异。

IF 1.8 4区 生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY
Prianka Luther, Aimee L. Boyle
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引用次数: 0

摘要

所有具有结构特征的蛋白质中有三分之一含有金属;然而,金属结合和肽/蛋白质折叠之间的相互作用尚未完全阐明。为了更好地理解金属结合如何影响肽折叠,应该在特定的支架内研究一系列金属。为此,我们修饰了一种含有组氨酸的卷曲螺旋肽,以创建一种含有半胱氨酸的支架,命名为CX3C,旨在结合重金属离子。此外,我们产生了一种名为CX2C的肽,它含有一个在天然蛋白质中更常见的结合位点。使用包括圆二色性(CD)光谱、UV-Vis光谱和尺寸排阻色谱与多角度光散射(SEC-MALS)耦合的分析技术的组合,我们检测了两种肽的金属结合特性的差异。由于极性半胱氨酸残基对疏水核心的破坏,这两种肽在apo状态下大部分未折叠。然而,通过添加Cd(II)、Pb(II)和Hg(II)来克服这种展开,并形成螺旋组件。两种肽对这些金属离子具有不同的亲和力,这一事实可能归因于离子的不同大小。我们还表明,肽复合物的低聚状态和金属离子的配位几何结构在两种肽支架之间不同。这些发现强调了肽一级结构的细微变化可能对金属结合有相当大的影响。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Differences in heavy metal binding to cysteine-containing coiled-coil peptides

Differences in heavy metal binding to cysteine-containing coiled-coil peptides

Differences in heavy metal binding to cysteine-containing coiled-coil peptides

One third of all structurally characterised proteins contain a metal; however, the interplay between metal-binding and peptide/protein folding has yet to be fully elucidated. To better understand how metal binding affects peptide folding, a range of metals should be studied within a specific scaffold. To this end, we modified a histidine-containing coiled-coil peptide to create a cysteine-containing scaffold, named CX3C, which was designed to bind heavy metal ions. In addition, we generated a peptide named CX2C, which contains a binding site more commonly found in natural proteins. Using a combination of analytical techniques including circular dichroism (CD) spectroscopy, UV–Vis spectroscopy and size-exclusion chromatography coupled to multi-angle light scattering (SEC-MALS), we examined the differences in the metal-binding properties of the two peptides. Both peptides are largely unfolded in the apo state due to the disruption of the hydrophobic core by inclusion of the polar cysteine residues. However, this unfolding is overcome by the addition of Cd(II), Pb(II) and Hg(II), and helical assemblies are formed. Both peptides have differing affinities for these metal ions, a fact likely attributed to the differing sizes of the ions. We also show that the oligomerisation state of the peptide complexes and the coordination geometries of the metal ions differ between the two peptide scaffolds. These findings highlight that subtle changes in the primary structure of a peptide can have considerable implications for metal binding.

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来源期刊
Journal of Peptide Science
Journal of Peptide Science 生物-分析化学
CiteScore
3.40
自引率
4.80%
发文量
83
审稿时长
1.7 months
期刊介绍: The official Journal of the European Peptide Society EPS The Journal of Peptide Science is a cooperative venture of John Wiley & Sons, Ltd and the European Peptide Society, undertaken for the advancement of international peptide science by the publication of original research results and reviews. The Journal of Peptide Science publishes three types of articles: Research Articles, Rapid Communications and Reviews. The scope of the Journal embraces the whole range of peptide chemistry and biology: the isolation, characterisation, synthesis properties (chemical, physical, conformational, pharmacological, endocrine and immunological) and applications of natural peptides; studies of their analogues, including peptidomimetics; peptide antibiotics and other peptide-derived complex natural products; peptide and peptide-related drug design and development; peptide materials and nanomaterials science; combinatorial peptide research; the chemical synthesis of proteins; and methodological advances in all these areas. The spectrum of interests is well illustrated by the published proceedings of the regular international Symposia of the European, American, Japanese, Australian, Chinese and Indian Peptide Societies.
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