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利用肽阵列技术研究人工卷曲螺旋缔合中的优先相互作用网络。

Investigation of the network of preferred interactions in an artificial coiled-coil association using the peptide array technique.

机构信息

Institute of Chemistry and Biochemistry, Freie Universität Berlin, Takustrasse 3, 14195 Berlin, Germany.

出版信息

Beilstein J Org Chem. 2012;8:640-9. doi: 10.3762/bjoc.8.71. Epub 2012 Apr 25.

DOI:10.3762/bjoc.8.71
PMID:22563362
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3343290/
Abstract

We screened a randomized library and identified natural peptides that bound selectively to a chimeric peptide containing α-, β- and γ-amino acids. The SPOT arrays provide a means for the systematic study of the possible interaction space accessible to the αβγ-chimera. The mutational analysis reveals the dependence of the binding affinities of α-peptides to the αβγ-chimera, on the hydrophobicity and bulkiness of the side chains at the corresponding hydrophobic interface. The stability of the resulting heteroassemblies was further confirmed in solution by CD and thermal denaturation.

摘要

我们筛选了一个随机文库，并鉴定出能与包含α-、β-和γ-氨基酸的嵌合肽特异性结合的天然肽。SPOT 阵列为系统研究αβγ-嵌合体可及的可能相互作用空间提供了一种手段。突变分析揭示了α-肽与αβγ-嵌合体的结合亲和力取决于相应疏水面上侧链的疏水性和体积。通过 CD 和热变性，在溶液中进一步证实了所得杂组装体的稳定性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4170/3343290/35a8ba79b40b/Beilstein_J_Org_Chem-08-640-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4170/3343290/6e36f83fa7c7/Beilstein_J_Org_Chem-08-640-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4170/3343290/22cc71d2e212/Beilstein_J_Org_Chem-08-640-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4170/3343290/b3caa2d51c63/Beilstein_J_Org_Chem-08-640-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4170/3343290/7812ebe5ef28/Beilstein_J_Org_Chem-08-640-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4170/3343290/6f070969dba5/Beilstein_J_Org_Chem-08-640-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4170/3343290/35a8ba79b40b/Beilstein_J_Org_Chem-08-640-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4170/3343290/6e36f83fa7c7/Beilstein_J_Org_Chem-08-640-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4170/3343290/22cc71d2e212/Beilstein_J_Org_Chem-08-640-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4170/3343290/b3caa2d51c63/Beilstein_J_Org_Chem-08-640-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4170/3343290/7812ebe5ef28/Beilstein_J_Org_Chem-08-640-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4170/3343290/6f070969dba5/Beilstein_J_Org_Chem-08-640-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4170/3343290/35a8ba79b40b/Beilstein_J_Org_Chem-08-640-g007.jpg

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本文引用的文献

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A systematic study of fundamentals in α-helical coiled coil mimicry by alternating sequences of β- and γ-amino acids.通过交替使用β-和γ-氨基酸的序列对α-螺旋卷曲螺旋模拟物的基础进行系统研究。
Amino Acids. 2011 Aug;41(3):733-42. doi: 10.1007/s00726-011-0941-z. Epub 2011 Jun 3.
2
A helix-forming αβγ-chimeric peptide with catalytic activity: a hybrid peptide ligase.一种具有催化活性的螺旋形成的 αβγ-嵌合肽：杂合肽连接酶。
Chem Commun (Camb). 2011 Mar 28;47(12):3544-6. doi: 10.1039/c0cc03760e. Epub 2011 Feb 15.
3
Complex networks govern coiled-coil oligomerization--predicting and profiling by means of a machine learning approach.
复杂网络控制着螺旋卷曲寡聚体的形成——通过机器学习方法进行预测和分析。
Mol Cell Proteomics. 2011 May;10(5):M110.004994. doi: 10.1074/mcp.M110.004994. Epub 2011 Feb 10.
4
Chemical modifications designed to improve peptide stability: incorporation of non-natural amino acids, pseudo-peptide bonds, and cyclization.旨在提高肽稳定性的化学修饰：非天然氨基酸的掺入、拟肽键和环化。
Curr Pharm Des. 2010;16(28):3185-203. doi: 10.2174/138161210793292555.
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A study to assess the cross-reactivity of cellulose membrane-bound peptides with detection systems: an analysis at the amino acid level.
J Pept Sci. 2010 Jun;16(6):297-302. doi: 10.1002/psc.1237.
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A beta/gamma motif to mimic alpha-helical turns in proteins.一种模拟蛋白质中α-螺旋转角的β/γ基序。
Chembiochem. 2010 Feb 15;11(3):335-9. doi: 10.1002/cbic.200900700.
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