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通过设计的肽氢键选择性识别人类端粒G-四链体,随后发生碱基堆积相互作用。

Selective recognition of human telomeric G-quadruplex with designed peptide hydrogen bonding followed by base stacking interactions.

作者信息

Tyagi Shikhar, Saxena Sarika, Kundu Nikita, Sharma Taniya, Chakraborty Amlan, Kaur Sarvpreet, Miyoshi Daisuke, Shankaraswamy Jadala

机构信息

Structural Biology Lab, Amity Institute of Biotechnology, Amity University Uttar Pradesh Sector-125, Expressway Highway Noida 201303 India

Department of Chemical Engineering, Monash University Clayton VIC 3800 Australia.

出版信息

RSC Adv. 2019 Dec 4;9(69):40255-40262. doi: 10.1039/c9ra08761c. eCollection 2019 Dec 3.

DOI:10.1039/c9ra08761c
PMID:35542665
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9076235/
Abstract

We described a novel synthetic peptide in which a glutamine residue binds through hydrogen bonding to a guanine-base and a trytophan residue intercalates with K resulting in stabilization of a human telomeric G-quadruplex with high selectivity over its complementary c-rich strand and a double-stranded DNA and its complementary C-rich strand. This peptide offers great potential for cancer treatment by inhibiting the telomere extension by telomerase.

摘要

我们描述了一种新型合成肽,其中谷氨酰胺残基通过氢键与鸟嘌呤碱基结合,色氨酸残基与钾离子嵌入,从而稳定人端粒G-四链体,相对于其互补的富含C链以及双链DNA及其互补的富含C链具有高选择性。这种肽通过抑制端粒酶的端粒延伸,在癌症治疗方面具有巨大潜力。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf9a/9076235/ddde065d02d2/c9ra08761c-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf9a/9076235/d9952a5f4910/c9ra08761c-s1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf9a/9076235/eda626cd1091/c9ra08761c-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf9a/9076235/9a805017d493/c9ra08761c-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf9a/9076235/0f6e29188c97/c9ra08761c-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf9a/9076235/ddde065d02d2/c9ra08761c-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf9a/9076235/d9952a5f4910/c9ra08761c-s1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf9a/9076235/eda626cd1091/c9ra08761c-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf9a/9076235/9a805017d493/c9ra08761c-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf9a/9076235/0f6e29188c97/c9ra08761c-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf9a/9076235/ddde065d02d2/c9ra08761c-f4.jpg

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Molecules. 2019 Jan 22;24(3):396. doi: 10.3390/molecules24030396.
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Cation-π interactions in protein-ligand binding: theory and data-mining reveal different roles for lysine and arginine.
在钾离子存在下,肽结合后人类c-Myc启动子G-四链体发生显著结构变化。
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