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Issue 69, 2019
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Selective recognition of human telomeric G-quadruplex with designed peptide via hydrogen bonding followed by base stacking interactions

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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.

Graphical abstract: Selective recognition of human telomeric G-quadruplex with designed peptide via hydrogen bonding followed by base stacking interactions

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Supplementary files

Article information


Submitted
25 Oct 2019
Accepted
26 Nov 2019
First published
04 Dec 2019

This article is Open Access

RSC Adv., 2019,9, 40255-40262
Article type
Paper

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

S. Tyagi, S. Saxena, N. Kundu, T. Sharma, A. Chakraborty, S. Kaur, D. Miyoshi and J. Shankaraswamy, RSC Adv., 2019, 9, 40255
DOI: 10.1039/C9RA08761C

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