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

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-str...

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Detalles Bibliográficos
Autores principales: Tyagi, Shikhar, Saxena, Sarika, Kundu, Nikita, Sharma, Taniya, Chakraborty, Amlan, Kaur, Sarvpreet, Miyoshi, Daisuke, Shankaraswamy, Jadala
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2019
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9076235/
https://www.ncbi.nlm.nih.gov/pubmed/35542665
http://dx.doi.org/10.1039/c9ra08761c
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author Tyagi, Shikhar
Saxena, Sarika
Kundu, Nikita
Sharma, Taniya
Chakraborty, Amlan
Kaur, Sarvpreet
Miyoshi, Daisuke
Shankaraswamy, Jadala
author_facet Tyagi, Shikhar
Saxena, Sarika
Kundu, Nikita
Sharma, Taniya
Chakraborty, Amlan
Kaur, Sarvpreet
Miyoshi, Daisuke
Shankaraswamy, Jadala
author_sort Tyagi, Shikhar
collection PubMed
description 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.
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spelling pubmed-90762352022-05-09 Selective recognition of human telomeric G-quadruplex with designed peptide via hydrogen bonding followed by base stacking interactions Tyagi, Shikhar Saxena, Sarika Kundu, Nikita Sharma, Taniya Chakraborty, Amlan Kaur, Sarvpreet Miyoshi, Daisuke Shankaraswamy, Jadala RSC Adv Chemistry 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. The Royal Society of Chemistry 2019-12-04 /pmc/articles/PMC9076235/ /pubmed/35542665 http://dx.doi.org/10.1039/c9ra08761c Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/
spellingShingle Chemistry
Tyagi, Shikhar
Saxena, Sarika
Kundu, Nikita
Sharma, Taniya
Chakraborty, Amlan
Kaur, Sarvpreet
Miyoshi, Daisuke
Shankaraswamy, Jadala
Selective recognition of human telomeric G-quadruplex with designed peptide via hydrogen bonding followed by base stacking interactions
title Selective recognition of human telomeric G-quadruplex with designed peptide via hydrogen bonding followed by base stacking interactions
title_full Selective recognition of human telomeric G-quadruplex with designed peptide via hydrogen bonding followed by base stacking interactions
title_fullStr Selective recognition of human telomeric G-quadruplex with designed peptide via hydrogen bonding followed by base stacking interactions
title_full_unstemmed Selective recognition of human telomeric G-quadruplex with designed peptide via hydrogen bonding followed by base stacking interactions
title_short Selective recognition of human telomeric G-quadruplex with designed peptide via hydrogen bonding followed by base stacking interactions
title_sort selective recognition of human telomeric g-quadruplex with designed peptide via hydrogen bonding followed by base stacking interactions
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9076235/
https://www.ncbi.nlm.nih.gov/pubmed/35542665
http://dx.doi.org/10.1039/c9ra08761c
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