Cargando…
Spectroscopic characterization and in vitro studies of biological activity of bradykinin derivatives
Eleven multiple analogs of bradykinin—a peptide that is a natural ligand of B1 and B2 receptors but does not bind or activate the B1 receptor unless Arg(9) is removed from the sequence by the action of carboxypeptidase N—were synthesized. Their biological activity was examined on T-REx cell lines ex...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9643506/ https://www.ncbi.nlm.nih.gov/pubmed/36348016 http://dx.doi.org/10.1038/s41598-022-23448-7 |
_version_ | 1784826543121367040 |
---|---|
author | Proniewicz, Edyta Burnat, Grzegorz Domin, Helena Iłowska, Emilia Roman, Adam Prahl, Adam |
author_facet | Proniewicz, Edyta Burnat, Grzegorz Domin, Helena Iłowska, Emilia Roman, Adam Prahl, Adam |
author_sort | Proniewicz, Edyta |
collection | PubMed |
description | Eleven multiple analogs of bradykinin—a peptide that is a natural ligand of B1 and B2 receptors but does not bind or activate the B1 receptor unless Arg(9) is removed from the sequence by the action of carboxypeptidase N—were synthesized. Their biological activity was examined on T-REx cell lines expressing B1 or B2 receptors using the intracellular IP1 assay. The mRNA expression of B1R and B2R in the lysate of tumor cell lines, e.g., U87-MG (human astrocytoma), SHP-77 (human small cell lung cancer), and H4 (human brain glioma), was determined. For five B1R antagonists, adsorption at the liquid/solid interface (Au nanoparticles (AuNPs) served as the solid surface) was discussed in terms of the vibrations of molecular fragments (structural factors) responsible for the biological properties of these analogs. |
format | Online Article Text |
id | pubmed-9643506 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-96435062022-11-15 Spectroscopic characterization and in vitro studies of biological activity of bradykinin derivatives Proniewicz, Edyta Burnat, Grzegorz Domin, Helena Iłowska, Emilia Roman, Adam Prahl, Adam Sci Rep Article Eleven multiple analogs of bradykinin—a peptide that is a natural ligand of B1 and B2 receptors but does not bind or activate the B1 receptor unless Arg(9) is removed from the sequence by the action of carboxypeptidase N—were synthesized. Their biological activity was examined on T-REx cell lines expressing B1 or B2 receptors using the intracellular IP1 assay. The mRNA expression of B1R and B2R in the lysate of tumor cell lines, e.g., U87-MG (human astrocytoma), SHP-77 (human small cell lung cancer), and H4 (human brain glioma), was determined. For five B1R antagonists, adsorption at the liquid/solid interface (Au nanoparticles (AuNPs) served as the solid surface) was discussed in terms of the vibrations of molecular fragments (structural factors) responsible for the biological properties of these analogs. Nature Publishing Group UK 2022-11-08 /pmc/articles/PMC9643506/ /pubmed/36348016 http://dx.doi.org/10.1038/s41598-022-23448-7 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Proniewicz, Edyta Burnat, Grzegorz Domin, Helena Iłowska, Emilia Roman, Adam Prahl, Adam Spectroscopic characterization and in vitro studies of biological activity of bradykinin derivatives |
title | Spectroscopic characterization and in vitro studies of biological activity of bradykinin derivatives |
title_full | Spectroscopic characterization and in vitro studies of biological activity of bradykinin derivatives |
title_fullStr | Spectroscopic characterization and in vitro studies of biological activity of bradykinin derivatives |
title_full_unstemmed | Spectroscopic characterization and in vitro studies of biological activity of bradykinin derivatives |
title_short | Spectroscopic characterization and in vitro studies of biological activity of bradykinin derivatives |
title_sort | spectroscopic characterization and in vitro studies of biological activity of bradykinin derivatives |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9643506/ https://www.ncbi.nlm.nih.gov/pubmed/36348016 http://dx.doi.org/10.1038/s41598-022-23448-7 |
work_keys_str_mv | AT proniewiczedyta spectroscopiccharacterizationandinvitrostudiesofbiologicalactivityofbradykininderivatives AT burnatgrzegorz spectroscopiccharacterizationandinvitrostudiesofbiologicalactivityofbradykininderivatives AT dominhelena spectroscopiccharacterizationandinvitrostudiesofbiologicalactivityofbradykininderivatives AT iłowskaemilia spectroscopiccharacterizationandinvitrostudiesofbiologicalactivityofbradykininderivatives AT romanadam spectroscopiccharacterizationandinvitrostudiesofbiologicalactivityofbradykininderivatives AT prahladam spectroscopiccharacterizationandinvitrostudiesofbiologicalactivityofbradykininderivatives |