Targeting of interleukin-10 receptor by a potential human interleukin-10 peptide efficiently blocks interleukin-10 pathway-dependent cell proliferation

Objective: Human interleukin-10 (IL-10) is a dimeric and pleiotropic cytokine that plays a crucial role in cellular immunoregulatory responses. As IL-10 binds to its receptors, IL-10Ra and IL-10Rb, it will suppress or induce the downstream cellular immune responses to protect from diseases. Material...

Full description

Saved in:
Bibliographic Details
Main Authors: Chun-Chun Chang, Cheng-Der Liu, Sheng-Feng Pan, Wei-Han Huang, Chih-Wen Peng, Hao-Jen Hsu
Format: Article
Language:English
Published: Wolters Kluwer Medknow Publications 2020-01-01
Series:Tzu Chi Medical Journal
Subjects:
Online Access:http://www.tcmjmed.com/article.asp?issn=1016-3190;year=2020;volume=32;issue=3;spage=245;epage=253;aulast=Chang
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1849323440247406592
author Chun-Chun Chang
Cheng-Der Liu
Sheng-Feng Pan
Wei-Han Huang
Chih-Wen Peng
Hao-Jen Hsu
author_facet Chun-Chun Chang
Cheng-Der Liu
Sheng-Feng Pan
Wei-Han Huang
Chih-Wen Peng
Hao-Jen Hsu
author_sort Chun-Chun Chang
collection DOAJ
description Objective: Human interleukin-10 (IL-10) is a dimeric and pleiotropic cytokine that plays a crucial role in cellular immunoregulatory responses. As IL-10 binds to its receptors, IL-10Ra and IL-10Rb, it will suppress or induce the downstream cellular immune responses to protect from diseases. Materials and Methods: In this study, a potential peptide derived from IL-10 based on molecular docking and structural analysis was designed and validated by a series of cell assays to block IL-10 binding to receptor IL-10Ra for the inhibition of cell growth. Results: The simulation results indicate that the designed peptide IL10NM25 bound to receptor IL-10Ra is dominated by electrostatic interactions, whereas van der Waals (VDW) and hydrophobic interactions are minor. The cell experiments showed that IL10NM25 specifically binds to receptor IL-10Ra on the cell surface of two B-lineage cell lines, B lymphoma derived (BJAB), and lymphoblastoid cell line, whereas the mutant and scramble peptides are not able to suppress the binding of IL-10 to receptor IL-10Ra, consistent with the molecular simulation predictions. Conclusion: This study demonstrates that structure-based peptide design can be effective in the development of peptide drug discovery.
format Article
id doaj-art-c51033471ebe49fea10d509f138f25dc
institution Kabale University
issn 1016-3190
2223-8956
language English
publishDate 2020-01-01
publisher Wolters Kluwer Medknow Publications
record_format Article
series Tzu Chi Medical Journal
spelling doaj-art-c51033471ebe49fea10d509f138f25dc2025-08-20T03:49:03ZengWolters Kluwer Medknow PublicationsTzu Chi Medical Journal1016-31902223-89562020-01-0132324525310.4103/tcmj.tcmj_237_19Targeting of interleukin-10 receptor by a potential human interleukin-10 peptide efficiently blocks interleukin-10 pathway-dependent cell proliferationChun-Chun ChangCheng-Der LiuSheng-Feng PanWei-Han HuangChih-Wen PengHao-Jen HsuObjective: Human interleukin-10 (IL-10) is a dimeric and pleiotropic cytokine that plays a crucial role in cellular immunoregulatory responses. As IL-10 binds to its receptors, IL-10Ra and IL-10Rb, it will suppress or induce the downstream cellular immune responses to protect from diseases. Materials and Methods: In this study, a potential peptide derived from IL-10 based on molecular docking and structural analysis was designed and validated by a series of cell assays to block IL-10 binding to receptor IL-10Ra for the inhibition of cell growth. Results: The simulation results indicate that the designed peptide IL10NM25 bound to receptor IL-10Ra is dominated by electrostatic interactions, whereas van der Waals (VDW) and hydrophobic interactions are minor. The cell experiments showed that IL10NM25 specifically binds to receptor IL-10Ra on the cell surface of two B-lineage cell lines, B lymphoma derived (BJAB), and lymphoblastoid cell line, whereas the mutant and scramble peptides are not able to suppress the binding of IL-10 to receptor IL-10Ra, consistent with the molecular simulation predictions. Conclusion: This study demonstrates that structure-based peptide design can be effective in the development of peptide drug discovery.http://www.tcmjmed.com/article.asp?issn=1016-3190;year=2020;volume=32;issue=3;spage=245;epage=253;aulast=Changcytokineinterleukin-10molecular dockingpeptide design
spellingShingle Chun-Chun Chang
Cheng-Der Liu
Sheng-Feng Pan
Wei-Han Huang
Chih-Wen Peng
Hao-Jen Hsu
Targeting of interleukin-10 receptor by a potential human interleukin-10 peptide efficiently blocks interleukin-10 pathway-dependent cell proliferation
Tzu Chi Medical Journal
cytokine
interleukin-10
molecular docking
peptide design
title Targeting of interleukin-10 receptor by a potential human interleukin-10 peptide efficiently blocks interleukin-10 pathway-dependent cell proliferation
title_full Targeting of interleukin-10 receptor by a potential human interleukin-10 peptide efficiently blocks interleukin-10 pathway-dependent cell proliferation
title_fullStr Targeting of interleukin-10 receptor by a potential human interleukin-10 peptide efficiently blocks interleukin-10 pathway-dependent cell proliferation
title_full_unstemmed Targeting of interleukin-10 receptor by a potential human interleukin-10 peptide efficiently blocks interleukin-10 pathway-dependent cell proliferation
title_short Targeting of interleukin-10 receptor by a potential human interleukin-10 peptide efficiently blocks interleukin-10 pathway-dependent cell proliferation
title_sort targeting of interleukin 10 receptor by a potential human interleukin 10 peptide efficiently blocks interleukin 10 pathway dependent cell proliferation
topic cytokine
interleukin-10
molecular docking
peptide design
url http://www.tcmjmed.com/article.asp?issn=1016-3190;year=2020;volume=32;issue=3;spage=245;epage=253;aulast=Chang
work_keys_str_mv AT chunchunchang targetingofinterleukin10receptorbyapotentialhumaninterleukin10peptideefficientlyblocksinterleukin10pathwaydependentcellproliferation
AT chengderliu targetingofinterleukin10receptorbyapotentialhumaninterleukin10peptideefficientlyblocksinterleukin10pathwaydependentcellproliferation
AT shengfengpan targetingofinterleukin10receptorbyapotentialhumaninterleukin10peptideefficientlyblocksinterleukin10pathwaydependentcellproliferation
AT weihanhuang targetingofinterleukin10receptorbyapotentialhumaninterleukin10peptideefficientlyblocksinterleukin10pathwaydependentcellproliferation
AT chihwenpeng targetingofinterleukin10receptorbyapotentialhumaninterleukin10peptideefficientlyblocksinterleukin10pathwaydependentcellproliferation
AT haojenhsu targetingofinterleukin10receptorbyapotentialhumaninterleukin10peptideefficientlyblocksinterleukin10pathwaydependentcellproliferation