Effects of Cyclization on Activity and Stability of α-Conotoxin TxIB

α-Conotoxin TxIB specifically blocked α6/α3β2β3 acetylcholine receptors (nAChRs), and it could be a potential probe for studying addiction and other diseases related to α6/α3β2β3 nAChRs. However, as a peptide, TxIB may suffer from low stability, short half-life, and poor bioavailability. In this stu...
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Autor*in:	Xincan Li [verfasserIn] Shuai Wang [verfasserIn] Xiaopeng Zhu [verfasserIn] Dongting Zhangsun [verfasserIn] Yong Wu [verfasserIn] Sulan Luo [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2020

Schlagwörter:	α-conotoxin TxIB α6/α3β2β3 nAChRs cyclization activity stability

Übergeordnetes Werk:	In: Marine Drugs - MDPI AG, 2005, 18(2020), 4, p 180
Übergeordnetes Werk:	volume:18 ; year:2020 ; number:4, p 180

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/md18040180

Katalog-ID:	DOAJ086570196

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spelling	10.3390/md18040180 doi (DE-627)DOAJ086570196 (DE-599)DOAJc75fa722c2c540b4b9c159199027d8df DE-627 ger DE-627 rakwb eng QH301-705.5 Xincan Li verfasserin aut Effects of Cyclization on Activity and Stability of α-Conotoxin TxIB 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier α-Conotoxin TxIB specifically blocked α6/α3β2β3 acetylcholine receptors (nAChRs), and it could be a potential probe for studying addiction and other diseases related to α6/α3β2β3 nAChRs. However, as a peptide, TxIB may suffer from low stability, short half-life, and poor bioavailability. In this study, cyclization of TxIB was used to improve its stability. Four cyclic mutants of TxIB (cTxIB) were synthesized, and the inhibition of these analogues on α6/α3β2β3 nAChRs as well as their stability in human serum were measured. All cyclized analogues had similar activity compared to wild-type TxIB, which indicated that backbone cyclization of TxIB had no significant effect on its activity. Cyclization of TxIB with a seven-residue linker improved its stability significantly in human serum. Besides this, the results showed that cyclization maintained the activity of α-conotoxin TxIB, which is conducive to its future application. α-conotoxin TxIB α6/α3β2β3 nAChRs cyclization activity stability Biology (General) Shuai Wang verfasserin aut Xiaopeng Zhu verfasserin aut Dongting Zhangsun verfasserin aut Yong Wu verfasserin aut Sulan Luo verfasserin aut In Marine Drugs MDPI AG, 2005 18(2020), 4, p 180 (DE-627)477992420 (DE-600)2175190-0 16603397 nnns volume:18 year:2020 number:4, p 180 https://doi.org/10.3390/md18040180 kostenfrei https://doaj.org/article/c75fa722c2c540b4b9c159199027d8df kostenfrei https://www.mdpi.com/1660-3397/18/4/180 kostenfrei https://doaj.org/toc/1660-3397 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_381 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 18 2020 4, p 180
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allfieldsSound	10.3390/md18040180 doi (DE-627)DOAJ086570196 (DE-599)DOAJc75fa722c2c540b4b9c159199027d8df DE-627 ger DE-627 rakwb eng QH301-705.5 Xincan Li verfasserin aut Effects of Cyclization on Activity and Stability of α-Conotoxin TxIB 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier α-Conotoxin TxIB specifically blocked α6/α3β2β3 acetylcholine receptors (nAChRs), and it could be a potential probe for studying addiction and other diseases related to α6/α3β2β3 nAChRs. However, as a peptide, TxIB may suffer from low stability, short half-life, and poor bioavailability. In this study, cyclization of TxIB was used to improve its stability. Four cyclic mutants of TxIB (cTxIB) were synthesized, and the inhibition of these analogues on α6/α3β2β3 nAChRs as well as their stability in human serum were measured. All cyclized analogues had similar activity compared to wild-type TxIB, which indicated that backbone cyclization of TxIB had no significant effect on its activity. Cyclization of TxIB with a seven-residue linker improved its stability significantly in human serum. Besides this, the results showed that cyclization maintained the activity of α-conotoxin TxIB, which is conducive to its future application. α-conotoxin TxIB α6/α3β2β3 nAChRs cyclization activity stability Biology (General) Shuai Wang verfasserin aut Xiaopeng Zhu verfasserin aut Dongting Zhangsun verfasserin aut Yong Wu verfasserin aut Sulan Luo verfasserin aut In Marine Drugs MDPI AG, 2005 18(2020), 4, p 180 (DE-627)477992420 (DE-600)2175190-0 16603397 nnns volume:18 year:2020 number:4, p 180 https://doi.org/10.3390/md18040180 kostenfrei https://doaj.org/article/c75fa722c2c540b4b9c159199027d8df kostenfrei https://www.mdpi.com/1660-3397/18/4/180 kostenfrei https://doaj.org/toc/1660-3397 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_381 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 18 2020 4, p 180
language	English
source	In Marine Drugs 18(2020), 4, p 180 volume:18 year:2020 number:4, p 180
sourceStr	In Marine Drugs 18(2020), 4, p 180 volume:18 year:2020 number:4, p 180
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	α-conotoxin TxIB α6/α3β2β3 nAChRs cyclization activity stability Biology (General)
isfreeaccess_bool	true
container_title	Marine Drugs
authorswithroles_txt_mv	Xincan Li @@aut@@ Shuai Wang @@aut@@ Xiaopeng Zhu @@aut@@ Dongting Zhangsun @@aut@@ Yong Wu @@aut@@ Sulan Luo @@aut@@
publishDateDaySort_date	2020-01-01T00:00:00Z
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callnumber-first	Q - Science
author	Xincan Li
spellingShingle	Xincan Li misc QH301-705.5 misc α-conotoxin TxIB misc α6/α3β2β3 nAChRs misc cyclization misc activity misc stability misc Biology (General) Effects of Cyclization on Activity and Stability of α-Conotoxin TxIB
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topic_title	QH301-705.5 Effects of Cyclization on Activity and Stability of α-Conotoxin TxIB α-conotoxin TxIB α6/α3β2β3 nAChRs cyclization activity stability
topic	misc QH301-705.5 misc α-conotoxin TxIB misc α6/α3β2β3 nAChRs misc cyclization misc activity misc stability misc Biology (General)
topic_unstemmed	misc QH301-705.5 misc α-conotoxin TxIB misc α6/α3β2β3 nAChRs misc cyclization misc activity misc stability misc Biology (General)
topic_browse	misc QH301-705.5 misc α-conotoxin TxIB misc α6/α3β2β3 nAChRs misc cyclization misc activity misc stability misc Biology (General)
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title	Effects of Cyclization on Activity and Stability of α-Conotoxin TxIB
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title_full	Effects of Cyclization on Activity and Stability of α-Conotoxin TxIB
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title_sort	effects of cyclization on activity and stability of α-conotoxin txib
callnumber	QH301-705.5
title_auth	Effects of Cyclization on Activity and Stability of α-Conotoxin TxIB
abstract	α-Conotoxin TxIB specifically blocked α6/α3β2β3 acetylcholine receptors (nAChRs), and it could be a potential probe for studying addiction and other diseases related to α6/α3β2β3 nAChRs. However, as a peptide, TxIB may suffer from low stability, short half-life, and poor bioavailability. In this study, cyclization of TxIB was used to improve its stability. Four cyclic mutants of TxIB (cTxIB) were synthesized, and the inhibition of these analogues on α6/α3β2β3 nAChRs as well as their stability in human serum were measured. All cyclized analogues had similar activity compared to wild-type TxIB, which indicated that backbone cyclization of TxIB had no significant effect on its activity. Cyclization of TxIB with a seven-residue linker improved its stability significantly in human serum. Besides this, the results showed that cyclization maintained the activity of α-conotoxin TxIB, which is conducive to its future application.
abstractGer	α-Conotoxin TxIB specifically blocked α6/α3β2β3 acetylcholine receptors (nAChRs), and it could be a potential probe for studying addiction and other diseases related to α6/α3β2β3 nAChRs. However, as a peptide, TxIB may suffer from low stability, short half-life, and poor bioavailability. In this study, cyclization of TxIB was used to improve its stability. Four cyclic mutants of TxIB (cTxIB) were synthesized, and the inhibition of these analogues on α6/α3β2β3 nAChRs as well as their stability in human serum were measured. All cyclized analogues had similar activity compared to wild-type TxIB, which indicated that backbone cyclization of TxIB had no significant effect on its activity. Cyclization of TxIB with a seven-residue linker improved its stability significantly in human serum. Besides this, the results showed that cyclization maintained the activity of α-conotoxin TxIB, which is conducive to its future application.
abstract_unstemmed	α-Conotoxin TxIB specifically blocked α6/α3β2β3 acetylcholine receptors (nAChRs), and it could be a potential probe for studying addiction and other diseases related to α6/α3β2β3 nAChRs. However, as a peptide, TxIB may suffer from low stability, short half-life, and poor bioavailability. In this study, cyclization of TxIB was used to improve its stability. Four cyclic mutants of TxIB (cTxIB) were synthesized, and the inhibition of these analogues on α6/α3β2β3 nAChRs as well as their stability in human serum were measured. All cyclized analogues had similar activity compared to wild-type TxIB, which indicated that backbone cyclization of TxIB had no significant effect on its activity. Cyclization of TxIB with a seven-residue linker improved its stability significantly in human serum. Besides this, the results showed that cyclization maintained the activity of α-conotoxin TxIB, which is conducive to its future application.
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title_short	Effects of Cyclization on Activity and Stability of α-Conotoxin TxIB
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