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[Synthesis and oxidative refolding of an N-terminal truncate of jingzhaotoxin-V and characterization of its activities of sodium channels].
Se Pu. 2007 Jul; 25(4):501-4.SP

Abstract

An N-terminal tyrosine residue truncate of Jingzhaotoxin-V (Y1-JZTX-V) was synthesized by solid-phase chemical methods using Fmoc-protected amino acids. Reversed-phase high performance liquid chromatography (RP-HPLC) and matrix assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF/TOF MS) were used to monitor the oxidative refolding of Y1-JZTX-V to find the optimal renaturation conditions of the synthetic linear peptide. When Y1-JZTX-V (0.05 mg/L) was dissolved in 0.1 mol/L Tris-HCl buffer containing 1 mmol/L GSH and 0.1 mmol/L GSSG at pH 7.50 and 4 degrees C, the best renaturation yield of the truncate toxin was obtained. Under the whole-cell patch-clamp mode, Y1-JZTX-V could inhibit tetrodotoxin-resistant (TTX-R) and tetrodotoxin-sensitive (TTX-S) sodium currents in adult rat dorsal root ganglion neurons with IC50 values of 160 nmol/L and 39.6 nmol/L, respectively. The inhibition potentiality of Y1-JZTX-V on TTX-S sodium currents was almost the same as the natural JZTX-V, while that on TTX-R sodium currents was obviously weakened. The IC50 value of Y1-JZTX-V on TTX-R sodium currents was 5.8 times as many as that of natural JZTX-V. Present findings indicated that the first tyrosine residue (Y1) in the N-terminal of JZTX-V was involved in the binding activities of JZTX-V to TTX-R sodium channels.

Links

clones/clone libraries

Authors+Show Affiliations

Quan M
The Key Laboratory of Protein Chemistry and Developmental Biology of Ministry of Education, Hunan Normal University, Changsha 410081, China.
Zeng X
No affiliation info available
Pi J
No affiliation info available
Deng M
No affiliation info available
Liang S
No affiliation info available

MeSH

Chromatography, High Pressure LiquidPeptidesProtein FoldingSodium ChannelsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSpider Venoms

Pub Type(s)

English Abstract
Journal Article

Language

chi

PubMed ID

17970106

Citation

Quan, Miaohua, et al. "[Synthesis and Oxidative Refolding of an N-terminal Truncate of jingzhaotoxin-V and Characterization of Its Activities of Sodium Channels]." Se Pu = Chinese Journal of Chromatography, vol. 25, no. 4, 2007, pp. 501-4.
Quan M, Zeng X, Pi J, et al. [Synthesis and oxidative refolding of an N-terminal truncate of jingzhaotoxin-V and characterization of its activities of sodium channels]. Se Pu. 2007;25(4):501-4.
Quan, M., Zeng, X., Pi, J., Deng, M., & Liang, S. (2007). [Synthesis and oxidative refolding of an N-terminal truncate of jingzhaotoxin-V and characterization of its activities of sodium channels]. Se Pu = Chinese Journal of Chromatography, 25(4), 501-4.
Quan M, et al. [Synthesis and Oxidative Refolding of an N-terminal Truncate of jingzhaotoxin-V and Characterization of Its Activities of Sodium Channels]. Se Pu. 2007;25(4):501-4. PubMed PMID: 17970106.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - [Synthesis and oxidative refolding of an N-terminal truncate of jingzhaotoxin-V and characterization of its activities of sodium channels]. AU - Quan,Miaohua, AU - Zeng,Xiongzhi, AU - Pi,Jianhui, AU - Deng,Meichun, AU - Liang,Songping, PY - 2007/11/1/pubmed PY - 2010/6/11/medline PY - 2007/11/1/entrez SP - 501 EP - 4 JF - Se pu = Chinese journal of chromatography JO - Se Pu VL - 25 IS - 4 N2 - An N-terminal tyrosine residue truncate of Jingzhaotoxin-V (Y1-JZTX-V) was synthesized by solid-phase chemical methods using Fmoc-protected amino acids. Reversed-phase high performance liquid chromatography (RP-HPLC) and matrix assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF/TOF MS) were used to monitor the oxidative refolding of Y1-JZTX-V to find the optimal renaturation conditions of the synthetic linear peptide. When Y1-JZTX-V (0.05 mg/L) was dissolved in 0.1 mol/L Tris-HCl buffer containing 1 mmol/L GSH and 0.1 mmol/L GSSG at pH 7.50 and 4 degrees C, the best renaturation yield of the truncate toxin was obtained. Under the whole-cell patch-clamp mode, Y1-JZTX-V could inhibit tetrodotoxin-resistant (TTX-R) and tetrodotoxin-sensitive (TTX-S) sodium currents in adult rat dorsal root ganglion neurons with IC50 values of 160 nmol/L and 39.6 nmol/L, respectively. The inhibition potentiality of Y1-JZTX-V on TTX-S sodium currents was almost the same as the natural JZTX-V, while that on TTX-R sodium currents was obviously weakened. The IC50 value of Y1-JZTX-V on TTX-R sodium currents was 5.8 times as many as that of natural JZTX-V. Present findings indicated that the first tyrosine residue (Y1) in the N-terminal of JZTX-V was involved in the binding activities of JZTX-V to TTX-R sodium channels. SN - 1000-8713 UR - https://www.unboundmedicine.com/medline/citation/17970106/[Synthesis_and_oxidative_refolding_of_an_N_terminal_truncate_of_jingzhaotoxin_V_and_characterization_of_its_activities_of_sodium_channels]_ L2 - https://antibodies.cancer.gov/detail/CPTC-TAP2-1 DB - PRIME DP - Unbound Medicine ER -