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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.

Authors+Show Affiliations

The Key Laboratory of Protein Chemistry and Developmental Biology of Ministry of Education, Hunan Normal University, Changsha 410081, China.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

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 -