This page has only limited features, please log in for full access.

Unclaimed
Chenhu Qin
Department of Biochemistry and Molecular Biology, College of Basic Medicine, Hubei University of Medicine, Shiyan 442000, China

Basic Info

Basic Info is private.

Honors and Awards

The user has no records in this section


Career Timeline

The user has no records in this section.


Short Biography

The user biography is not available.
Following
Followers
Co Authors
The list of users this user is following is empty.
Following: 0 users

Feed

Journal article
Published: 30 August 2021 in Toxins
Reads 0
Downloads 0

Thermally processed Buthus martensii Karsch scorpions are a traditional Chinese medical material for treating various diseases. However, their pharmacological foundation remains unclear. Here, a new degraded peptide of scorpion toxin was identified in Chinese scorpion medicinal material by proteomics. It was named BmK86-P1 and has six conserved cysteine residues. Homology modeling and circular dichroism spectra experiments revealed that BmK86-P1 not only contained representative disulfide bond-stabilized α-helical and β-sheet motifs but also showed remarkable stability at test temperatures from 20–95 °C. Electrophysiology experiments indicated that BmK86-P1 was a highly potent and selective inhibitor of the hKv1.2 channel with IC50 values of 28.5 ± 6.3 nM. Structural and functional dissection revealed that two residues of BmK86-P1 (i.e., Lys19 and Ile21) were the key residues that interacted with the hKv1.2 channel. In addition, channel chimeras and mutagenesis experiments revealed that three amino acids (i.e., Gln357, Val381 and Thr383) of the hKv1.2 channel were responsible for BmK86-P1 selectivity. This research uncovered a new bioactive peptide from traditional Chinese scorpion medicinal material that has desirable thermostability and Kv1.2 channel-specific activity, which strongly suggests that thermally processed scorpions are novel peptide resources for new drug discovery for the Kv1.2 channel-related ataxia and epilepsy diseases.

ACS Style

Chenhu Qin; Xuhua Yang; Zheng Zuo; Liuting Yang; Fan Yang; Zhijian Cao; Zongyun Chen; Yingliang Wu. BmK86-P1, a New Degradation Peptide with Desirable Thermostability and Kv1.2 Channel-Specific Activity from Traditional Chinese Scorpion Medicinal Material. Toxins 2021, 13, 610 .

AMA Style

Chenhu Qin, Xuhua Yang, Zheng Zuo, Liuting Yang, Fan Yang, Zhijian Cao, Zongyun Chen, Yingliang Wu. BmK86-P1, a New Degradation Peptide with Desirable Thermostability and Kv1.2 Channel-Specific Activity from Traditional Chinese Scorpion Medicinal Material. Toxins. 2021; 13 (9):610.

Chicago/Turabian Style

Chenhu Qin; Xuhua Yang; Zheng Zuo; Liuting Yang; Fan Yang; Zhijian Cao; Zongyun Chen; Yingliang Wu. 2021. "BmK86-P1, a New Degradation Peptide with Desirable Thermostability and Kv1.2 Channel-Specific Activity from Traditional Chinese Scorpion Medicinal Material." Toxins 13, no. 9: 610.