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Due to the increasing drug-resistant of Candida albicans (C. albicans), there is an urgent need to develop a novel therapeutic agent for C. albicans induced inflammatory disease treatment. Antimicrobial peptides (AMPs) are regarded as one of the most promising antifungal drugs. However, most of the designed AMPs showed side-effects. In the present study, 10 novel peptides were designed based on the sequence of frog skin secretions peptide (Ranacyclin AJ). Among them, AKK8 (RWRFKWWKK) exhibited the strongest antifungal effect against both standard and clinically isolated drug-resistant C. albicans. AKK8 killed C. albicans (within 30 min), and the antifungal effect lasted for 24 h, showed an efficient and long lasted antifungal effect against C. albicans. Notably, AKK8 showed low toxicity to human red blood cells and high stability in human serum. Moreover, AKK8 administration showed therapeutic effects on systemic infections mice induced by the clinical drug-resistant C. albicans, in a dose-depended manner. These findings suggested that AKK8 may be a potential candidate for the anti-inflammation treatments for diseases caused by clinical drug-resistant C. albicans.
Atikan Wubulikasimu; Yanting Huang; Ahmidin Wali; Abulimiti Yili; Mingqiang Rong. A designed antifungal peptide with therapeutic potential for clinical drug-resistant Candida albicans. Biochemical and Biophysical Research Communications 2020, 533, 404 -409.
AMA StyleAtikan Wubulikasimu, Yanting Huang, Ahmidin Wali, Abulimiti Yili, Mingqiang Rong. A designed antifungal peptide with therapeutic potential for clinical drug-resistant Candida albicans. Biochemical and Biophysical Research Communications. 2020; 533 (3):404-409.
Chicago/Turabian StyleAtikan Wubulikasimu; Yanting Huang; Ahmidin Wali; Abulimiti Yili; Mingqiang Rong. 2020. "A designed antifungal peptide with therapeutic potential for clinical drug-resistant Candida albicans." Biochemical and Biophysical Research Communications 533, no. 3: 404-409.
Spider venoms contain many functional proteins/peptides such as proteinases, serine/cysteine proteinase inhibitors, insecticidal toxins, and ion channel toxins. However, to date, no peptide toxin with procoagulant activities has been identified from spider venom. In this study, a novel toxin LCTX-F2 with coagulation-promoting activity was identified and characterized in the venom of the spider Lycosa singoriensis (L. singoriensis). LCTX-F2 significantly shortened activated partial thromboplastin time (APTT), clotting time, and plasma recalcification time. This toxin directly interacted with several coagulation factors such as FXIIa, kallikrein, thrombin, and FXa and increased their protease activities. In liver bleeding and tail bleeding mouse models, LCTX-F2 significantly decreased the number of blood cells and bleeding time in a dose-dependent manner. At the same dosage, LCTX-F2 exhibited a more significant procoagulant effect than epsilon aminocaproic acid (EACA). Moreover, LCTX-F2 showed no cytotoxic or hemolytic activity against either normal cells or red blood cells. Our results suggested that LCTX-F2 is a potentiator of coagulation factors with the potential for use in the development of procoagulant drugs.
Pengpeng Li; Zhongzhe Zhang; Qiong Liao; Er Meng; James Mwangi; Ren Lai; Mingqiang Rong. LCTX-F2, a Novel Potentiator of Coagulation Factors From the Spider Venom of Lycosa singoriensis. Frontiers in Pharmacology 2020, 11, 1 .
AMA StylePengpeng Li, Zhongzhe Zhang, Qiong Liao, Er Meng, James Mwangi, Ren Lai, Mingqiang Rong. LCTX-F2, a Novel Potentiator of Coagulation Factors From the Spider Venom of Lycosa singoriensis. Frontiers in Pharmacology. 2020; 11 ():1.
Chicago/Turabian StylePengpeng Li; Zhongzhe Zhang; Qiong Liao; Er Meng; James Mwangi; Ren Lai; Mingqiang Rong. 2020. "LCTX-F2, a Novel Potentiator of Coagulation Factors From the Spider Venom of Lycosa singoriensis." Frontiers in Pharmacology 11, no. : 1.
Elastase is a globular glycoprotein and belongs to the chymotrypsin family. It is involved in several inflammatory cascades on the basis of cleaving the important connective tissue protein elastin, and is strictly regulated to a balance by several endogenous inhibitors. When elastase and its inhibitors are out of balance, severe diseases will develop, especially those involved in the cardiopulmonary system. Much attention has been attracted in seeking innovative elastase inhibitors and various advancements have been taken on clinical trials of these inhibitors. Natural functional peptides from venomous animals have been shown to have anti-protease properties. Here, we identified a kazal-type serine protease inhibitor named ShSPI from the cDNA library of the venom glands of Scolopendra hainanum. ShSPI showed significant inhibitory effects on porcine pancreatic elastase and human neutrophils elastase with Ki values of 225.83 ± 20 nM and 12.61 ± 2 nM, respectively. Together, our results suggest that ShSPI may be an excellent candidate to develop a drug for cardiopulmonary diseases.
Ning Luan; Qiyu Zhao; Zilei Duan; Mengyao Ji; Meichen Xing; Tengyu Zhu; James Mwangi; Mingqiang Rong; Jiangxin Liu; Ren Lai. Identification and Characterization of ShSPI, a Kazal-Type Elastase Inhibitor from the Venom of Scolopendra Hainanum. Toxins 2019, 11, 708 .
AMA StyleNing Luan, Qiyu Zhao, Zilei Duan, Mengyao Ji, Meichen Xing, Tengyu Zhu, James Mwangi, Mingqiang Rong, Jiangxin Liu, Ren Lai. Identification and Characterization of ShSPI, a Kazal-Type Elastase Inhibitor from the Venom of Scolopendra Hainanum. Toxins. 2019; 11 (12):708.
Chicago/Turabian StyleNing Luan; Qiyu Zhao; Zilei Duan; Mengyao Ji; Meichen Xing; Tengyu Zhu; James Mwangi; Mingqiang Rong; Jiangxin Liu; Ren Lai. 2019. "Identification and Characterization of ShSPI, a Kazal-Type Elastase Inhibitor from the Venom of Scolopendra Hainanum." Toxins 11, no. 12: 708.
Flaviviruses are single-stranded RNA viruses predominantly transmitted by the widely distributed Aedes mosquitoes in nature. As important human pathogens, the geographic reach of Flaviviruses and their threats to public health are increasing, but there is currently no approved specific drug for treatment. In recent years, the development of peptide antivirals has gained much attention. Natural host defense peptides which uniquely evolved to protect the hosts have been shown to have antiviral properties. In this study, we firstly collected the venom of the Alopecosa nagpag spider from Shangri-La County, Yunnan Province. A defense peptide named Av-LCTX-An1a (Antiviral-Lycotoxin-An1a) was identified from the spider venom, and its anti-dengue serotype-2 virus (DENV2) activity was verified in vitro. Moreover, a real-time fluorescence-based protease inhibition assay showed that An1a functions as a DENV2 NS2B-NS3 protease inhibitor. Furthermore, we also found that An1a restricts zika virus (ZIKV) infection by inhibiting the ZIKV NS2B-NS3 protease. Together, our findings not only demonstrate that An1a might be a candidate for anti-flavivirus drug but also indicate that spider venom is a potential resource library rich in antiviral precursor molecules.
Mengyao Ji; Tengyu Zhu; Meichen Xing; Ning Luan; James Mwangi; Xiuwen Yan; Guoxiang Mo; Mingqiang Rong; Bowen Li; Ren Lai; Lin Jin. An Antiviral Peptide from Alopecosa nagpag Spider Targets NS2B-NS3 Protease of Flaviviruses. Toxins 2019, 11, 584 .
AMA StyleMengyao Ji, Tengyu Zhu, Meichen Xing, Ning Luan, James Mwangi, Xiuwen Yan, Guoxiang Mo, Mingqiang Rong, Bowen Li, Ren Lai, Lin Jin. An Antiviral Peptide from Alopecosa nagpag Spider Targets NS2B-NS3 Protease of Flaviviruses. Toxins. 2019; 11 (10):584.
Chicago/Turabian StyleMengyao Ji; Tengyu Zhu; Meichen Xing; Ning Luan; James Mwangi; Xiuwen Yan; Guoxiang Mo; Mingqiang Rong; Bowen Li; Ren Lai; Lin Jin. 2019. "An Antiviral Peptide from Alopecosa nagpag Spider Targets NS2B-NS3 Protease of Flaviviruses." Toxins 11, no. 10: 584.
Nonhuman primates (NHPs) play an indispensable role in biomedical research because of their similarities in genetics, physiological, and neurological function to humans. Proteomics profiling of monkey heart could reveal significant cardiac biomarkers and help us to gain a better understanding of the pathogenesis of heart disease. However, the proteomic study of monkey heart is relatively lacking. Here, we performed the proteomics profiling of the normal monkey heart by measuring three major anatomical regions (vessels, valves, and chambers) based on iTRAQ‐coupled LC‐MS/MS analysis. Over 3,200 proteins were identified and quantified from three heart tissue samples. Furthermore, multiple bioinformatics analyses such as gene ontology analysis, protein–protein interaction analysis, and gene‐diseases association were used to investigate biological network of those proteins from each area. More than 60 genes in three heart regions are implicated with heart diseases such as hypertrophic cardiomyopathy, heart failure, and myocardial infarction. These genes associated with heart disease are mainly enriched in citrate cycle, amino acid degradation, and glycolysis pathway. At the anatomical level, the revelation of molecular characteristics of the healthy monkey heart would be an important starting point to investigate heart disease. As a unique resource, this study can serve as a reference map for future in‐depth research on cardiac disease‐related NHP model and novel biomarkers of cardiac injury.
Hao‐Liang Hu; Yu Kang; Yong Zeng; Ming Zhang; Qiong Liao; Ming‐Qiang Rong; Qin Zhang; Ren Lai. Region‐resolved proteomics profiling of monkey heart. Journal of Cellular Physiology 2019, 234, 13720 -13734.
AMA StyleHao‐Liang Hu, Yu Kang, Yong Zeng, Ming Zhang, Qiong Liao, Ming‐Qiang Rong, Qin Zhang, Ren Lai. Region‐resolved proteomics profiling of monkey heart. Journal of Cellular Physiology. 2019; 234 (8):13720-13734.
Chicago/Turabian StyleHao‐Liang Hu; Yu Kang; Yong Zeng; Ming Zhang; Qiong Liao; Ming‐Qiang Rong; Qin Zhang; Ren Lai. 2019. "Region‐resolved proteomics profiling of monkey heart." Journal of Cellular Physiology 234, no. 8: 13720-13734.
Endogenous peptides play an important role in multiple biological processes in many species. Liquid chromatography coupled tandem mass spectrometry (LC-MS/MS) is an important technique for detecting these peptides at a large scale. Herein, we present PPIP, which is a dedicated peptidogenomics software for identifying endogenous peptides based on peptidomics and RNA-Seq data. This software automates the de novo transcript assembly based on RNA-Seq data, construction of a protein reference database based on the de novo assembled transcripts, peptide identification, function analysis and HTML-based report generation. Different function components are integrated using Docker technology. The Docker image of PPIP is available at https://hub.docker.com/r/shawndp/ppip, and the source code under GPL-3 license is available at https://github.com/Shawn-Xu/PPIP. A user manual of PPIP is available at https://shawn-xu.github.io/PPIP.
Mingqiang Rong; Baojin Zhou; Ruo Zhou; Qiong Liao; Yong Zeng; Shaohang Xu; Zhonghua Liu. PPIP: Automated Software for Identification of Bioactive Endogenous Peptides. Journal of Proteome Research 2018, 18, 721 -727.
AMA StyleMingqiang Rong, Baojin Zhou, Ruo Zhou, Qiong Liao, Yong Zeng, Shaohang Xu, Zhonghua Liu. PPIP: Automated Software for Identification of Bioactive Endogenous Peptides. Journal of Proteome Research. 2018; 18 (2):721-727.
Chicago/Turabian StyleMingqiang Rong; Baojin Zhou; Ruo Zhou; Qiong Liao; Yong Zeng; Shaohang Xu; Zhonghua Liu. 2018. "PPIP: Automated Software for Identification of Bioactive Endogenous Peptides." Journal of Proteome Research 18, no. 2: 721-727.
Jingzhaotoxin-34 (JZTX-34) is a selective inhibitor of tetrodotoxin-sensitive (TTX-S) sodium channels. In this study, we found that JZTX-34 selectively acted on Nav1.7 with little effect on other sodium channel subtypes including Nav1.5. If the DIIS3-S4 linker of Nav1.5 is substituted by the correspond linker of Nav1.7, the sensitivity of Nav1.5 to JZTX-34 extremely increases to 1.05 µM. Meanwhile, a mutant D816R in the DIIS3-S4 linker of Nav1.7 decreases binding affinity of Nav1.7 to JZTX-34 about 32-fold. The reverse mutant R800D at the corresponding position in Nav1.5 greatly increased its binding affinity to JZTX-34. This implies that JZTX-34 binds to DIIS3-S4 linker of Nav1.7 and the critical residue of Nav1.7 is D816. Unlike β-scorpion toxin trapping sodium channel in an open state, activity of JZTX-34 requires the sodium channel to be in a resting state. JZTX-34 exhibits an obvious analgesic effect in a rodent pain model. Especially, it shows a longer duration and is more effective than morphine in hot pain models. In a formalin-induced pain model, JZTX-34 at dose of 2 mg/kg is equipotent with morphine (5 mg/kg) in the first phase and several-fold more effective than morphine in second phase. Taken together, our data indicate that JZTX-34 releases pain by selectively binding to the domain II voltage sensor of Nav1.7 in a closed configuration.
Xiongzhi Zeng; Pengpeng Li; Bo Chen; Juan Huang; Ren Lai; Jingze Liu; Mingqiang Rong. Selective Closed-State Nav1.7 Blocker JZTX-34 Exhibits Analgesic Effects against Pain. Toxins 2018, 10, 64 .
AMA StyleXiongzhi Zeng, Pengpeng Li, Bo Chen, Juan Huang, Ren Lai, Jingze Liu, Mingqiang Rong. Selective Closed-State Nav1.7 Blocker JZTX-34 Exhibits Analgesic Effects against Pain. Toxins. 2018; 10 (2):64.
Chicago/Turabian StyleXiongzhi Zeng; Pengpeng Li; Bo Chen; Juan Huang; Ren Lai; Jingze Liu; Mingqiang Rong. 2018. "Selective Closed-State Nav1.7 Blocker JZTX-34 Exhibits Analgesic Effects against Pain." Toxins 10, no. 2: 64.