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学者姓名：杨娟娟
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Abstract ：
为提高铁观音茶精油的稳定性,利用喷雾干燥法制备稳定的铁观音茶精油微胶囊.通过单因素和正交试验探究壁材的种类和浓度、芯壁比、包埋温度对微胶囊包埋效果的影响,研究微胶囊的分子结构、微观状态和稳定性等.以明胶、阿拉伯树胶和麦芽糊精为壁材(浓度比为1∶1∶1),在壁材浓度1％(w/v),芯壁比为1∶2(w/w),均质温度为50℃条件下,制得精油微胶囊包埋率为97.12％,产率为62.44％.红外光谱分析结果证实铁观音茶精油被成功包埋;扫描电镜分析结果显示微胶囊囊壁结构相对完整,表面光滑;微胶囊的释放动力研究结果表明微胶囊在4,25℃时达到精油缓慢释放的效果.研究为铁观音茶精油的拓展应用提供理论参考和数据支撑.
Keyword ：
壁材 壁材 微胶囊 微胶囊 稳定性 稳定性 结构表征 结构表征 铁观音茶精油 铁观音茶精油
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| GB/T 7714 | 操晓亮 , 薛婉茹 , 庄志雄 et al. 铁观音茶精油微胶囊化制备及结构表征 [J]. | 包装与食品机械 , 2023 , 41 (6) : 40-45,52 . |
| MLA | 操晓亮 et al. "铁观音茶精油微胶囊化制备及结构表征" . | 包装与食品机械 41 . 6 (2023) : 40-45,52 . |
| APA | 操晓亮 , 薛婉茹 , 庄志雄 , 谢李玲 , 叶淑芳 , 孟春 et al. 铁观音茶精油微胶囊化制备及结构表征 . | 包装与食品机械 , 2023 , 41 (6) , 40-45,52 . |
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Immunotherapy has revolutionized cancer treatment, but its efficacy is severely hindered by the lack of effective predictors. Herein, we developed a homogeneous, low-volume, efficient, and sensitive exosomal programmed death-ligand 1 (PD-L1, a type of transmembrane protein) quantitation method for cancer diagnosis and immunotherapy response prediction (HOLMES-Exo(PD-L1)). The method combines a newly evolved aptamer that efficiently binds to PD-L1 with less hindrance by antigen glycosylation than antibody, and homogeneous thermophoresis with a rapid binding kinetic. As a result, HOLMES-Exo(PD-L1) is higher in sensitivity, more rapid in reaction time, and easier to operate than existing enzyme-linked immunosorbent assay (ELISA)-based methods. As a consequence of an outstanding improvement of sensitivity, the level of circulating exosomal PD-L1 detected by HOLMES-Exo(PD-L1) can effectively distinguish cancer patients from healthy volunteers, and for the first time was found to correlate positively with the metastasis of adenocarcinoma. Overall, HOLMES-Exo(PD-L1) brings a fresh approach to exosomal PD-L1 quantitation, offering unprecedented potential for early cancer diagnosis and immunotherapy response prediction.
Keyword ：
aptamers aptamers exosomes exosomes liquid biopsy liquid biopsy PD-L1 PD-L1 thermophoresis thermophoresis
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| GB/T 7714 | Huang, Mengjiao , Yang, Juanjuan , Wang, Teng et al. Homogeneous, Low-volume, Efficient, and Sensitive Quantitation of Circulating Exosomal PD-L1 for Cancer Diagnosis and Immunotherapy Response Prediction [J]. | ANGEWANDTE CHEMIE-INTERNATIONAL EDITION , 2020 , 59 (12) : 4800-4805 . |
| MLA | Huang, Mengjiao et al. "Homogeneous, Low-volume, Efficient, and Sensitive Quantitation of Circulating Exosomal PD-L1 for Cancer Diagnosis and Immunotherapy Response Prediction" . | ANGEWANDTE CHEMIE-INTERNATIONAL EDITION 59 . 12 (2020) : 4800-4805 . |
| APA | Huang, Mengjiao , Yang, Juanjuan , Wang, Teng , Song, Jia , Xia, Jinglu , Wu, Lingling et al. Homogeneous, Low-volume, Efficient, and Sensitive Quantitation of Circulating Exosomal PD-L1 for Cancer Diagnosis and Immunotherapy Response Prediction . | ANGEWANDTE CHEMIE-INTERNATIONAL EDITION , 2020 , 59 (12) , 4800-4805 . |
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Ribosomal protein S1 (RpsA) has been identified as a novel target of pyrazinoic acid (POA), which is the active form of pyrazinamide (PZA), in vivo. RpsA plays a crucial role in trans-translation, which is widespread in microbes. In our investigation, we first described the discovery of promising RpsA antagonists for drug-resistant mycobacterium (MtRpsAd438A) and M. smegmatis, as well as wild-type M. tuberculosis. These antagonists were discovered via structure/ligand-based virtual screening approaches. A total of 21 targeted compounds were selected by virtual screening, combined scores, affinity, similarities and rules for potential as drugs. Next, the affinities of these compounds for three targeted proteins were tested in vitro by applying various technologies, including fluorescence quenching titration (FQT), saturation transfer difference (STD), and chemical shift perturbation (CSP) assays. The results showed that seven compounds had a high affinity for the targeted proteins. Our discovery set the stage for discovering new chemical entities (NCEs) for PZA-resistant tuberculosis and providing key residues for rational drug design to target RpsA.
Keyword ：
Drug-resistant Drug-resistant RPS1 RPS1 Trans-translation Trans-translation Virtual screening Virtual screening
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| GB/T 7714 | Zhi, Yunbao , Dai, Yazhuang , Yang, Juanjuan et al. Lead compounds and key residues of ribosomal protein S1 in drug-resistant Mycobacterium tuberculosis [J]. | BIOORGANIC CHEMISTRY , 2019 , 82 : 58-67 . |
| MLA | Zhi, Yunbao et al. "Lead compounds and key residues of ribosomal protein S1 in drug-resistant Mycobacterium tuberculosis" . | BIOORGANIC CHEMISTRY 82 (2019) : 58-67 . |
| APA | Zhi, Yunbao , Dai, Yazhuang , Yang, Juanjuan , Tan, Shuhua , Lin, Donghai , Lin, Kejiang . Lead compounds and key residues of ribosomal protein S1 in drug-resistant Mycobacterium tuberculosis . | BIOORGANIC CHEMISTRY , 2019 , 82 , 58-67 . |
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Mycobacterium tuberculosis (Mtb) is the key devastating bacterial pathogen responsible for tuberculosis. Increasing emergence of multi-drug-resistant, extensively drug-resistant, and rifampicin/isoniazid-resistant strains of Mtb makes the discovery of validated drug targets an urgent priority. As a vital translational component of the protein biosynthesis system, elongation factor Tu (EF-Tu) is an important molecular switch responsible for selection and binding of the cognate aminoacyl-tRNA to the acceptor site on the ribosome. In addition, EF-Tu from Mtb (MtbEF-Tu) is involved in the initial step of trans-translation which is an effective system for rescuing the stalled ribosomes from non-stop translation complexes under stress conditions. Given its crucial role in protein biosynthesis, EF-Tu is identified as an excellent molecular target for drug design. Here, we reported the recombinant expression, purification, biophysical characterization, and structural modeling of the MtbEF-Tu protein. Our results demonstrated that prokaryotic expression plasmids of pET28a-MtbEF-Tu could be expressed efficiently in Escherichia coli. We successfully purified the 6x His-tagged proteins with a yield of 16.8 mg from 1 l of Luria Bertani medium. Dynamic light scattering experiments showed that MtbEF-Tu existed in a monomeric form, and circular dichroism experiments indicated that MtbEF-Tu was well structured. Moreover, isothermal titration calorimetry experiments displayed that the purified MtbEF-Tu protein possessed intermediate binding affinities for guanosine-5-triphosphate (GTP) and GDP. The GTP/GDP-binding sites were predicted by flexible molecular docking approach which reveals that GTP/GDP binds to MtbEF-Tu mainly through hydrogen bonds. Our work lays the essential basis for further structural and functional studies of MtbEF-Tu as well as MtbEF-Tu-related novel drug developments.
Keyword ：
MtbEF-Tu MtbEF-Tu protein biosynthesis protein biosynthesis protein expression and purification protein expression and purification protein-guanine nucleotide interaction protein-guanine nucleotide interaction tuberculosis tuberculosis
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| GB/T 7714 | Yang, Juanjuan , Hong, Jing , Luo, Ling et al. Biophysical characterization and ligand-binding properties of the elongation factor Tu from Mycobacterium tuberculosis [J]. | ACTA BIOCHIMICA ET BIOPHYSICA SINICA , 2019 , 51 (2) : 139-149 . |
| MLA | Yang, Juanjuan et al. "Biophysical characterization and ligand-binding properties of the elongation factor Tu from Mycobacterium tuberculosis" . | ACTA BIOCHIMICA ET BIOPHYSICA SINICA 51 . 2 (2019) : 139-149 . |
| APA | Yang, Juanjuan , Hong, Jing , Luo, Ling , Liu, Ke , Meng, Chun , Ji, Zhi-liang et al. Biophysical characterization and ligand-binding properties of the elongation factor Tu from Mycobacterium tuberculosis . | ACTA BIOCHIMICA ET BIOPHYSICA SINICA , 2019 , 51 (2) , 139-149 . |
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Mycobacteriophages express various peptides/proteins to infect Mycobacterium tuberculosis (M. tb). Particular attention has been paid to mycobacteriophage-derived endolysin proteins. We herein characterized a small mycobacteriophage-derived peptide designated AK15 with potent anti-M. tb activity. AK15 adopted cationic amphiphilic -helical structure, and on the basis of this structure, we designed six isomers with increased hydrophobic moment by rearranging amino acid residues of the helix. We found that one of these isomers, AK15-6, exhibits enhanced anti-mycobacterial efficiency. Both AK15 and AK15-6 directly inhibited M. tb by trehalose 6,6-dimycolate (TDM) binding and membrane disruption. They both exhibited bactericidal activity, cell selectivity, and synergistic effects with rifampicin, and neither induced drug resistance to M. tb. They efficiently attenuated mycobacterial load in the lungs of M. tb-infected mice. We observed that lysine, arginine, tryptophan, and an -helix are key structural requirements for their direct anti-mycobacterial action. Of note, they also exhibited immunomodulatory effects, including inhibition of proinflammatory response in TDM-stimulated or M. tb-infected murine bone marrow-derived macrophages (BMDMs) and M.tb-infected mice and induction of only a modest level of cytokine (tumor necrosis factor (TNF-) and interleukin-6 (IL-6)) production in murine BMDMs and a T-cell cytokine (interferin- (IFN-) and TNF-) response in murine lung and spleen. In summary, characterization of a small mycobacteriophage-derived peptide and its improved isomer revealed that both efficiently restrain M. tb infection via dual mycobactericidal-immunoregulatory activities. Our work provides clues for identifying small mycobacteriophage-derived anti-mycobacterial peptides and improving those that have cationic amphiphilic -helices.
Keyword ：
amino acid amino acid antibiotic antibiotic antimicrobial peptide (AMP) antimicrobial peptide (AMP) anti-mycobacterial peptide anti-mycobacterial peptide drug action drug action drug resistance drug resistance endolysin endolysin -helix -helix hydrophobic moment hydrophobic moment immune regulation immune regulation mycobacteriophage mycobacteriophage Mycobacterium tuberculosis Mycobacterium tuberculosis peptides peptides structure-function structure-function
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| GB/T 7714 | Yang, Yang , Liu, Zhen , He, Xiaoqin et al. A small mycobacteriophage-derived peptide and its improved isomer restrict mycobacterial infection via dual mycobactericidal-immunoregulatory activities [J]. | JOURNAL OF BIOLOGICAL CHEMISTRY , 2019 , 294 (19) : 7615-7631 . |
| MLA | Yang, Yang et al. "A small mycobacteriophage-derived peptide and its improved isomer restrict mycobacterial infection via dual mycobactericidal-immunoregulatory activities" . | JOURNAL OF BIOLOGICAL CHEMISTRY 294 . 19 (2019) : 7615-7631 . |
| APA | Yang, Yang , Liu, Zhen , He, Xiaoqin , Yang, Juanjuan , Wu, Jing , Yang, Hailong et al. A small mycobacteriophage-derived peptide and its improved isomer restrict mycobacterial infection via dual mycobactericidal-immunoregulatory activities . | JOURNAL OF BIOLOGICAL CHEMISTRY , 2019 , 294 (19) , 7615-7631 . |
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A novel antioxidant peptide from protein hydrolysate of Allium tuberosum Rottler was identified as Phe-Pro-Leu-Pro-Ser-Phe (FF-6). It could not only quench multiple radicals efficiently, but also promote cell survival by protecting against oxidative damage. The residue Leu played a vital role in radical-scavenging process and interaction with ABTS(center dot) (+) radicals. When substituted residue Leu with Ala, the radical-scavenging capacity and cytoprotective effect of FF-6 were almost lost. Moreover, the peptide could increase the expression level of proteins PI3K, Akt, phospho-Akt, mTOR, phospho-mTOR, but not affect peroxiredoxin-6. According to these results, the potential mechanism responsible for the protection of oxidative damage and promotion of cell survival was taken place through the PI3K/Akt/mTOR signaling pathway. These findings could be helpful for better elucidating the antioxidant mechanism and shed light on synthetic of alternative antioxidants with more potent activity as nutraceuticals or pharmaceuticals.
Keyword ：
Akt/mTOR signaling pathway Akt/mTOR signaling pathway Allium tuberosum Rottler Allium tuberosum Rottler Antioxidant peptide Antioxidant peptide Free radicals Free radicals Oxidative damage Oxidative damage
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| GB/T 7714 | Chen, Taotao , Chen, Zheng , Wang, Huimin et al. Underlying action mechanism of a novel antioxidant peptide derived from Allium tuberosum Rottler protein hydrolysates and its protective effects on hydrogen peroxide induced cell injury [J]. | JOURNAL OF FUNCTIONAL FOODS , 2018 , 40 : 606-613 . |
| MLA | Chen, Taotao et al. "Underlying action mechanism of a novel antioxidant peptide derived from Allium tuberosum Rottler protein hydrolysates and its protective effects on hydrogen peroxide induced cell injury" . | JOURNAL OF FUNCTIONAL FOODS 40 (2018) : 606-613 . |
| APA | Chen, Taotao , Chen, Zheng , Wang, Huimin , Chen, Xiaodong , Yang, Juanjuan , Han, Aidong et al. Underlying action mechanism of a novel antioxidant peptide derived from Allium tuberosum Rottler protein hydrolysates and its protective effects on hydrogen peroxide induced cell injury . | JOURNAL OF FUNCTIONAL FOODS , 2018 , 40 , 606-613 . |
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Proteins were extracted from perilla (Penile frutescens L. Britton) seed by-products and hydrolyzed with an alkaline protease. Antioxidant peptides were purified from the hydrolysate by size-exclusion chromatography and RP-HPLC. Two peptides with strong antioxidant activity were identified as Tyr-Leu (YL) and Phe-Tyr (FY) with the molecular mass of 294.33 Da and 328.33 Da, respectively. Synthesized YL and FY efficiently quenched free radicals (DPPH, ABTS and hydroxyl radicals) and showed high oxygen radical absorbance capacity. The two peptides also inhibited lipid peroxidation in the rat liver. Furthermore, YL and FY could protect HepG-2 cells against hydrogen peroxide-induced oxidative damage without cytotoxicity. Based on the structure-activity analysis, the Tyr residue was crucial for the antioxidant activity of YL and FY. The results indicate that the protein hydrolysate from perilla seed by-products possessed potent biological activity and can be utilized to develop health-related nutraceutical ingredients.
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| GB/T 7714 | Yang, Juanjuan , Hu, Lei , Cai, Tiantian et al. Purification and identification of two novel antioxidant peptides from perilla (Perilla frutescens L. Britton) seed protein hydrolysates [J]. | PLOS ONE , 2018 , 13 (7) . |
| MLA | Yang, Juanjuan et al. "Purification and identification of two novel antioxidant peptides from perilla (Perilla frutescens L. Britton) seed protein hydrolysates" . | PLOS ONE 13 . 7 (2018) . |
| APA | Yang, Juanjuan , Hu, Lei , Cai, Tiantian , Chen, Qiuluan , Ma, Qian , Yang, Jie et al. Purification and identification of two novel antioxidant peptides from perilla (Perilla frutescens L. Britton) seed protein hydrolysates . | PLOS ONE , 2018 , 13 (7) . |
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The trans-translation system is recognized as an excellent target for developing new drugs to rapidly sterilize Mycobacterium tuberculosis (TB) infection and significantly shorten TB treatment duration. As a vital component of the trans-translation system for rescuing stalled ribosomes, the SmpB protein from Mycobacterium tuberculosis (MtbSmpB, 1-160 a. a.) mediates tmRNA binding to stalled ribosomes through forming a complex with tmRNA. So far, few works have been conducted to prepare, characterize biophysical properties and determine three-dimensional structure for the full-length MtbSmpB protein. In the present work, we successfully expressed and purified the His-tagged full-length MtbSmpB protein in Escherichia coli with a yield of 26.9 mg from 1 L of Luria Bertani medium. We also obtained MtbSmpB with a yield of 18.5 mg from 1 L of M9 minimal medium. The MtbSmpB protein showed a single band in SDS-PAGE with a molecular weight of similar to 20 kDa consistent with the measurement from MALDI-TOF-mass spectrometry. The dynamic light scattering experiment indicated that MtbSmpB existed in a monomeric form. Moreover, both circular dichroism and nuclear magnetic resonance (NMR) experiments exhibited that MtbSmpB was well structured, suggesting that it could be feasible to determine its solution structure by NMR spectroscopy. NMR titration experiments showed that MtbSmpB specifically bound to tmRNA. This work lays the essential basis for further determining the solution structure and dynamics of the full-length MtbSmpB protein.
Keyword ：
MtbSmpB MtbSmpB NMR NMR Protein expression and purification Protein expression and purification Protein-tmRNA interaction Protein-tmRNA interaction Tuberculosis Tuberculosis
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| GB/T 7714 | Yang, Juanjuan , Liu, Yindi , Xu, Shuli et al. Expression, purification and characterization of the full-length SmpB protein from Mycobacterium tuberculosis [J]. | PROTEIN EXPRESSION AND PURIFICATION , 2018 , 151 : 9-17 . |
| MLA | Yang, Juanjuan et al. "Expression, purification and characterization of the full-length SmpB protein from Mycobacterium tuberculosis" . | PROTEIN EXPRESSION AND PURIFICATION 151 (2018) : 9-17 . |
| APA | Yang, Juanjuan , Liu, Yindi , Xu, Shuli , Lin, Haiying , Meng, Chun , Lin, Donghai . Expression, purification and characterization of the full-length SmpB protein from Mycobacterium tuberculosis . | PROTEIN EXPRESSION AND PURIFICATION , 2018 , 151 , 9-17 . |
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利用原核表达系统获得包涵体表达形式的重组蛋白hPD-L220~123(IgV结构域)和hPD-L220~208(IgV结构域和IgC结构域);将重组蛋白利用Ni-NTA柱亲和层析纯化与复性后,作为免疫原免疫Balb/c雌性小鼠制备鼠抗人的多抗血清,经ELISA法检测其效价均达到1:106;Western-blot实验结果表明,制备的多抗血清均能特异性识别hPD-L2蛋白.以制备的多抗血清进行IHC实验评估与鉴定,结果显示:以hPD-L220~123重组蛋白为免疫原制备的多抗血清阳性较弱且定位模糊,以hPD-L220~208重组蛋白为免疫原制备的多抗血清具有很强的膜定位且背景清晰.
Keyword ：
主要抗原表位区 主要抗原表位区 人源PD-L2蛋白 人源PD-L2蛋白 原核表达 原核表达 抗血清 抗血清
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| GB/T 7714 | 杨娟娟 , 刘照 , 夏菁潞 et al. 人源程序性死亡配体PD-L2蛋白的原核表达与抗血清制备 [J]. | 福州大学学报（自然科学版） , 2018 , 46 (3) : 438-444 . |
| MLA | 杨娟娟 et al. "人源程序性死亡配体PD-L2蛋白的原核表达与抗血清制备" . | 福州大学学报（自然科学版） 46 . 3 (2018) : 438-444 . |
| APA | 杨娟娟 , 刘照 , 夏菁潞 , 罗岭 , 俞博彤 , 孟春 . 人源程序性死亡配体PD-L2蛋白的原核表达与抗血清制备 . | 福州大学学报（自然科学版） , 2018 , 46 (3) , 438-444 . |
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As of February 2017, approximately 7639 amphibian species have been described in the AmphibiaWeb database. However, only 20 cathelicidin-like antimicrobial peptides have been identified to date from 10 amphibian species. Half of these peptides were identified from genome sequences and have not yet been functionally characterized. In this study, a novel cathelicidin-like peptide designated cathelicidin-PP was purified from the skin of tree frog Polypedates puerensis. Cathelicidin-PP is a 32 residue peptide of sequence ASENGKCNLLCLVKKKLRAVGNVIKTVVGKIA. Circular dichroism spectroscopy indicated that cathelicidin-PP mainly adopts a beta-sheet structure in membrane-mimetic solutions. Cathelicidin-PP exhibits potent antimicrobial activity against bacteria and fungi, especially Gram-negative bacteria. Meanwhile, it shows low cytotoxicity toward mammalian cells. Scanning electron microscopy analysis indicated that cathelicidin-PP kills bacteria through the disruption of the bacterial cell membrane integrity. Furthermore, cathelicidin-PP exerts significant anti-inflammatory functions by inhibiting the lipopolysaccharide (LPS)-mediated generation of nitric oxide and pro-inflammatory cytokines, tumor necrosis factor-alpha, interleukin-1 beta, and interleukin-6. The MAPKs (ERK, JNK, and p38) and NF-kappa B signaling pathways are involved in the anti-inflammatory effect. Cathelicidin-PP caused partial neutralization of LPS in a dose-dependent manner. Quantitative PCR indicated that infection of tree frogs with bacteria causes increased expression of cathelicidin-PP in immune-related tissues. Taken together, cathelicidin-PP is the first identified cathelicidin-like peptide from tree frogs. Our findings demonstrate that in addition to direct bactericidal capacity, cathelicidin-PP also possesses immunomodulatory properties, including partial neutralization of LPS, and inhibiting the production of inflammatory cytokines.
Keyword ：
Anti-inflammation Anti-inflammation Cathelicidin Cathelicidin LPS neutralization LPS neutralization Polypedates puerensis Polypedates puerensis Tree frog Tree frog
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| GB/T 7714 | Mu, Lixian , Zhou, Lei , Yang, Juanjuan et al. The first identified cathelicidin from tree frogs possesses anti-inflammatory and partial LPS neutralization activities [J]. | AMINO ACIDS , 2017 , 49 (9) : 1571-1585 . |
| MLA | Mu, Lixian et al. "The first identified cathelicidin from tree frogs possesses anti-inflammatory and partial LPS neutralization activities" . | AMINO ACIDS 49 . 9 (2017) : 1571-1585 . |
| APA | Mu, Lixian , Zhou, Lei , Yang, Juanjuan , Zhuang, Li , Tang, Jing , Liu, Tong et al. The first identified cathelicidin from tree frogs possesses anti-inflammatory and partial LPS neutralization activities . | AMINO ACIDS , 2017 , 49 (9) , 1571-1585 . |
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