Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Drug Conjugates Using Different Dynamic Covalent Bonds and their Application in Cancer Therapy. You have to login with your ACS ID befor you can login with your Mendeley account. Jingchao Li, Dong Cui, Jiaguo Huang, Shasha He, Zebin Yang, Yan Zhang, Yu Luo, Kanyi Pu. Yaqi Lyu, Qingqing Xiao, Yi Li, Yubing Wu, Wei He, Lifang Yin. Yao Chen, Xinzhu Shan, Cong Luo, Zhonggui He. Cys residues in BEST1 wild type and SAPs, namely, C69W, R218C, F17C, W24C, Y29C R92C, R105C, C221W, Y227C, Y236C, R355C, and W93C, were predicted to be deleterious by PolyPhen-2, PANTHER, SNPs&GO, and I-Mutatnt3. Conditions that perturb correct protein folding lead to accumulation of misfolded proteins in the ER lumen, which induce ER stress and oxidative stress. Hui-Yun Zhang, Cong-yong Sun, Michael Adu-Frimpong, Jiang-nan Yu, Xi-ming Xu. Self-assembly of pentapeptides into morphology-adaptable nanomedicines for enhanced combinatorial chemo-photodynamic therapy. Polymer-Assisted Magnetic Nanoparticle Assemblies for Biomedical Applications. The PDI was initially discovered by Christian Anfinsen as an ER enzyme that facilitates the formation of correct disulfide bonds in proteins. Reduction of a typical disulfide bond by DTT via two sequential thiol-disulfide exchange reactions. Similar mechanisms operate in eukaryotic cells. Oxidation-strengthened disulfide-bridged prodrug nanoplatforms with cascade facilitated drug release for synergetic photochemotherapy. Process analytical technology (PAT) as a versatile tool for real-time monitoring and kinetic evaluation of photocatalytic reactions. Shumeng Li, Xinzhu Shan, Yuequan Wang, Qin Chen, Jin Sun, Zhonggui He, Bingjun Sun, Cong Luo. The modulation of the redox potential of the disulfide bonds may be due to sequence differences within the conserved fold, in particular the ionization properties of active site residues.89 These sequence effects also have been observed in the redox stability of DRPs. antitumor efficacy of a polyunsaturated fatty acid-conjugated pH-responsive self-assembled ion-pairing liposome-encapsulated prodrug. Hyperbranched polyglycerol β-cyclodextrin as magnetic platform for optimization of doxorubicin cytotoxic effects on Saos-2 bone cancerous cell line. Carrier-free nanodrug: A novel strategy of cancer diagnosis and synergistic therapy. Martin Rößler, Philipp U. Huth, Marcel A. Liauw. Similarly, in PRPH2, Cys in the following positions 72, 82, 150, 165, 213, 214, 222, and 250 was predicted to form the disulfide bond between 72 and 82, 213 and 250, 214 and 222, and 150 and 165. Giovanni Chiappetta, ... Michel B. Toledano, in Methods in Enzymology, 2010. Our findings give new insight into the stimuli responsiveness of disulfide bonds and provide a good foundation for the development of novel redox dual-responsive DDS for cancer therapy. Jun Zeng, Chen Li, Xing Duan, Fuyue Liu, Anqin Li, Chunhan Luo, Li Jia, Yifang Gan, Lu Yan, Yaxin Zheng. not otherwise permitted to reproduce, republish, redistribute, or sell any Supporting Information Weder, H-D Belitz, in Encyclopedia of Food Sciences and Nutrition (Second Edition), 2003. Glutathione and Reactive Oxygen Species Dual-Responsive Block Copolymer Prodrugs for Boosting Tumor Site-Specific Drug Release and Enhanced Antitumor Efficacy. For both proteins, oxidation and zinc release are associated with an … Mingming Li, Yashan Ning, Jialiang Chen, Xingchen Duan, Na Song, Dan Ding, Xuncheng Su. Harold A. Scheraga, ... Ervin Welker, in Methods in Enzymology, 2001. Similarly, in PRPH2, wild-type Cys residues, namely, C165Y, C165R, C213R, C213F, C213Y, C214Y, C214S, and C250F, and SAPS W25C and Y141C, were predicted to be deleterious by PolyPhen-2, SNAP, I-Mutatnt3, and Align-GVGD. The prodrugs can self-assemble into uniform-size nanoparticles with impressively high drug loading (>55%). A remarkable number of PDI isoforms exists in the ER lumen (Table 2), implicating either a redundancy or specification in their functions. You’ve supercharged your research process with ACS and Mendeley! Yujia Jiang, Junhui Zhou, Xuefei Zhao, Jianhua Zhang, Ruiwei Guo, Anjie Dong, Lian‐dong Deng. “Locked” cancer cells are more sensitive to chemotherapy. Huabing Chen, Zhanjun Gu, Hongwei An, Chunying Chen, Jie Chen, Ran Cui, Siqin Chen, Weihai Chen, Xuesi Chen, Xiaoyuan Chen, Zhuo Chen, Baoquan Ding, Qian Dong, Qin Fan, Ting Fu, Dayong Hou, Qiao Jiang, Hengte Ke, Xiqun Jiang, Gang Liu, Suping Li, Tianyu Li, Zhuang Liu, Guangjun Nie, Muhammad Ovais, Daiwen Pang, Nasha Qiu, Youqing Shen, Huayu Tian, Chao Wang, Hao Wang, Ziqi Wang, Huaping Xu, Jiang-Fei Xu, Xiangliang Yang, Shuang Zhu, Xianchuang Zheng, Xianzheng Zhang, Yanbing Zhao, Weihong Tan, Xi Zhang, Yuliang Zhao. Strategies to Obtain Encapsulation and Controlled Release of Small Hydrophilic Molecules. Notice that in the oxidized (disulfide) state, each sulfur atom has lost a bond to hydrogen and gained a bond to sulfur. Redox and pH Dual-Responsive Injectable Hyaluronan Hydrogels with Shape-Recovery and Self-Healing Properties for Protein and Cell Delivery. Dimeric prodrug-based nanomedicines for cancer therapy. The sklearn. Yinxian Yang, Bingjun Sun, Shiyi Zuo, Ximu Li, Shuang Zhou, Lingxiao Li, Cong Luo, Hongzhuo Liu, Maosheng Cheng, Yongjun Wang, Shujun Wang, Zhonggui He, Jin Sun.
Dual Receptor-Targeted and Redox-Sensitive Polymeric Micelles Self-Assembled from a Folic Acid-Hyaluronic Acid-SS-Vitamin E Succinate Polymer for Precise Cancer Therapy. Disulfide bonds have been widely used to develop reduction-responsive drug-delivery systems (DDS) for cancer therapy. A surfactant-like chemotherapeutic agent as a nanocarrier for delivering photosensitizers against cancer: A facile drug-delivering-drug strategy. These reagents can produce results that disagree with the majority of other methods, even for relatively simple measurements such as the Keq between DTT and glutathione.156,157 These blocking reagents have also produced anomalous results for the oxidative folding of bovine pancreatic trypsin inhibitor (BPTI), when compared to experiments carried out under identical conditions using acid quenching.117,158 At higher concentrations, these reagents may also chemically modify other residues of the protein.159. Liqian Zhou, Haiyang Xie, Xiaona Chen, Jianqin Wan, Shengjun Xu, Yaxuan Han, Dong Chen, Yiting Qiao, Lin Zhou, Shusen Zheng, Hangxiang Wang. Secretory Proteins Form Their Disulfide Bonds in the ER Lumen. ScienceDirect ® is a registered trademark of Elsevier B.V. ScienceDirect ® is a registered trademark of Elsevier B.V. URL: https://www.sciencedirect.com/science/article/pii/B9780123850959002360, URL: https://www.sciencedirect.com/science/article/pii/B9780123944474100653, URL: https://www.sciencedirect.com/science/article/pii/B9780123786302000104, URL: https://www.sciencedirect.com/science/article/pii/B9780124095472124175, URL: https://www.sciencedirect.com/science/article/pii/B9780128001684000068, URL: https://www.sciencedirect.com/science/article/pii/B012227055X009822, URL: https://www.sciencedirect.com/science/article/pii/B9780323508780000021, URL: https://www.sciencedirect.com/science/article/pii/S0076687901411530, URL: https://www.sciencedirect.com/science/article/pii/B9780124058835000144, URL: https://www.sciencedirect.com/science/article/pii/S007668791073010X, Encyclopedia of Biological Chemistry (Second Edition), 2013, Handbook of Biologically Active Peptides (Second Edition), Encyclopedia of Biological Chemistry (Second Edition), The ability to form and break a disulfide-bond depends on the, Application of Evolutionary Based in Silico Methods to Predict the Impact of Single Amino Acid Substitutions in Vitelliform Macular Dystrophy, C. 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These include the folding of proteins in which disulfide bonds occur through oxidation of sequential cysteines, ones in which long-range, non-sequential cysteines are used, and even to pathways that rely on the initial production of non-native disulfide bonds that are subsequently reduced during the folding process to allow the formation of native bonds in order to achieve the mature, functional structure … Just as HOOH (hydrogen peroxide) is more oxidized than HOH (O in H2O2 has oxidation number of 1- while the O in H2O has an oxidation number of 2-), RSSR is the oxidized form (S oxidation number 1-) and RSH is the reduced form (S oxidation number 2-) of thiols. Knowledge on cysteine oxidation state and disulfide bond connectivity is of great importance to protein chemistry and 3-D structures. Guolian Ren, Pei Chen, Jiaqi Tang, Wenju Guo, Rongrong Wang, Ning Li, Yujie Li, Guoshun Zhang, Ruili Wang, Shuqiu Zhang. PEGylation of lipophilic SN38 prodrug with DSPE-mPEG These reductions can also occur over a broad range of pHs and buffers. Highlights: DiANNA is a artificial neural network and web server, which determines the cysteine oxidation state and disulfide connectivity of a protein, given only its amino acid sequence. Jinhong Du, Bonnie Choi, Yuxuan Liu, Anchao Feng, San H. Thang. Disulfide Bonds. Two cysteine side chains can covalently interact in a protein to produce a disulfide. Zhifei Cheng, Yuanyuan Cheng, Qian Chen, Mingming Li, Jie Wang, Hui Liu, Mengwen Li, Yashan Ning, Zhilin Yu, Yinsong Wang, Hao Wang. Cancer-Selective Bioreductive Chemotherapy Mediated by Dual Hypoxia-Responsive Nanomedicine upon Photodynamic Therapy-Induced Hypoxia Aggravation. Knowledge on cysteine oxidation state and disulfide bond connectivity is of great importance to protein chemistry and 3-D structures. Intramolecular disulfide bonds stabilize the tertiary structures of proteins while thoisethat occur intermolecularly are involved in stabilizing quartenary structure. Disulfide bonds exert a strong influence on the properties of proteins. Hongyan Su, Yan Wang, Shuo Liu, Yue Wang, Qian Liu, Guangxuan Liu, Qin Chen. Advances and perspectives in carrier-free nanodrugs for cancer chemo-monotherapy and combination therapy. Cysteine sulfenic acid has a number of biological functions. The PDIs function to shuffle disulfide bonds, stabilize proper intermediates, and resolve aberrant disulfide bonds via a thiol-disulfide exchange reaction, with the transient formation of mixed disulfide bond between PDI and its substrate protein (Figure 2). Xueli Zhao, Shuang-Quan Zang, Xiaoyuan Chen. But in the absence of a nearby second cysteine, thiol oxidation typically leads to the formation of sulfenic acid (S–OH), sulfinic acid (SO 2H), S-nitrosothiols (S– NO), or S-glutathione (S–SG). Smart Magnetic and Fluorogenic Photosensitizer Nanoassemblies Enable Redox‐Driven Disassembly for Photodynamic Therapy. Here, the oxidation state of sulfur is changed from − 2 - 2 − 2 to − In biochemistry, the terminology R-S-S-R connectivity is commonly used to describe the overall linkages. Smythe, in Comprehensive Medicinal Chemistry III, 2017. Zhaomeng Wang, Mengchi Sun, Tian Liu, Xiao Tan, Haotian Zhang, Xiangyu Zhang, Zhonggui He, Jin Sun. Precise nanomedicine for intelligent therapy of cancer. In bacteria, disulfide bonds in bioactive peptides and polypeptides of the secretory pathway are formed in the periplasm; in eukaryotes, such (poly)peptides tend to acquire their disulfide bonds in the endoplasmic reticulum (ER) although disulfide bond formation can occasionally occur at other sites (including extracellularly). Disulfide bonds stabilize protein structure by organizing and destabilizing the denatured protein relative to the native structure. Organic Semiconducting Pro‐nanostimulants for Near‐Infrared Photoactivatable Cancer Immunotherapy. Find more information on the Altmetric Attention Score and how the score is calculated. Probing the Superiority of Diselenium Bond on Docetaxel Dimeric Prodrug Nanoassemblies: Small Roles Taking Big Responsibilities. AEMTS blocking facilitates the subsequent fractionation (by adding a positively charged cysteamine group for every blocked thiol) and does not require the maintenance of low pH during the subsequent analysis. In vivo Shou-Yuan Sung, Yu-Lin Su, Wei Cheng, Pei-Fan Hu, Chi-Shiun Chiang, Wen-Ting Chen. Information. Files available from the ACS website may be downloaded for personal use only. thioredoxins and glutaredoxins). The formation of disulfide bonds between the correct pairs of cysteine residues is essential for the folding and stability of many proteins (Narayan et al. The formation of an intramolecular disulfide bond between cysteines C38 and C83 enhances the nitrite reductase activity by 50-fold over that of the monomer with free sulfhydryl or 140-fold over that of the dimer with intermolecular disulfide bonds. As the two atoms of hydrogen are lost by thiol to make a disulfide bond, through the oxidation of carbonic acid or nitric acid it further attains oxygens to form sulfones that succeed towards the formation of sulfonic acid. oxidative stress response). Hao Zhao, Jiabao Xu, Wenjing Huang, Guiting Zhan, Yanbing Zhao, Huabing Chen. Yingli Wang, Jiamei Wang, Liyuan Yang, Wei Wei, Bingjun Sun, Kexin Na, Yuxi Song, Haotian Zhang, Zhonggui He, Jin Sun, Yongjun Wang. Disulfide-bond regeneration can be arrested at different times, either by acid quenching or by a rapid thiol-blocking agent such as aminoethylmethane thiosulfonate (AEMTS)154 and similar thiosulfonates. Abstract Disulfide bonds have been widely used to develop reduction-responsive drug-delivery systems (DDS) for cancer therapy. system. Tables showing the characterization of prodrug nanoassemblies, cytotoxicity, and pharmacokinetic parameters. Chutong Tian, Jingjing Guo, Gang Wang, Bingjun Sun, Kexin Na, Xuanbo Zhang, Zhuangyan Xu, Maosheng Cheng, Zhonggui He, Jin Sun. Disulfide bond formation involves a reaction between the sulfhydryl (SH) side chains of two cysteine residues: an S− anion from one sulfhydryl group acts as a nucleophile, attacking the side chain of a second cysteine to create a disulfide bond, and in the process releases electrons (reducing equivalents) for transfer. Electronic Supporting Information files are available without a subscription to ACS Web Editions. Cysteine sulfenic acid (–SOH) is the initial product of oxidation of cysteine by cellular reactive oxygen species such as hydrogen peroxide. The reaction was carried for 15 min at 4 °C under stirring, and the excess dye removed by TCA precipitation. In BEST1, five Cys residues in their corresponding positions 23, 42, 69, 221, and 251 were involved in disulfide bond formation between 221 and 251 and 23 and 42. 4). The redox state of the cytoplasm of eukaryotic and prokaryotic cells is reducing due to the presence of numerous disulfide bond reductases (e.g. The PDI was initially discovered by Christian Anfinsen as an ER enzyme that facilitates the … More interestingly, the position of disulfide bonds in the carbon chain linkage has profound impacts on the redox dual responsiveness, thereby affecting the drug release, cytotoxicity, pharmacokinetics, biodistribution, and in vivo antitumor efficacy of prodrug nanoassemblies. This feature is incredibly rare among proteins, as nearly all proteins are stabilized by the formation of disulfide bonds. Efficient Intestinal Digestion and On Site Tumor‐Bioactivation are the Two Important Determinants for Chylomicron‐Mediated Lymph‐Targeting Triglyceride‐Mimetic Docetaxel Oral Prodrugs. Disulfide bonds can also serve catalytic (e.g. Additional details on the experimental methods. Because disulfide bond formation is reversible, disulfide bonds can also regulate biological activity through their ability to stabilize specific protein structures. Near-infrared photoresponsive drug delivery nanosystems for cancer photo-chemotherapy. Wei Yin, Wendong Ke, Nannan Lu, Yuheng Wang, Abd Al-Wali Mohammed M. Japir, Fathelrahman Mohammed, Yi Wang, Yueyin Pan. Sena Karaosmanoglu, Mengjiao Zhou, Bingyang Shi, Xiujuan Zhang, Gareth R. Williams, Xianfeng Chen. Thus, the disulfide formed during translation has to be reduced and re-oxidized and the early formation of a non-native disulfide will catalyze disulfide bond isomerization once the polypeptide chain is released (Fig. Yang Li, Yuwen Chen, Yulan Huang, Wenbi Wu, Yu Liu, Jing Zhang, Meijuan Huang, Maling Gou. This occurs as a protein-based relay of oxidation/reduction reactions, involving, for example, a PDI and the oxidoreductases Ero1 (associated with the ER membrane). Liying Wang, Xinru You, Qi Lou, Siyu He, Junfu Zhang, Chunlei Dai, Meng Zhao, Minyi Zhao, Hai Hu, Jun Wu. The most common way of creating this bond is by the oxidation of sulfhydryl groups. Liyi Fu, Fengming Zou, Qingwang Liu, Beilei Wang, Junqing Wang, Huamin Liang, Xiaofei Liang, Jing Liu, Jinjun Shi, Qingsong Liu. Jianhui Yuan, Qi Zhou, Xuelin Dong, Binbin Zhang, Qin Wang, Yajiang Yang, Yonggui Liao, Hong Wang. The ER is a vastly more common site than the cytosol (which is very rarely the site of disulfide bond formation) because the ER intralumenal environment is more oxidizing than that of the cytosol.1 The redox environment is at least partly reflected by the ratio of oxidized glutathione (GSSG) to reduced glutathione (GSH), which in the case of the ER (and periplasm), is shifted in favor of GSSG.1, Z. Chang, in Encyclopedia of Cell Biology, 2016. Nanotherapeutics for Antimetastatic Treatment. Proteins Using High-Resolution NMR: A Study of Disulfide Bond Compensation Andria L. Skinner1 and Jennifer S. Laurence1,* 1Department of Pharmaceutical Chemistry, The University of Kansas, Lawrence, KS 66047 Abstract It is well established that the oxidation state of cysteine residues in proteins are critical to overall physical stability. Glutathione-sensitive PEGylated curcumin prodrug nanomicelles: Preparation, characterization, cellular uptake and bioavailability evaluation. DsbA's highly oxidizing nature is a result of hydrogen bond, electrostatic and helix-dipole interactions that favour the thiolate over the disulfide at the active site. If the blocking of thiols is too slow, the blocking agent may act as an oxidizing agent; the unblocked thiols may attack the disulfide bond of the blocked thiols and form an intraprotein disulfide bond. Bin Yang, Lin Wei, Yuequan Wang, Na Li, Bin Ji, Kaiyuan Wang, Xuanbo Zhang, Shenwu Zhang, Shuang Zhou, Xiaohui Yao, Hang Song, Yusheng Wu, Haotian Zhang, Qiming Kan, Tao Jin, Jin Sun. These metrics are regularly updated to reflect usage leading up to the last few days. 6 Kinetic control by limiting glutaredoxin amounts enables thiol oxidation in the reducing mitochondrial intermembrane space (2 RSH → RS-SR + 2 H+ + 2 e-) This process of oxidation can produce stable protein dimers, polymers, or complexes, in which the sulfide bonds can help in protein folding. http://pubs.acs.org/page/copyright/permissions.html. Compounds containing a disulfide bridge are able to undergo disulfide exchange reactions (also called “interchange”) with thiols. A light-induced nitric oxide controllable release nano-platform based on diketopyrrolopyrrole derivatives for pH-responsive photodynamic/photothermal synergistic cancer therapy. & Account Managers, For Under these conditions, the cytosolic copper chaperone Atox1, which delivers Cu(I) to the secretory pathway, gets oxidized, i.e., a disulfide bond is formed between the cysteine residues of the Cu(I)-binding CxxC motif. of metformin. Zhiqiang Zhao, Fujun Yang, Xuanbo Zhang, Jin Sun, Zhonggui He, Cong Luo. The redox dual-responsive mechanism is elucidated, and how the position of disulfide bonds in the carbon chain affects the redox dual responsiveness and antitumor efficiency of prodrug nanoassemblies is also clarified. The disulfide bonds, often present in secretory proteins and virtually absent in cytosolic proteins, are formed in the ER lumen where a relatively high oxidative redox potential is commonly maintained and PDIs are abundant (Braakman and Bulleid, 2011). in vitro Self-facilitated ROS-responsive nanoassembly of heterotypic dimer for synergistic chemo-photodynamic therapy. 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