留言板

尊敬的读者、作者、审稿人, 关于本刊的投稿、审稿、编辑和出版的任何问题, 您可以本页添加留言。我们将尽快给您答复。谢谢您的支持!

姓名
邮箱
手机号码
标题
留言内容
验证码
x 关闭 永久关闭

应中央军委要求，2022年9月起，《药学实践杂志》将更名为《药学实践与服务》，双月刊，正文96页；2023年1月起，拟出版月刊，正文64页，数据库收录情况与原《药学实践杂志》相同。欢迎作者踊跃投稿！

蛋白质结晶的新进展与药物设计

陈维敬,  仲维清

downloadPDF
文章导航 > 药学实践与服务  > 2012 >  30(2): 81-85,136
陈维敬, 仲维清. 蛋白质结晶的新进展与药物设计[J]. 药学实践与服务, 2012, 30(2): 81-85,136. doi: 10.3969/j.issn.1006-0111.2012.02.001
引用本文: 陈维敬, 仲维清. 蛋白质结晶的新进展与药物设计[J]. 药学实践与服务, 2012, 30(2): 81-85,136. doi: 10.3969/j.issn.1006-0111.2012.02.001
shu
CHEN Wei-jing, ZHONG Wei-qing. New progress of protein crystallization and drug design[J]. Journal of Pharmaceutical Practice and Service, 2012, 30(2): 81-85,136. doi: 10.3969/j.issn.1006-0111.2012.02.001
Citation: CHEN Wei-jing, ZHONG Wei-qing. New progress of protein crystallization and drug design[J]. Journal of Pharmaceutical Practice and Service, 2012, 30(2): 81-85,136. doi: 10.3969/j.issn.1006-0111.2012.02.001
shu

蛋白质结晶的新进展与药物设计

doi: 10.3969/j.issn.1006-0111.2012.02.001

  • 第二军医大学药学院无机化学教研室, 上海 200433

基金项目: 国家自然科学基金资助项目(20371050).

New progress of protein crystallization and drug design

  • School of Pharmacy, Second Military Medical University, Shanghai 200433, China

  • 摘要: 蛋白质是生命的基础,其功能与它的三维结构密切相关,关于蛋白质的结构信息,对科学家根据结构同源性确定药物靶标以及发现新的药物靶标等方面均有至关重要的作用。因此,蛋白质晶体的获得及其与药物设计的关系日益受到重视,已成为生命科学中的一个重要领域,本文主要综述了蛋白质结晶技术的最新研究进展以及在药物设计中的应用。
    Abstract: Protein was the foundation of all life, and its function was closely related to its three-dimensional structure. The structure information of proteins was crucial for the determination of drug targets and helped scientists to discover new drug targets according to the structure homology between the protein targets and drugs. Therefore, the availability of protein crystal, which was the basis for its structure information and the drug design, had become an important field in life science. The latest research progresses of protein crystallization technology and its application in the drug design were summarized in this review.
  • [1] Pastwa E,Somiari SB, Czyz M, et al. Proteomics in human cancer research[J]. Proteom Clin Appl, 2007, 1(1): 4.
    [2] Curcio E, Simone S, Gianluca DP. et al. Memabrane crystallization of lysozyme under forced solution flow[J]. J Membrane Sci, 2005, 257(1-2): 134.
    [3] Zhang XM, Wei KG, Ma RY, et al. Precipitants and additives for membrane crystallization of lysozyme[J]. Biotechnol J, 2006, 1(11): 1302.
    [4] Zhang XM, Zhang P, Ma RY, et al. The study of continuous membrane crystallization on lysozyme[J]. Desalination, 2008, 219(1-3):101.
    [5] 庞鸿宇, 刘丽英, 马润宇, 等. 木瓜蛋白酶动态膜结晶的实验研究[J]. 膜科学与技术, 2010, 30(1): 30.
    [6] Xiao T, Takag J, Wang JH, et al. Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics[J]. Nature, 2004, 432(7013): 59.
    [7] 李俊君, 陈 强, 李 刚, 等. 微流控技术应用于蛋白质结晶的研究[J]. 化学进展, 2009, 21(5): 1034.
    [8] 马建华, 仓怀兴. 空间蛋白质晶体生长新技术[J]. 生物物理学报, 2009, 25(s1):: 314.
    [9] Koide S. Engineering of recombinant crystallization chaperones[J]. Curr Opin Struct Biol, 2009, 19(4): 449.
    [10] Day PW, Rasmussen SG, Parnot C, et al. A monoclonal antibody for G protein-coupled receptor crystallography[J]. Nat Methods, 2007, 4(11): 927.
    [11] Rasmussen SG, Choi HJ, Rosenbaum DM, et al. Crystal structure of the human beta2 adrenergic G-protein-coupled receptor[J]. Nature, 2007, 450(7168): 383.
    [12] Korotkov KV, Pardon E, Steyaert J, et al. Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody[J]. Structure, 2009, 17(2): 255.
    [13] Lam AY, Pardon E, Korotkov KV, et al. Nanobody-aided structure determination of the EpsI:EpsJ pseudopilin heterodimer from Vibrio vulnificus[J]. J Struct Biol, 2009, 166(1): 8.
    [14] Uysal S, Vasquez V, Tereshko V, et al. The crystal structure of fulllength KcsA in its closed conformation[J]. Proc Natl Acad Sci USA, 2009, 106(16): 6644.
    [15] Sennhauser G, Grutter MG. Chaperone-assisted crystallography with DARPins[J]. Structure, 2008, 16(10): 1443.
    [16] Mio K, Maruyama Y, Ogura T, et al. Single particle reconstruction of membrane proteins: A tool for understanding the 3D structure of disease-related macromolecules[J]. Progress Biophys Mol Biol, 2010, 103(1): 122.
    [17] Fujiyoshi Y. Structural physiology based on electron crystallography[J]. Protein Sci, 2011, 20(5): 806.
    [18] Bill RM, Henderson PJF, Iwata S, et al. Overcoming barriers to membrane protein structure determination[J]. Nat Biotech, 2011, 29(4): 335.
    [19] Leulliot N, Tresaugues L, Bremang M, et al. High-throughput crystal-optimization strategies in the South Paris Yeast Structural Genomics project: one size fits all[J]. Acta Crystallogr D, 2005, 61(6): 664.
    [20] Kambach C. Pipelines, robots, crystals and biology: What use high throughput solving structures of challenging targets[J]. Curr Protein Pept Sci, 2007, 8(2): 205.
    [21] Luft JR, Snell EH, DeTitta GT. Lessons from high-throughput protein crystallization screening: 10 years of practical experience[J]. Expert Opin Drug Discov, 2011, 6(5): 465.
    [22] Leach AR, Gillet VJ, Lewis RA, et al. Three-dimensional pharmacophore methods in drug discovery[J]. J Med Chem, 2010, 53(2): 539.
    [23] Scapin G. Structural biology and drug discovery[J]. Curr Pharm Des, 2006, 12(17): 2087.
    [24] Arinaminpathy Y, Khurana E, Engelman DM, et al. Computational analysis of membrane proteins: the largest class of drug targets[J]. Drug Discov Today, 2009, 14(23-24): 1130.
    [25] Grey J, Thompson D. Challenges and opportunities for new protein crystallization strategies in structure-based drug design[J]. Expert Opin Drug Discov, 2010, 5(11): 1039.
    [26] 甘 淋, 刘银坤. Stathm in蛋白:一个潜在的肿瘤标志物[J]. 肿瘤, 2010, 30(1): 73.
    [27] Tabernero L, Aricescu AR, Jones EY, et al. Protein tyrosine phosphatases: structure-function relationships[J]. FEBS J, 2008, 275(5): 867.
    [28] Chrysina ED, Chajistamatiou A, Chegkazi M. From structure-based to knowledge-based drug design through x-ray protein crystallography: sketching glycogen phosphorylase binding sites[J]. Curr Med Chem, 2011, 18(17): 2620.
    [29] Rosano C, Stec-Martyna E, Lappano R. Structure-based approach for the discovery of novel selective estrogen receptor modulators[J]. Curr Med Chem, 2011, 18(8): 1188.
    [30] Morrow JK, Lei DC, Lu C, et al. Recent development of anticancer therapeutics targeting Akt[J]. Rec Pat Anti-Cancer Drug Dis, 2011, 6(1): 146.
    [31] Munikumar RD, Dhanaji AT, Seon HS, et al. Structure based design of heat shock protein 90 inhibitors acting as anticancer agents[J]. Bioorg Med Chem, 2011,19(5): 1714.
    [32] Yuan YX, Pe JF, Lai LH. LigBuilder 2: A practical de novo drug design approach[J]. J Chem Inf Model, 2011, 51(5): 1083.
    [33] Bon RS, Zhong G, Anouk Stigter E, et al. Structure-guided development of selective rabggtase inhibitors[J]. Angew Chem Int Ed, 2011, 50(21): 4957.
    [34] Mai D, Jones J, Rodgers JW, et al. A Screen to Identify Small Molecule Inhibitors of Protein-Protein Interactions in Mycobacteria[J]. ASSAY Drug Dev Tech. 2011, 9(3):299.
    [35] Madabushi S, Yao H, Marsh M, et al. Structural clusters of evolutionary trace residues are statistically significant and common in proteins[J], J Mol Biol, 2002, 316(1): 139.
    [36] Song YL, Qi YP, Zhang WN, et al. Evolutionary trace analysis of eukaryotic DNA topoisomerase I superfamily: Identification of novel antitumor drug binding site[J]. Sci China Ser C, 2005, 28(4): 375.
    [37] Sheng CQ, Dong GQ, Che XY, et al. Evolutionary trace analysis of CYP51 family: implication for site-directed mutagenesis and novel antifungal drug design[J]. J Mol Mod, 2010, 16(2): 279.
  • [1] 陈枫, 杨慈荣, 张圳, 陈飞, 刘霞.  基于药物重定位建立以α1酸性糖蛋白为靶点的高通量筛选平台及潜在减肥药物的发现 . 药学实践与服务, 2024, 42(3): 114-120. doi: 10.12206/j.issn.2097-2024.202309057
    [2] 李安鹏, 陈帅, 宋佳, 梁伦海, 邹季花, 邹燕, 赵庆杰.  红火蚁毒素物质基础研究进展 . 药学实践与服务, 2023, 41(9): 524-527. doi: 10.12206/j.issn.2097-2024.202204119
    [3] 陈帅, 李安鹏, 李星星, 赵庆杰, 邹燕.  Hippo 信号通路在器官再生过程中的作用机制研究进展 . 药学实践与服务, 2023, 41(8): 472-477. doi: 10.12206/j.issn.2097-2024.202301008
    [4] 罗川, 李锦, 张万年, 缪震元.  小分子p53-MDM2抑制剂先导化合物苄普地尔的研究 . 药学实践与服务, 2021, 39(2): 126-129. doi: 10.12206/j.issn.1006-0111.202009031
    [5] 罗川, 马建江, 缪震元, 吴岳林.  沙蟾毒精酯类衍生物的合成和抗肿瘤活性研究 . 药学实践与服务, 2021, 39(1): 35-37, 57. doi: 10.12206/j.issn.1006-0111.202007022
    [6] 姚争光, 王志斌, 夏春年, 庄春林.  冠状病毒小分子抑制剂研究进展 . 药学实践与服务, 2020, 38(5): 385-397. doi: 10.12206/j.issn.1006-0111.202005020
    [7] 李安, 周小青, 孙阔, 杨谨如, 朱勇飞, 陆一鸣.  药物分子与靶蛋白相互作用的研究进展 . 药学实践与服务, 2019, 37(1): 1-4,31. doi: 10.3969/j.issn.1006-0111.2019.01.001
    [8] 姜艳娟, 崔俐俊, 贺潇蒙, 刘娜, 盛春泉.  (1,3)-β-D-葡聚糖合成酶小分子抑制剂药效团模型的构建 . 药学实践与服务, 2018, 36(2): 116-120. doi: 10.3969/j.issn.1006-0111.2018.02.005
    [9] 王珂琪, 许维恒, 丁力, 张俊平.  蛋白激酶CK2α在大鼠肝纤维化病理过程中的表达变化 . 药学实践与服务, 2015, 33(6): 518-521,575. doi: 10.3969/j.issn.1006-0111.2015.06.010
    [10] 黄瑾, 王建, 袁芳, 胡文娟.  皮肤角质形成细胞中TRPV1受体激活后的蛋白质组差异分析 . 药学实践与服务, 2013, 31(5): 334-337. doi: 10.3969/j.issn.1006-0111.2013.05.004
    [11] 李敏, 姜鹏, 王淑萍, 韩琳, 黄慧梅, 畅婉琳, 柳润辉.  蛋白质组学在中药研究中的应用 . 药学实践与服务, 2013, 31(4): 241-245. doi: 10.3969/j.issn.1006-0111.2013.04.001
    [12] 孔丹凤, 赵雯, 卢婷利, 惠倩倩, 王韵晴, 陈涛.  分子印迹技术在药物分离中的研究进展 . 药学实践与服务, 2011, 29(3): 161-164.
    [13] 王婧, 肖振宇, 邱磊, 张俊平.  商陆皂苷甲作用于子宫内膜异位症大鼠腹腔巨噬细胞蛋白质组的差异分析 . 药学实践与服务, 2010, 28(6): 410-413,450.
    [14] 黄海强, 李慧梁, 汤健, 苏娟, 张卫东.  前列腺癌治疗新靶点——hedgehog通路 . 药学实践与服务, 2008, (4): 249-251.
    [15] 丁力, 丁家崇, 郭葆玉.  抗肿瘤药物新靶点半胱天冬酶-10 . 药学实践与服务, 2006, (2): 76-79.
    [16] 樊蓉, 张纯, 高申.  蛋白多肽类药物的药代动力学研究概况 . 药学实践与服务, 2006, (3): 135-138.
    [17] 李国栋, 王捷频.  蛋白质、多肽类药物制剂的研究现状 . 药学实践与服务, 2001, (6): 344-345,349.
    [18] 郭涛.  释放肽和蛋白质的聚合物 . 药学实践与服务, 1995, (2): 86-86.
    [19] 张淑香, 俞惠然, 杨淑云, 刘淑琴, 杨晶华, 邵泽生, 隋全正.  蓝萼甲素在体外对DNA, RNA和蛋白质生物合成的影响 . 药学实践与服务, 1990, (3): 62-64.
    [20] 刘海友.  心得安生物利用度受食物中蛋白质的影响 . 药学实践与服务, 1984, (1): 43-44.
  • 加载中
WeChat 点击查看大图
计量
  • 文章访问数:  2923
  • HTML全文浏览量:  205
  • PDF下载量:  432
  • 被引次数: 0
出版历程
  • 收稿日期:  2010-07-22
  • 修回日期:  2011-07-11

蛋白质结晶的新进展与药物设计

doi: 10.3969/j.issn.1006-0111.2012.02.001
  • 第二军医大学药学院无机化学教研室, 上海 200433
    • 基金项目:  国家自然科学基金资助项目(20371050).
  • 收稿日期: 2010-07-22
  • 修回日期: 2011-07-11

摘要: 蛋白质是生命的基础,其功能与它的三维结构密切相关,关于蛋白质的结构信息,对科学家根据结构同源性确定药物靶标以及发现新的药物靶标等方面均有至关重要的作用。因此,蛋白质晶体的获得及其与药物设计的关系日益受到重视,已成为生命科学中的一个重要领域,本文主要综述了蛋白质结晶技术的最新研究进展以及在药物设计中的应用。

English Abstract

陈维敬, 仲维清. 蛋白质结晶的新进展与药物设计[J]. 药学实践与服务, 2012, 30(2): 81-85,136. doi: 10.3969/j.issn.1006-0111.2012.02.001
引用本文: 陈维敬, 仲维清. 蛋白质结晶的新进展与药物设计[J]. 药学实践与服务, 2012, 30(2): 81-85,136. doi: 10.3969/j.issn.1006-0111.2012.02.001
shu
CHEN Wei-jing, ZHONG Wei-qing. New progress of protein crystallization and drug design[J]. Journal of Pharmaceutical Practice and Service, 2012, 30(2): 81-85,136. doi: 10.3969/j.issn.1006-0111.2012.02.001
Citation: CHEN Wei-jing, ZHONG Wei-qing. New progress of protein crystallization and drug design[J]. Journal of Pharmaceutical Practice and Service, 2012, 30(2): 81-85,136. doi: 10.3969/j.issn.1006-0111.2012.02.001
shu

    全文HTML

参考文献 (37)

目录

    /

    返回文章
    返回

    版权所有：《药学实践与服务》编辑委员会

    主管、主办: 中国人民解放军海军军医大学地址: 上海市杨浦区国和路325号邮政编码: 200433

    电话: （021）81871324,81871397 E-mail: yxsjzzs@163.com

    网站备案号 沪ICP备05003363号-1

    本系统由 北京仁和汇智信息技术有限公司 开发    百度统计