|本期目录/Table of Contents|

[1]葛慧华,张丹丹,吴姝羽,等.Foldon介导的寡聚化类弹性蛋白多肽的相变特性[J].应用与环境生物学报,2018,24(04):853-859.[doi:10.19675/j.cnki.1006-687x.2017.09045]
　GE Huihua,ZHANG Dandan,WU Shuyu,et al.Phase transition behavior of elastin-like polypeptides oligomerized with the Foldon domain[J].Chinese Journal of Applied & Environmental Biology,2018,24(04):853-859.[doi:10.19675/j.cnki.1006-687x.2017.09045]
点击复制

Foldon介导的寡聚化类弹性蛋白多肽的相变特性()
分享到：

《应用与环境生物学报》[ISSN:1006-687X/CN:51-1482/Q]

卷:
24卷
期数:
2018年04期
页码:
853-859
栏目:
研究论文
出版日期:
2018-08-20

文章信息/Info

Title:
Phase transition behavior of elastin-like polypeptides oligomerized with the Foldon domain
作者:
葛慧华; 张丹丹; 吴姝羽; 邱 岳; 张光亚
华侨大学化工学院生物工程与技术系 厦门 361021
Author(s):
GE Huihua;  ZHANG Dandan;  WU Shuyu;  QIU Yue & ZHANG Guangya**
Department of Bioengineering and Biotechnology, Huaqiao University, Xiamen 361021, China
关键词:
类弹性蛋白多肽; 相变温度; 拓扑结构与性能关系; Hofmeister离子序; 蛋白寡聚化
Keywords:
elastin-like polypeptides;  transition temperature;  relationship of topological structure and properties;  Hofmeister series;  protein oligomerization
分类号:
Q615 : Q51
DOI:
10.19675/j.cnki.1006-687x.2017.09045
摘要:
为了解SpyCatcher-ELPs40（C-E）相变异常的原因并考察寡聚化结构域对其相变行为的影响，将Foldon（F）分别与C-E和ELPs40（E）融合，构建拓扑结构为非共价三臂星型寡聚化的C-E-F和E-F；探究不同盐浓度和类型对其相变特性的影响，并与其他ELPs进行比较. 结果显示：融合了Foldon的ELPs40的相变温度高于线型ELPs120而低于线型ELPs40及SpyTag/SpyCatcher介导的共价三臂星型ELPs，非共价三臂星型C-E-F的相变温度变化幅度较大，与等重复数的C-E和ELPs40相比，平均分别高出28.75 ℃和35.6 ℃，尤其在NaCl浓度为0.8 mol/L时，相差分别为41.2 ℃和47.1 ℃. 同时，Na2CO3浓度在0.7 mol/L及以上时，非共价三臂星型C-E-F才会在低温下发生相变，而其在较低浓度的Na2SO4溶液中相变现象明显，不符合Hofmeister效应. 本研究报道了非线型ELPs特殊的相变行为，并证明ELPs拓扑结构会影响其相变行为，但Foldon和SpyCatcher表面电荷是更重要的因素. （图6 表1 参32）
Abstract:
To investigate the underlying mechanism of the unique phase transition behavior of SpyCatcher-ELPs40 (C-E) and the influence of the oligomerization domain on the phase transition of C-E, we constructed a non-covalent three-armed star oligomerization of C-E-F and E-F by fusing the Foldon (F) domain with SpyCatcher-ELPs40 (C-E) and ELPs40 (E). Results showed that the phase transition temperature of ELPs40 fused with Foldon was higher than that of ELPs120, whereas it was lower than those of ELPs40 and the SpyTag/SpyCatcher-mediated covalent three-armed elastin-like polypeptides (ELPs). This proved that the topology of ELPs could affect their phase transition behaviors. The phase transition temperature of C-E-F was 28.8 ℃ and 35.6 ℃ higher than those of C-E and ELPs40, respectively, although C-E-F had a similar sequence with C-E and ELPs40. When the concentration of NaCl was 0.8 mol/L, the differences in the phase transition temperatures were 41.2 ℃ and 47.1 , respectively. We could only observe the phase transition of C-E-F in the Na2CO3 solution with high concentration (≥ 0.7 mol/L); however, the phase transition could be clearly detected in the Na2SO4 solution, even when the concentration of Na2SO4 was very low. This result was obviously inconsistent with the Hofmeister series. This is the first report of non-linear ELPs that has shown this unique phase transition behavior. The possible reason was related to the charges distributed on the solvent accessible surface and the oligomeric state of C-E-F triggered by the Foldon domain.

参考文献/References:

1 Meyer DE, Chilkoti A. Genetically encoded synthesis of protein-based polymers with precisely specified molecular weight and sequence by recursive directional ligation: examples from the elastin-like polypeptide system [J]. Biomacromolecules, 2002, 3 (2): 357-367
2 Osborne JL, Farmer R, Woodhouse KA. Self-assembled elastin-like polypeptide particles. Acta Biomater, 2008, 4 (1): 49-57
3 Trabbic-Carlson K, Liu L, Kim B, Chilkoti A. Expression and purification of recombinant proteins from Escherichia coli: comparison of an elastin-like polypeptide fusion with an oligohistidine fusion [J]. Protein Sci, 2004, 13 (12): 3274-3284
4 Christensen T, Amiram M, Dagher S, Trabbic-Carlson K, Shamji MF, Setton LA, Chilkoti A. Fusion order controls expression level and activity of elastin-like polypeptide fusion proteins [J]. Protein Sci, 2009, 18 (7): 1377-1387
5 Meyer DE, Chilkoti A. Quantification of the effects of chain length and concentration on the thermal behavior of elastin-like polypeptides [J]. Biomacromolecules, 2004, 5 (3): 846-851
6 Cho Y, Zhang Y, Christensen T, Sagle LB, Chilkoti A, Cremer PS. Effects of Hofmeister anions on the phase transition temperature of elastin-like polypeptides [J]. J Phys Chem B, 2008, 112 (44): 13765-13771
7 Mcmillan RA, Conticello VP. Synthesis and characterization of elastin-mimetic protein gels derived from a well-defined polypeptide precursor [J]. Macromolecules, 2000, 33 (13): 4809-4821
8 葛慧华, 黄志宏, 王文研, 张诗冉, 张光亚. 以类弹性蛋白多肽为标签纯化1,3-丙二醇氧化还原酶[J]. 应用与环境生物学报, 2013, 19 (4): 709-712 [Ge HH, Huang ZH, Wang WY, Zhang SR, Zhang GY. Low concentration of salt triggers elastin-like polypeptides inverse transition to purify 1,3-propanediol oxidoreductase [J]. Chin J Appl Environ Biol, 2013, 19 (4): 709-712]
9 Chow D, Nunalee ML, Lim DW, Simnick AJ, Chilkoti A. Peptide-based biopolymers in biomedicine and biotechnology [J]. Mater Sci Eng R Rep, 2008, 62 (4): 125-155
10 Boudko SP, Londer YY, Letarov AV, Sernova NA, Engel J, Mesyanzhinov VV. Domain organization, folding and stability of bacteriophage T4 fibritin, a segmented coiled-coil protein [J]. Eur J Biochem, 2002, 269 (3): 833-841
11 Frank S, Kammerer RA, Mechling D, Schulthess T, Landwehr R, Bann J, Guo Y, Lustig A, B?chinger HP, Engel J. Stabilization of short collagen-like triple helices by protein engineering [J]. J Mol Biol, 2001, 308 (5): 1081-1089
12 Meier S, Güthe S, Kiefhaber T, Grzesiek S. Foldon, the natural trimerization domain of T4 fibritin, dissociates into a monomeric A-state form containing a stable beta-hairpin: atomic details of trimer dissociation and local beta-hairpin stability from residual dipolar couplings [J]. J Mol Biol, 2004, 344 (4): 1051-1069
13 Bhardwaj A, Walker-Kopp N, Wilkens S, Cingolani G. Foldon-guided self-assembly of ultra-stable protein fibers [J]. Protein Sci, 2008, 17 (9): 1475-1485
14 Wang X, Ge H, Zhang D, Wu S, Zhang G. Oligomerization triggered by foldon: a simple method to enhance the catalytic efficiency of lichenase and xylanase [J]. BMC Biotechnol, 2017, 17 (1): 57: 1-10
15 Zhang W, Sun F, Tirrell DA, Arnold FH. Controlling macromolecular topology with genetically encoded SpyTag-SpyCatcher chemistry [J]. J Am Chem Soc, 2013, 135: 13988-13997
16 Wang J, Wang Y, Wang X, Wu S, Zhang G. Enhanced thermal stability of lichenase from Bacillus subtilis 168 by SpyTag/SpyCatcher-mediated spontaneous cyclization [J]. Biotechnol Biofuels, 2016, 9 (1): 79:1-9
17 张丹丹, 蔡征文, 王金丹, 王心哲, 吴姝羽, 张光亚. 不同拓扑结构类弹性蛋白相变特性及机理研究. 中国科学: 化学, 2016, 46: 881-890 [Zhang DD, Cai ZW, Wang XZ, Wu SY, Zhang GY. The phase transition of elastin-like polypeptides with different topological structures [J]. Sci Sin Chem, 2016, 46: 881-890]
18 Roberts S, Dzuricky M, Chilkoti A. Elastin-like polypeptides as models of intrinsically disordered proteins [J]. FEBS Lett, 2015, 589 (19): 2477-2486
19 Macewan SR, Hassouneh W, Chilkoti A. Non-chromatographic purification of recombinant elastin-like polypeptides and their fusions with peptides and proteins from Escherichia coli [J]. J Vis Exp, 2014, 88: 1-8
20 Lim DW, Nettles DL, Setton LA, Chilkoti A. Rapid cross-linking of elastin-like polypeptides with (hydroxymethyl) phosphines in aqueous solution [J]. Biomacromolecules, 2007, 8 (5): 1463-1470
21 Lim DW, Trabbic-Carlson K, Mackay JA, Chilkoti A. Improved non-chromatographic purification of a recombinant protein by cationic elastin-like polypeptides [J]. Biomacromolecules, 2007, 8 (5): 1417-1424
22 Kracke B, Cole JT, Kaiser CJO, Hellenkamp B, Krysiak S, Ghoorchian A, Braun GB, Holland NB, Hugel T. Thermo-switchable nanoparticles based on elastin-like polypeptides [J]. Macromolecules, 2015, 48 (16): 5868-5877
23 Ghoorchian A, Cole JT, Holland NB. Thermoreversible micelle formation using a three-armed star elastin-like polypeptide [J]. Macromolecules, 2010, 43 (9): 4340-4345
24 Ghoorchian A, Holland NB. Molecular architecture influences the thermally induced aggregation behavior of elastin-like polypeptides [J]. Biomacromolecules, 2011, 12 (11): 4022-4029
25 Fujita Y, Mie M, Kobatake E. Construction of nanoscale protein particle using temperature-sensitive elastin-like peptide and polyaspartic acid chain [J]. Biomaterials, 2009, 30 (20): 3450-3457
26 Bataille L, Dieryck W, Hocquellet A. Recombinant production and purification of short hydrophobic Elastin-like polypeptides with low transition temperatures [J]. Protein Expres Purif, 2016, 121: 81-87
27 Mcdaniel JR, Radford DC, Chilkoti A. A unified model for de novo design of elastin-like polypeptides with tunable inverse transition temperatures [J]. Biomacromolecules, 2013, 14 (8): 2866-2872
28 Aladini F, Araman C, Becker CFW. Chemical synthesis and characterization of elastin‐like polypeptides (ELPs) with variable guest residues [J]. J Pep Sci, 2016, 22 (5): 334-342
29 Christensen T, Hassouneh W, Trabbic-Carlson K, Chilkoti A. Predicting transition temperatures of elastin-like polypeptide fusion proteins [J]. Biomacromolecules, 2013, 14 (5): 1514-1519
30 Guthe S, Kapinos L, M?glich A, Meier S, Grzesiek S, Kiefhaber T. Very fast folding and association of a trimerization domain from bacteriophage T4 fibritin [J]. J Mol Biol, 2004, 337 (4): 905-915
31 Zhang Y, Cremer PS. Chemistry of Hofmeister anions and osmolytes [J]. Annu Rev Phys Chem, 2010, 61: 63-83
32 Ghoorchian A, Vandemark K, Freeman K, Kanbow S, Holland NB, Streletzky KA. Size and shape characterization of thermoreversible micelles of three-armed star elastin-like polypeptides [J]. J Phys Chem B, 2013, 117 (29): 8865-887

相似文献/References:

[1]葛慧华,黄志宏,王文研,等.以类弹性蛋白多肽为标签纯化1,3-丙二醇氧化还原酶[J].应用与环境生物学报,2013,19(04):709.[doi:10.3724/SP.J.1145.2013.00709]
　GE Huihua,HUANG Zhihong,WANG Wenyan,et al.Low Concentration of Salt Triggers Elastin-like Polypeptides Inverse Transition to Purify 1,3-propanediol Oxidoreductase[J].Chinese Journal of Applied & Environmental Biology,2013,19(04):709.[doi:10.3724/SP.J.1145.2013.00709]
[2]葛慧华,吴姝羽,沈婷婷,等.类弹性蛋白多肽长度对不溶活性ELPs-木聚糖酶聚集体酶学性质的影响*[J].应用与环境生物学报,2016,22(05):848.[doi:10.3724/SP.J.1145.2015.12018]
　GE Huihua,WU Shuyu,SHEN Tingting & ZHANG Guangya**.The influence of elastin-like polypeptides length on the enzymatic properties of insoluble active ELPs-xylanase aggregates*[J].Chinese Journal of Applied & Environmental Biology,2016,22(04):848.[doi:10.3724/SP.J.1145.2015.12018]
[3]葛慧华,王心哲,邱岳,等.酶及寡聚化结构域影响类弹性蛋白多肽相变的规律及机制[J].应用与环境生物学报,2020,26(06):1534.[doi:DOI: 10.19675/j.cnki.1006-687x.2019.10045]
　GE Huihua,WANG Xinzhe,QIU Yue & ZHANG Guangya.Influences of exogenous enzymes and foldons on the phase transition of elastin-like polypeptides and the underlying mechanisms[J].Chinese Journal of Applied & Environmental Biology,2020,26(04):1534.[doi:DOI: 10.19675/j.cnki.1006-687x.2019.10045]

更新日期/Last Update: 2018-08-25