Login Register Cart 0
Generic placeholder image

Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Back
Journal Home About Journal Editorial Board Journal Insight Current Issue Volumes/Issues
Subscribe
Research Article

Investigation on the Interaction between Tetrakis (4-carboxylphenyl) Porphyrin and CopC by Spectroscopy and Docking Methods

Author(s): Zhen Song*, Jin Liu, Wen Yuan, Ze Bai and Nvwa Gao

Volume 27, Issue 7, 2020

Page: [674 - 685] Pages: 12

DOI: 10.2174/0929866526666191204124245

Price: $65

Abstract

Background: Recently, the small molecule that inhibits the human copper-trafficking proteins Atox1 and CCS was reported, which suggested that small molecule has an effect on the copper regulation system in the cell. The copper chaperones CopC is regarded as a redox switch and possess barrel structure, thus the interaction between CopC and small molecules could give helpful information to elucidate the copper regulation mechanism. In addition, porphyrins play an important role in the metabolism of living body. In the early-stage tumors, porphyrins were usually used to diagnosis. After the amphiphilic porphyrins were given by intravenous injection, serum albumins and serum proteins were the most usual carrier to transfer them. Then these molecules can accumulate in malignant tumours and contact with cancer cells. Obviously, in drug distribution and efficacy, investigation of the interaction between the porphyrins and protein is an important research area. Obviously, in drug distribution and efficacy, investigation of the interaction between the porphyrins and protein is an important research area.

Objective: In this article, our motivation is to establish a relation between Tetrakis (4- carboxylphenyl) porphyrin and CopC.

Methods: In this article, we propose a framework for achieving our aforementioned object. Firstly, FTIR spectra and CD were used to detect the structure changes of CopC. Secondly, the fluorescence spectroscopic and UV-Vis spectra were used to measure quenching mechanism, binding distance, binding site and binding distance. Using Tb 3+ as a probe to detect the interaction between CopC and TCPP. Finally, molecular docking methods was used to show the results more vivid.

Results: Following the proposed framework, firstly, FTIR and CD results indicated that the CopC conformation was changed by TCPP. The β-sheet content was reduced and the random coil content was increased. Secondly, fluorescence spectra data indicated that the combination ratio of TCPPCopC was 1:1, and the inclusion constant is (5.88 ± 0.12) × 10 5 M -1 . In addition, Tb 3+ was used as a probe to detect the interaction between CopC and TCPP. The result further verified that CopC can interact with TCPP. The thermodynamic parameters of interaction between CopC and TCPP (ΔH, ΔS) indicated that the force between CopC and TCPP was mainly hydrophobic interaction. Finally, the distance between tryptophan in CopC and TCPP was calculated through forster energy transfer and molecular docking.

Conclusion: The results revealed that TCPP can form 1:1 complex with CopC, and the binding constant has been calculated to be (5.88 ± 0.12) × 10 5 M -1 . In addition, it was revealed that TCPP quench the fluorescence of CopC by the static quenching mechanism and the binding site n equals one. The formation of CopC-TCPP complex depended on the hydrophobic force and the distance between TCPP and tryptophan residue in CopC was 2.07 nm.

Keywords: CopC, TCPP, fluorescence, copper, dock, interaction.

« Previous
Graphical Abstract

[1]
Xiao, C.Q.; Jiang, F.L.; Zhou, B.; Li, R.; Liu, Y. Interaction between a cationic porphyrin and bovine serum albumin studied by surface plasmon resonance, fluorescence spectroscopy and cyclic voltammetry. Photochem. Photobiol. Sci., 2011, 10(7), 1110-1117.
[http://dx.doi.org/10.1039/c1pp05008g] [PMID: 21431181]
[2]
Lu, X.L.; Fan, J.J.; Liu, Y.; Hou, A.X. Characterization of the interaction between cationic Erbium (III)–porphyrin complex with bovine serum albumin. J. Mol. Struct., 2009, 934, 1-8.
[http://dx.doi.org/10.1016/j.molstruc.2009.05.037]
[3]
Campbell, D.L.; Gudgin-Dickson, E.F.; Forkert, P.G.; Pottier, R.H.; Kennedy, J.C. Detection of early stages of carcinogenesis in adenomas of murine lung by 5-aminolevulinic acid-induced protoporphyrin IX fluorescence. Photochem. Photobiol., 1996, 64(4), 676-682.
[http://dx.doi.org/10.1111/j.1751-1097.1996.tb03123.x] [PMID: 8863473]
[4]
Saboktakin, M.R.; Tabatabaie, R.M.; Ostovarazar, P.; Maharramov, A.; Ramazanov, M.A. Synthesis and characterization of modified starch hydrogels for photodynamic treatment of cancer. Int. J. Biol. Macromol., 2012, 51(4), 544-549.
[http://dx.doi.org/10.1016/j.ijbiomac.2012.06.024] [PMID: 22732133]
[5]
Saboktakin, M.R.; Tabatabaee, R.M. The novel polymeric systems for photodynamic therapy technique. Int. J. Biol. Macromol., 2014, 65, 398-414.
[http://dx.doi.org/10.1016/j.ijbiomac.2014.01.019] [PMID: 24440522]
[6]
Sil, S.; Chakraborti, A.S. Binding of porphyrin to horseradish peroxidase: Effects on structure and function. Int. J. Biol. Macromol., 2005, 36(1-2), 16-22.
[http://dx.doi.org/10.1016/j.ijbiomac.2005.03.003] [PMID: 15907997]
[7]
Robinson, N.J.; Winge, D.R. Copper metallochaperones. Annu. Rev. Biochem., 2010, 79, 537-562.
[http://dx.doi.org/10.1146/annurev-biochem-030409-143539] [PMID: 20205585]
[8]
Huffman, D.L.; O’Halloran, T.V. Energetics of copper trafficking between the Atx1 metallochaperone and the intracellular copper transporter, CCC2. J. Biol. Chem., 2000, 275(25), 18611-18614.
[http://dx.doi.org/10.1074/jbc.C000172200] [PMID: 10764731]
[9]
Arnesano, F.; Banci, L.; Bertini, I.; Mangani, S.; Thompsett, A.R. A redox switch in CopC: An intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites. Proc. Natl. Acad. Sci. USA, 2003, 100(7), 3814-3819.
[http://dx.doi.org/10.1073/pnas.0636904100] [PMID: 12651950]
[10]
Rae, T.D.; Schmidt, P.J.; Pufahl, R.A.; Culotta, V.C.; O’Halloran, T.V. Undetectable intracellular free copper: The requirement of a copper chaperone for superoxide dismutase. Science, 1999, 284(5415), 805-808.
[http://dx.doi.org/10.1126/science.284.5415.805] [PMID: 10221913]
[11]
Puig, S.; Thiele, D.J. Molecular mechanisms of copper uptake and distribution. Curr. Opin. Chem. Biol., 2002, 6(2), 171-180.
[http://dx.doi.org/10.1016/S1367-5931(02)00298-3] [PMID: 12039001]
[12]
Arnesano, F.; Banci, L.; Bertini, I.; Thompsett, A.R. Solution structure of CopC: A cupredoxin-like protein involved in copper homeostasis. Structure, 2002, 10(10), 1337-1347.
[http://dx.doi.org/10.1016/S0969-2126(02)00858-4] [PMID: 12377120]
[13]
Djoko, K.Y.; Xiao, Z.; Huffman, D.L.; Wedd, A.G. Conserved mechanism of copper binding and transfer. A comparison of the copper-resistance proteins PcoC from Escherichia coli and CopC from Pseudomonas syringae. Inorg. Chem., 2007, 46(11), 4560-4568.
[http://dx.doi.org/10.1021/ic070107o] [PMID: 17477524]
[14]
Koay, M.; Zhang, L.; Yang, B.; Maher, M.J.; Xiao, Z.; Wedd, A.G.; Cop, C. CopC protein from Pseudomonas syringae: Intermolecular transfer of copper from both the copper(I) and copper(II) sites. Inorg. Chem., 2005, 44(15), 5203-5205.
[http://dx.doi.org/10.1021/ic0506198] [PMID: 16022515]
[15]
Sze, C.M.; Khairallah, G.N.; Xiao, Z.; Donnelly, P.S.; O’Hair, R.A.J.; Wedd, A.G. Interaction of cisplatin and analogues with a Met-rich protein site. J. Biol. Inorg. Chem., 2009, 14(2), 163-165.
[http://dx.doi.org/10.1007/s00775-008-0452-x] [PMID: 19034536]
[16]
Song, Z.; Zheng, X.; Yang, B. Conformational stability of CopC and roles of residues Tyr79 and Trp83. Protein Sci., 2013, 22(11), 1519-1530.
[http://dx.doi.org/10.1002/pro.2338] [PMID: 23963820]
[17]
Wang, J.; Luo, C.; Shan, C.; You, Q.; Lu, J.; Elf, S.; Zhou, Y.; Wen, Y.; Vinkenborg, J.L.; Fan, J.; Kang, H.; Lin, R.; Han, D.; Xie, Y.; Karpus, J.; Chen, S.; Ouyang, S.; Luan, C.; Zhang, N.; Ding, H.; Merkx, M.; Liu, H.; Chen, J.; Jiang, H.; He, C. Inhibition of human copper trafficking by a small molecule significantly attenuates cancer cell proliferation. Nat. Chem., 2015, 7(12), 968-979.
[http://dx.doi.org/10.1038/nchem.2381] [PMID: 26587712]
[18]
Pang, E.; Zhao, Y.; Yang, B.S. Fluorescence study on the interaction between apoCopC and cupric. Chin. Sci. Bull., 2005, 50, 2302-2305.
[http://dx.doi.org/10.1007/BF03183739]
[19]
Byler, D.M.; Susi, H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers, 1986, 25(3), 469-487.
[http://dx.doi.org/10.1002/bip.360250307] [PMID: 3697478]
[20]
Mandeville, J.S.; Froehlich, E.; Tajmir-Riahi, H.A. Study of curcumin and genistein interactions with human serum albumin. J. Pharm. Biomed. Anal., 2009, 49(2), 468-474.
[http://dx.doi.org/10.1016/j.jpba.2008.11.035] [PMID: 19135819]
[21]
Wu, S.Y.; Pérez, M.D.; Puyol, P.; Sawyer, L. β-lactoglobulin binds palmitate within its central cavity. J. Biol. Chem., 1999, 274(1), 170-174.
[http://dx.doi.org/10.1074/jbc.274.1.170] [PMID: 9867826]
[22]
Demirdöven, N.; Cheatum, C.M.; Chung, H.S.; Khalil, M.; Knoester, J.; Tokmakoff, A. Two-dimensional infrared spectroscopy of antiparallel β-sheet secondary structure. J. Am. Chem. Soc., 2004, 126(25), 7981-7990.
[http://dx.doi.org/10.1021/ja049811j] [PMID: 15212548]
[23]
Burstein, E.A.; Vedenkina, N.S.; Ivkova, M.N. Fluorescence and the location of tryptophan residues in protein molecules. Photochem. Photobiol., 1973, 18(4), 263-279.
[http://dx.doi.org/10.1111/j.1751-1097.1973.tb06422.x] [PMID: 4583619]
[24]
Jiang, C.Q.; Luo, L. Lysozyme enhanced europium–metacycline complex fluorescence: A new spectrofluorimetric method for the determination of lysozyme. Anal. Chim. Acta, 2004, 511, 11-16.
[http://dx.doi.org/10.1016/j.aca.2004.01.043]
[25]
Jahanban-Esfahlan, A.; Panahi-Azar, V.; Sajedi, S. Spectroscopic and molecular docking studies on the interaction between N-acetyl cysteine and bovine serum albumin. Biopolymers, 2015, 103(11), 638-645.
[http://dx.doi.org/10.1002/bip.22697] [PMID: 26139573]
[26]
Ware, W.R. Oxygen quenching of fluorescence in solution an experimental study of the diffusion process. J. Phys. Chem., 1962, 66, 455-458.
[http://dx.doi.org/10.1021/j100809a020]
[27]
Lakowicz, J.R.; Weber, G. Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules. Biochemistry, 1973, 12(21), 4161-4170.
[http://dx.doi.org/10.1021/bi00745a020] [PMID: 4795686]

Rights & Permissions Print Cite
Article Metrics
23
© 2024 Bentham Science Publishers | Privacy Policy