Small amine molecules: Solvent design toward facile improvement of protein stability against aggregation and inactivation

Current Pharmaceutical Biotechnology

Volumn 17, Issue 2, 2016, Pages 116-125

  Shiraki, Kentaro ^a   Tomita, Shunsuke ^b   Inoue, Naoto ^a  

^a UNIVERSITY OF TSUKUBA   (Japan)

^b NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

Author keywords

Amine compound; Amino acid derivative; Arginine; Polyamine; Protein aggregation; Protein inactivation; Solvent additive

Indexed keywords

AMINE; LYSOZYME; AMINO ACID; PROTEIN; SOLVENT;

ARTICLE; CHEMICAL MODIFICATION; ENZYME ACTIVITY; HEAT TREATMENT; LIPID SOLUBILITY; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN STABILITY; ANIMAL; CHEMISTRY; HUMAN; SOLUBILITY;

AMINES; AMINO ACIDS; ANIMALS; HUMANS; PROTEIN STABILITY; PROTEINS; SOLUBILITY; SOLVENTS;

EID: 84949844521     PISSN: 13892010     EISSN: 18734316     Source Type: Journal    
DOI: 10.2174/1389201017666151029110229     Document Type: Article

References (105)

1. Manning, M.C.; Chou, D.K.; Murphy, B.M.; Payne, R.W.; Katayama, D.S. Stability of protein pharmaceuticals: An update. Pharm. Res., 2010, 27, 544-575.
2. Hamada, H.; Arakawa, T.; Shiraki, K. Effect of additives on protein aggregation. Curr. Pharm. Biotechnol., 2009, 10, 400-407.
3. Shiraki, K.; Kudou, M.; Fujiwara, S.; Imanaka, T.; Takagi, M. Biophysical effect of amino acids on the prevention of protein aggregation. J. Biochem., 2002, 132, 591-595.
4. Buchner, J.; Rudolph, R. Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli. Bio/Technol., 1991, 9, 157-162.
5. Shiraki, K.; Kudou, M.; Nishikori, S.; Kitagawa, H.; Imanaka, T.; Takagi, M. Arginine ethylester prevents thermal inactivation and aggregation of lysozyme. Eur. J. Biochem., 2004, 271, 3242-3247.
6. Shiraki, K.; Kudou, M.; Sakamoto, R.; Yanagihara, I.; Takagi, M. Amino acid esters prevent thermal inactivation and aggregation of lysozyme. Biotechnol. Prog., 2005, 21, 640-643.
7. Matsuoka, T.; Tomita, S.; Hamada, H.; Shiraki, K. Amidated amino acids are prominent additives to prevent heat-induced aggregation of lysozyme. J. Biosci. Bioeng., 2007, 103, 440-443.
8. Hamada, H.; Shiraki, K. L-Argininamide improves the refolding more effectively than L-arginine. J. Biotechnol., 2007, 130, 153-160.
9. Matsuoka, T.; Hamada, H.; Matsumoto, K.; Shiraki, K. Indispensable structure of solution additives to prevent inactivation of lysozyme for heating and refolding. Biotechnol. Prog., 2009, 25, 1515-1524.
10. Okanojo, M.; Shiraki, K.; Kudou, M.; Nishikori, S.; Takagi, M. Diamines prevent thermal aggregation and inactivation of lysozyme. J. Biosci. Bioeng., 2005, 100, 556-561.
11. Kudou, M.; Shiraki, K.; Fujiwara, S.; Imanaka, T.; Takagi, M. Prevention of thermal inactivation and aggregation of lysozyme by polyamines. Eur. J. Biochem., 2003, 270, 4547-4554.
12. Hirano, A.; Hamada, H.; Shiraki, K. Trans-cyclohexanediamines prevent thermal inactivation of protein: role of hydrophobic and electrostatic interactions. Protein J., 2008, 27, 253-257.
13. Hirano, A.; Hamada, H.; Okubo, T.; Noguchi, T.; Higashibata, H.; Shiraki, K. Correlation between thermal aggregation and stability of lysozyme with salts described by molar surface tension increment: an exceptional propensity of ammonium salts as aggregation suppressor. Protein J., 2007, 26, 423-433.
14. Ahern, T.J.; Klibanov, A.M. The mechanisms of irreversible enzyme inactivation at 100oC. Science, 1985, 228, 1280-1284.
15. Zale, S.E.; Klibanov, A.M. Why does ribonuclease irreversibly inactivate at high temperatures? Biochemistry, 1986, 25, 5432-5444.
16. Volkin, D.B.; Klibanov, A.M. Thermal destruction processes in proteins involving cystine residues. J. Biol. Chem., 1987, 262, 2945-2950.
17. Volkin, D.B.; Mach, H.; Middaugh, C.R. Degradative covalent reactions important to protein stability. Mol. Biotechnol., 1997, 8, 105-122.
18. Tyler-Cross, R.; Schirch, V. Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides. J. Biol. Chem., 1991, 266, 22549-22556.
19. Wright, H.T. Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins. Crit. Rev. Biochem. Mol. Biol., 1991, 26, 1-52.
20. Chelius, D.; Rehder, D.S.; Bondarenko, P.V. Identification and characterization of deamidation sites in the conserved regions of human immunoglobulin gamma antibodies. Anal. Chem., 2005, 77, 6004-6011.
21. Krokhin, O.V.; Antonovici, M.; Ens, W.; Wilkins, J.A.; Standing, K.G. Deamidation of-Asn-Gly-sequences during sample preparation for proteomics: Consequences for MALDI and HPLC-MALDI analysis. Anal. Chem., 2006, 78, 6645-6650.
22. Patel, K.; Borchardt, R.T. Chemical pathways of peptide degradation. II. Kinetics of deamidation of an asparaginyl residue in a model hexapeptide. Pharm. Res., 1990, 7, 703-711.
23. Cohen, S.L.; Price, C.; Vlasak, J. β-elimination and peptide bond hydrolysis: Two distinct mechanisms of human IgG1 hinge fragmentation upon storage. J. Am. Chem. Soc., 2007, 129, 6976-6977.
24. Wang, Z.; Rejtar, T.; Zhou, Z.S.; Karger, B.L. Desulfurization of cysteine-containing peptides resulting from sample preparation for protein characterization by mass spectrometry. Rapid Commun. Mass Spectrom., 2010, 24, 267-275.
25. Ahern, T.J.; Klibanov, A.M. Analysis of processes causing thermal inactivation of enzymes. Methods Biochem. Anal., 1988, 33, 91-127.
26. Florence, T.M. Degradation of protein disulphide bonds in dilute alkali. Biochem. J., 1980, 189, 507-520.
27. Wang, W. Protein aggregation and its inhibition in biopharmaceutics. Int. J. Pharm., 2005, 289, 1-30.
28. Davies, M.J. The oxidative environment and protein damage. Biochim. Biophys. Acta, 2005, 1703, 93-109.
29. Takai, E.; Kitamura, T.; Kuwabara, J.; Ikawa, S.; Yoshizawa, S.; Shiraki, K.; Kawasaki, H.; Arakawa, R.; Kitano, K. Chemical modification of amino acids by atmospheric-pressure cold plasma in aqueous solution. J. Phys. D: Appl. Phys., 2014, 47, 285403.
30. Joshi, A.B.; Sawai, M.; Kearney, W.R.; Kirsch, L.E. Studies on the mechanism of aspartic acid cleavage and glutamine deamidation in the acidic degradation of glucagon. J. Pharm. Sci., 2005, 94, 1912-1927.
31. Tomita, S.; Shiraki, K. Why do solution additives suppress the heat-induced inactivation of proteins? inhibition of chemical modifications. Biotechnol. Prog., 2011, 27, 855-862.
32. Kurinomaru, T.; Kameda, T.; Shiraki, K. Effects of hydrophobicity and multivalency of polyamines on enzyme hyperactivation of α-chymotrypsin. J. Mol. Catal. B: Enzymatic, 2015, 115, 135-139.
33. Arakawa, T.; Kita, Y. Multi-faceted arginine: mechanism of the effects of arginine on protein. Curr. Protein Pept. Sci., 2014, 15, 608-620.
34. Rudolph, R.; Lilie, H. In vitro folding of inclusion body proteins. FASEB J., 1996, 10, 49-56.
35. Lilie, H.; Schwarz, E.; Rudolph, R. Advances in refolding of proteins produced in E. coli. Curr. Opin. Biotechnol., 1998, 9, 497-501.
36. Lange, C.; Rudolph, R. Suppression of protein aggregation by Larginine. Curr. Pharm. Biotechnol., 2009, 10, 408-414.
37. Buchner, J.; Pastan, I.; Brinkmann, U. A method for increasing the yield of properly folded recombinant fusion proteins: Single-chain immunotoxins from renaturation of bacterial inclusion bodies. Anal. Biochem., 1992, 205, 263-270.
38. Kohnert, U.; Rudolph, R.; Verheijen, J.H.; Weening-Verhoeff, E.J.; Stern, A.; Opitz, U.; Martin, U.; Lill, H.; Prinz, H.; Lechner, M.; Kresse, G.B.; Bucket, P.; Fischer, S. Biochemical properties of the kringle 2 and protease domains are maintained in the refolded t-PA deletion variant BM 06.022. Protein Eng., 1992, 5, 93-100.
39. Lin, W.J.; Traugh, J.A. Renaturation of casein kinase II from recombinant subunits produced in Escherichia coli: Purification and characterization of the reconstituted holoenzyme. Protein Expr. Purif., 1993, 4, 256-264.
40. Stoyan, T.; Michaelis, U.; Schooltink, H.; Van Dam, M.; Rudolph, R.; Heinrich, P.C.; Rose-John, S. Recombinant soluble human interleukin-6 receptor. Expression in Escherichia coli, renaturation and purification. Eur. J. Biochem., 1993, 216, 239-245.
41. Ahn, J.H.; Lee, Y.P.; Rhee, J.S. Investigation of refolding condition for Pseudomonas fluorescens lipase by response surface methodology. J. Biotechnol., 1997, 54, 151-160.
42. Suenaga, M.; Ohmae, H.; Tsuji, S.; Itoh, T.; Nishimura, O. Renaturation of recombinant human neurotrophin-3 from inclusion bodies using a suppressor agent of aggregation. Biotechnol. Appl. Biochem., 1998, 28, 119-124.
43. Tsumoto, K.; Shinoki, K.; Kondo, H.; Uchikawa, M.; Juji, T.; Kumagai, I. Highly efficient recovery of functional single-chain Fv fragments from inclusion bodies overexpressed in Escherichia coli by controlled introduction of oxidizing reagent-application to a human single-chain Fv fragment. J. Immunol. Methods, 1998, 219, 119-129.
44. Asano, R.; Kudo, T.; Makabe, K.; Tsumoto, K.; Kumagai, I. Antitumor activity of interleukin-21 prepared by novel refolding procedure from inclusion bodies expressed in Escherichia coli. FEBS Lett., 2002, 528, 70-76.
45. Fujiwara, Y.; Aiki, Y.; Yang, L.; Takaiwa, F.; Kosaka, A.; Tsuji, N.M.; Shiraki, K.; Sekikawa, K. Extraction and purification of human interleukin-10 from transgenic rice seeds. Protein Expr. Purif., 2010, 72, 125-130.
46. Umetsu, M.; Tsumoto K.; Hara, M.; Ashish, K.; Goda, S.; Kumagai, I. How additives influence the refolding of immunoglobulinfolded proteins in a stepwise dialysis system. Spectroscopic evidence for highly efficient refolding of a single-chain Fv fragment. J. Biol. Chem. 2003, 278, 8979-8987.
47. Fujimoto, A.; Hirano, A.; Shiraki, K. Ternary system of solution additives with arginine and salt for refolding of β-galactosidase. Protein J., 2010, 29, 161-166.
48. Kudou, M.; Ejima, D.; Sato, H.; Yumioka, R.; Arakawa, T.; Tsumoto, K Refolding single-chain antibody (scFv) using lauroyl-Lglutamate as a solubilization detergent and arginine as a refolding additive. Protein Expr. Purif. 2011, 77, 68-74.
49. Gunda, V.; Boosani, C.S.; Verma, R.K.; Guda, C.; Sudhakar, Y.A. L-Arginine mediated renaturation enhances yield of human, α6 Type IV collagen non-collagenous domain from bacterial inclusion bodies. Protein Pept. Lett. 2012, 19, 1112-1121.
50. Flocco, M.M.; Mowbray, S.L. Planar stacking interactions of arginine and aromatic side-chains in proteins. J. Mol. Biol., 1994, 235, 709-717.
51. Mitchell, J.B.; Nandi, C.L.; McDonald, I.K.; Thornton, J.M.; Price, S.L. Amino/aromatic interactions in proteins: is the evidence stacked against hydrogen bonding? J. Mol. Biol. 1994, 239, 315-331.
52. Schug, K.A.; Lindner, W. Noncovalent binding between guanidinium and anionic groups: Focus on biological-and synthetic-based arginine/guanidinium interactions with phosph[on]ate and sulf[on]ate residues. Chem. Rev., 2005, 105, 67-114.
53. Shah, D.; Li, J.; Shaikh, A.R.; Rajagopalan, R. Arginine-aromatic interactions and their effects on arginine-induced solubilization of aromatic solutes and suppression of protein aggregation. Biotechnol. Prog. 2012, 28, 223-231.
54. Arakawa, T.; Kitam Y.; Koyama A.H. Solubility enhancement of gluten and organic compounds by arginine. Int. J. Pharm., 2008, 355, 220-223.
55. Takai, E.; Yoshizawa, S.; Ejima, D.; Arakawa, T.; Shiraki, K. Synergistic solubilization of porcine myosin in physiological salt solution by arginine. Int. J. Biol. Macromol., 2013, 62, 647-651.
56. Arakawa, T.; Tsumoto, K. The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation. Biochem. Biophys. Res. Commun., 2003, 304, 148-152.
57. Ishibashi, M.; Tsumoto, K.; Tokunaga, M.; Ejima, D.; Kita, Y.; Arakawa, T. Is arginine a protein-denaturant? Protein Expr. Purif., 2005, 42, 1-6.
58. Ito, L.; Shiraki, K.; Matsuura, T.; Okumura, M.; Hasegawa, K.; Baba, S.; Yamaguchi, H.; Kumasaka, T. High-resolution X-ray analysis reveals binding of arginine to aromatic residues of lysozyme surface: Implication of suppression of protein aggregation by arginine. Protein Eng., 2011, 24, 269-274.
59. Nakakido, M.; Tanaka, Y.; Mitsuhori, M.; Kudou, M.; Ejima, D.; Arakawa, T.; Tsumoto, K. Structure-based analysis reveals hydration changes induced by arginine hydrochloride. Biophys. Chem., 2008, 137, 105-109.
60. Hirano, A.; Arakawa, T.; Shiraki, K. Arginine increases the solubility of coumarin: Comparison with salting-in and salting-out additives. J. Biochem., 2008, 144, 363-369.
61. Hirano, A.; Kameda, T.; Arakawa, T.; Shiraki, K. Arginine-assisted solubilization system for drug substances: Solubility experiment and simulation. J. Phys. Chem. B, 2010, 114, 13455-13462.
62. Arakawa, T.; Hirano, A.; Shiraki, K.; Kita, Y.; Koyama, A.H. Stabilizing and destabilizing effects of arginine on deoxyribonucleic acid. Int. J. Biol. Macromol., 2010, 46, 217-222.
63. Hirano, A.; Tokunaga, H.; Tokunaga, M.; Arakawa, T.; Shiraki, K. The solubility of nucleobases in aqueous arginine solutions. Arch. Biochem. Biophys., 2010, 497, 90-96.
64. Ariki, R.; Hirano, A.; Arakawa, T.; Shiraki, K. Arginine increases the solubility of alkyl gallates through interaction with the aromatic ring. J. Biochem., 2011, 149, 389-394.
65. Hirano, A.; Kameda, T.; Shinozaki, D.; Arakawa, T.; Shiraki, K. Molecular dynamics simulation of the arginine-assisted solubilization of caffeic acid: Intervention in the interaction. J. Phys. Chem. B, 2013, 117, 7518-7527.
66. Baynes, B.M.; Trout, B.L. Rational design of solution additives for the prevention of protein aggregation. Biophys. J., 2004, 87, 1631-1639.
67. Baynes, B.M.; Wang, D.I.; Trout, B.L. Role of arginine in the stabilization of proteins against aggregation. Biochemistry, 2005, 44, 4919-4925.
68. Shukla, D.; Trout, B.L. Interaction of arginine with proteins and the mechanism by which it inhibits aggregation. J. Phys. Chem. B, 2010, 114, 13426-13438.
69. Vagenende, V.; Han, A.X.; Mueller, M.; Trout, B.L. Proteinassociated cation clusters in aqueous arginine solutions and their effects on protein stability and size. ACS Chem. Biol., 2013, 8, 416-422.
70. Woods, A.S. The mighty arginine, the stable quaternary amines, the powerful aromatics, and the aggressive phosphate: Their role in the noncovalent minuet. J. Proteome Res., 2004, 3, 478-484.
71. Crowley, P.B.; Golovin, A. Cation-π interactions in protein-protein interfaces. Proteins, 2004, 59, 231-239.
72. Luo, R.; David, L.; Hung, H.; Devaney, J.; Gilson, M.K. Strength of Solvent-Exposed Salt-Bridges. J. Phys. Chem. B, 1999, 103, 727-736.
73. Springs, B.; Haake, P. Equilibrium constants for association of guanidinium and ammonium ions with oxyanions: The effect of changing basicity of the oxyanion. Bioorg. Chem., 1977, 6, 181-190.
74. Shah, D.; Shaikh, A.R.; Peng, X.; Rajagopalan, R. Effects of arginine on heat-induced aggregation of concentrated protein solutions. Biotechnol. Prog., 2011, 27, 513-520.
75. Arakawa, T.; Timasheff, S.N. Preferential interactions of proteins with solvent components in aqueous amino acid solutions. Arch. Biochem. Biophys., 1983, 224, 169-177.
76. Arakawa, T.; Timasheff, S.N. Preferential interactions of proteins with salts in concentrated solutions. Biochemistry, 1982, 21, 6545-6552.
77. Arakawa, T.; Timasheff, S.N. Mechanism of protein salting in and salting out by divalent cation salts: Balance between hydration and salt binding. Biochemistry, 1984, 23, 5912-5923.
78. Arakawa, T.; Ejima, D.; Tsumoto, K.; Obeyama, N.; Tanaka, Y.; Kita, Y.; Timasheff, S.N. Suppression of protein interactions by arginine: a proposed mechanism of the arginine effects. Biophys. Chem., 2007, 127, 1-8.
79. Inoue, N.; Takai, E.; Arakawa, T.; Shiraki, K. Arginine and lysine reduce the high viscosity of serum albumin solutions for pharmaceutical injection. J. Biosci. Bioeng., 2014, 117, 539-543.
80. Inoue, N.; Takai, E.; Arakawa, T.; Shiraki, K Specific decrease in solution viscosity of antibodies by arginine for therapeutic formulations. Mol. Pharm., 2014, 11, 1889-1896.
81. Cirkovas, A.; Sereikaite, J. Different effects of L-arginine on the heat-induced unfolding and aggregation of proteins. Biologicals, 2011, 39, 181-188.
82. Fukuda, M.; Kameoka, D.; Torizawa, T.; Saitoh, S.; Yasutake, M.; Imaeda, Y.; Koga, A.; Mizutani, A. Thermodynamic and fluorescence analyses to determine mechanisms of IgG1 stabilization and destabilization by arginine. Pharm. Res., 2014, 31, 992-1002.
83. Takai, E.; Uda, K.; Matsushita, S.; Shikiya, Y.; Yamada, Y.; Shiraki, K.; Zako, T.; Maeda, M. Cysteine inhibits amyloid fibrillation of lysozyme and directs the formation of small worm-like aggregates through non-covalent interactions. Biotechnol. Prog., 2014, 30, 470-478.
84. Clark, E.D. Refolding of recombinant proteins. Curr. Opin. Biotechnol., 1998, 9, 157-163.
85. Clark, E.D. Protein refolding for industrial processes. Curr. Opin. Biotechnol., 2001, 12, 202-207.
86. Maeda, Y.; Koga, H.; Yamada, H.; Ueda, T.; Imoto, T. Effective renaturation of reduced lysozyme by gentle removal of urea. Protein Eng., 1995, 8, 201-205.
87. Rozema, D.; Gellman, S.H. Artificial chaperone-assisted refolding of denatured-reduced lysozyme: Modulation of the competition between renaturation and aggregation. Biochemistry, 1996, 35, 15760-15771.
88. Wang, S.; Raghani, A. Arginine as an eluent for automated on-line Protein A/size exclusion chromatographic analysis of monoclonal antibody aggregates in cell culture. J. Chromatogr. B, 2014, 945, 115-120.
89. Tsumoto, K.; Umetsu, M.; Kumagai, I.; Ejima, D.; Arakawa, T. Solubilization of active green fluorescent protein from insoluble particles by guanidine and arginine. Biochem. Biophys. Res. Commun., 2003, 312, 1383-1386.
90. Hamada, H.; Takahashi, R.; Noguchi, T.; Shiraki, K. The differences in the effect of solution additives on heat-and refoldinginduced aggregation. Biotechnol. Prog., 2008, 24, 436-443.
91. Tomita, S.; Tanabe, Y.; Shiraki, K. Oligoethylene glycols prevent thermal aggregation of α-chymotrypsin in a temperature-dependent manner: implications for design guidelines. Biotechnol. Prog., 2013, 29, 1325-1330.
92. Raina, A.; Jänne, J. Physiology of the natural polyamines putrescine, spermidine and spermine. Med. Biol., 1975, 53, 121-147.
93. Robert, A, Casero, Jr.; Anthony, E. Polyamine catabolism and disease. Biochem. J., 2009, 421, 323-338.
94. Minois, N.; Carmona-Gutierrez, D.; Madeo, F. Polyamines in aging and disease. Aging, 2011, 3, 716-732.
95. Yancey, P.H.; Clark, M.E.; Hand, S.C.; Bowlus, R.D.; Somero, G.N. Living with water stress: evolution of osmolyte systems. Science, 1982, 217, 1214-1222.
96. Perl, D.; Welker, C.; Schindler, T.; Schröder, K.; Marahiel, MA.; Jaenicke, R.; Schmid, F.X. Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nat. Struct. Biol., 1998, 5, 229-35.
97. Motono, C.; Yamagishi, A.; Oshima, T. Urea-induced unfolding and conformational stability of 3-isopropylmalate dehydrogenase from the thermophile thermus thermophilus and its mesophilic counterpart from Escherichia coli. Biochemistry, 1999, 38, 1332-1337.
98. Shiraki, K.; Nishikori, S.; Fujiwara, S.; Hashimoto, H.; Kai, Y.; Takagi, M.; Imanaka, T. Comparative analyses of the conformational stability of a hyperthermophilic protein and its mesophilic counterpart. Eur. J. Biochem., 2001, 268, 4144-4150.
99. Vieille, C.; Zeikus, G.J. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol. Mol. Biol. Rev., 2001, 65, 1-43.
100. Kumar, S.; Tsai, C.J.; Nussinov, R. Factors enhancing protein thermostability. Protein Eng., 2000, 13, 179-191.
101. Zhou, X.X.; Wang, Y.B.; Pan, Y.J.; Li, W.F. Differences in amino acids composition and coupling patterns between mesophilic and thermophilic proteins. Amino Acids, 2008, 34, 25-33.
102. Chelius, D.; Rehder, D.S.; Bondarenko, P.V. Identification and characterization of deamidation sites in the conserved regions of human immunoglobulin gamma antibodies. Anal. Chem., 2005, 77, 6004-6011.
103. Oshima, T. Unique polyamines produced by an extreme thermophile, Thermus thermophilus. Amino Acids, 2007, 33, 367-372.
104. Oshima, T. Thermine: a new polyamine from an extreme thermophile. Biochem. Biophys. Res. Commun., 1975, 63, 1093-1098.
105. Oshima, T. A new polyamine, thermospermine, 1,12-diamino-4,8-diazadodecane, from an extreme thermophile. J. Biol. Chem., 1979, 254, 8720-8722.