Isosteric replacement of sulfur with other chalcogens in peptides and proteins

Journal of Peptide Science

Volumn 11, Issue 4, 2005, Pages 187-214

  Moroder, Luis ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

Ligation; Methionine and cysteine; Methoxinine; Peptide synthesis; Protein expression; Selenium and tellurium analogues; Selenocysteine; Selenocystine; Selenomethionine; Structural and functional properties; Synthesis; Tellurocysteine; Tellurocystine; Telluromethionine

Indexed keywords

AMINO ACID; AMINO ACID DERIVATIVE; CHALCOGEN; CYSTEINE; CYSTEINE DERIVATIVE; CYSTINE; DISULFIDE; ENZYME; HEAVY METAL; METHIONINE; METHIONINE DERIVATIVE; MUTANT PROTEIN; NORLEUCINE; OXYGEN; PEPTIDE; PROTEIN; SELENIDE; SELENIUM; SELENIUM DERIVATIVE; SELENOCYSTEINE; SELENOCYSTINE; SELENOMETHIONINE; SERINE; SULFUR; TELLURIUM; TELLURIUM DERIVATIVE;

CATALYSIS; ENZYME MECHANISM; ENZYME SYNTHESIS; OXIDATION REDUCTION POTENTIAL; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; REVIEW; STEREOCHEMISTRY; X RAY CRYSTALLOGRAPHY;

CHALCOGENS; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; METHIONINE; MODELS, MOLECULAR; PEPTIDES; PROTEINS; SELENIUM; SERINE; SULFUR; TELLURIUM;

EID: 17444431205     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/psc.654     Document Type: Review

References (296)

1. Torchinsky YM. Sulfur in Proteins. Pergamon: Oxford, 1981; 1-277.
2. Giles NM, Watts AB, Giles GI, Fry FH, Littlechild JA, Jacob C. Metal and redox modulation of cysteine protein function. Chem. Biol. 2003; 10: 677-693.
3. Jacob C, Giles GI, Giles NM, Sies H. Sulfur and selenium: the role of oxidation state in protein structure and function. Angew. Chem. Int. Ed. 2003; 42: 4742-4758.
4. Jacob C, Holme AL, Fry FH. The sulfinic acid switch in proteins. Org. Biol. Chem. 2004; 2: 1951-1956.
5. Mugesh G, du Mont WW, Sies H. Chemistry of biologically important synthetic organoselenium compounds. Chem. Rev. 2001; 101: 2125-2179.
6. Stryer L. Biochemistry, 3rd edn. W. H. Freeman and Co: New York, USA, 1998.
7. Rose GD, Geselowitz AR, Lesser GJ, Lee RH, Zehfus MH. Hydrophobicity of amino acid residues in globular proteins. Science 1985; 229: 834-838.
8. Stadtman ER. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu. Rev. Biochem. 1993; 62: 797-821.
9. Brot N, Weissbach H. Biochemistry of methionine sulfoxide residues in proteins. Biofactors 1991; 3: 91-96.
10. Becker G, Musiol HJ. Houben-Weyl, Methods of Organic Chemistry, Synthesis of Peptides and Peptidomimetics (E 22a), Goodman M, Felix A, Moroder L, Toniolo C (eds). Georg Thieme Verlag: Stuttgart, 2002; 109-110.
11. Morley JS. Synthesis of human gastrin (I) and the biological properties of analogues. Peptides 1966, Beyermann H (ed.). North-Holland: Amsterdam, 1967; 226-234.
12. Kenner GW, Mendive JJ, Sheppard RC. Analogues of gastrin containing leucine in place of methionine. J. Chem. Soc. (C) 1968; 761-764.
13. Wünsch E, Jaeger E, Deffner M, Scharf R. Zur Synthese des [15-Leucin]Human-Gastrins I. III. Mitteilung: Zur Reindarstellung des synthetischen Heptadecapeptidamids. Hoppe Seyler's Z. Physiol. Chem. 1972; 353: 1716-1720.
14. Wünsch E, Wendlberger G, Hallet A, Jaeger E, Knof S, Moroder L, Scharf R, Schmidt I, Thamm P, Wilschowitz L. Zur Totalsynthese des Human-Big-Gastrins I und seines 32-Leucin-Analogons. Z. Naturforsch. 1977; 32c: 495-506.
15. Moroder L, Göhring W, Nyfeler R, Scharf R, Thamm P, Wendlberger G. Zur Synthese von Human-Little-Gastrin I und dessen Leucin-15-, Norleucin-25- und Methoxinin-15-Analoga. Hoppe Seyler's Z. Physiol. Chem. 1983; 364: 157-171.
16. 13]-S-peptide. J. Am. Chem. Soc. 1969; 91: 492-496.
17. Cowie DB, Cohen GN, Bolton ET, DeRobinchon-Szulmajster H. Amino acid analogue incorporation into bacterial proteins. Biochim. Biophys. Acta 1959; 34: 39-46.
18. Barker DG, Bruton CJ. The fate of norleucine as a replacement for methionine in protein synthesis. J. Mol. Biol. 1979; 133: 217-231.
19. Anfinsen CB, Corley LG. An active variant of staphylococcal nuclease containing norleucine in place of methionine. J. Biol. Chem. 1969; 244: 5149-5152.
20. Gilles AM, Marliére P, Rose T, Sarfati R, Longin R, Meier A, Fermandjian S, Monnot M, Cohen GN, Bàzu O. Conservative replacement of methionine by norleucine in Escherichia coli adenylate kinase. J. Biol. Chem. 1988; 263: 8204-8209.
21. Koide H, Yokoyama S, Kawai G, Ha JM, Oka T, Kawai S, Miyake T, Fuwa T, Miyazawa T. Biosynthesis of a protein containing a nonprotein amino acid by Escherichia coli: L-2-aminohexanoic acid at position 21 in human epidermal growth factor. Proc. Natl Acad. Sci. USA 1988; 85: 6237-6241.
22. Fersht AR, Dingwall C. An editing mechanism for the methionyl-tRNA synthetase in the selection of amino acids in protein synthesis. Biochemistry 1979; 18: 1250-1255.
23. Budisa N. Bioincorporation of Methionine Non-natural Amino Acid Analogues and Its Use for X-ray Crystallographic and Folding Studies of proteins. Dissertation, Technical University of Munich: Munich, 1999.
24. Budisa N, Steipe B, Demange P, Eckerskorn C, Kellermann S, Huber R. High-level biosynthetic substitution of methionine in proteins by its analogues 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli. Eur. J. Biochem. 1995; 230: 788-796.
25. Budisa N, Huber R, Golbik R, Minks C, Weyher E, Moroder L. Atomic mutations in annexin V. Thermodynamic studies of isomorphous protein variants. Eur. J. Biochem. 1998; 253: 1-9.
26. Roblin RO, Lampen JO, English JP, Cole QP, Vaughan Jr. Studies in chemotherapy. VIII. Methionine and purine antagonists and their relation to the sulfonamides. J. Am. Chem. Soc. 1945; 67 290-294.
27. Christensen JA. On the synthesis of methoxinine. Acta Chem. Scand. 1954; 8: 129.
28. Greven HM, Bruins AHNM, van der Vlugt FA. Peptides 1971, Nesvadba H (ed.). North-Holland: Amsterdam, 1973: 290-297.
29. Gillessen D, Trzeciak A, Müller RKM, Studer RO. Synthesis and biological activities of methoxinine-analogues of the C terminal octapeptide of cholecystokinin-pancreozymin. Int. J. Peptide Protein Res. 1979; 13: 130-136.
30. Wünsch E, Moroder L, Gillessen D, Soerensen UB, Bali JP. Biological and immunological properties of human gastrin-I analogues. Hoppe Seyler's Z. Physiol. Chem. 1982; 363: 665-669.
31. Harada T, Seto K, Murooka Y. O-Alkylhomoserine and methionine biosynthesis in Corynebacterium. J. Biochem. 1969; 65 493-496.
32. Besse D, Budisa N, Karnbrock W, Minks C, Musiol HJ, Pegoraro S, Siedler F, Weyher E, Moroder L. Chalcogen-analogues of amino acids. Their use in x-ray crystallographic and folding studies of peptides and proteins. Biol. Chem. 1997; 378: 211-218.
33. Clark LC, Combs GF, Turnbull BW, Slate EH, Chalker DK, Chow J, Davis LS, Glover PA, Graham GF, Gross EG, Krongrad A, Lesher JL, Park HK, Sanders BB, Smith CL, Taylor Jr. Effects of selenium supplementation for cancer prevention in patients with carcinoma of the skin - A randomized controlled trial. J. Am. Med. Assoc. 1996; 276: 1957-1963.
34. Chang JC, Gutenmann WH, Reid CM, Lisk DJ. Selenium content of Brazil nuts from two geographic locations in Brazil. Chemosphere 1995; 30: 801-802.
35. Wrobel K, Kannamkumarath SS, Wrobel K, Caruso JA. Hydrolysis of proteins with methanesulfonic acid for improved HPLC-ICP-MS determination of seleno-methionine in yeast and nuts. Anal. Bioanal. Chem. 2003; 375: 133-138.
36. Cowie DB, Cohen GN. Biosynthesis by Escherichia coli of active altered proteins containing selenium instead of sulfur. Biochim. Biophys. Acta 1957; 26: 252-261.
37. Munier R, Cohen GN. Incorporation of structural analogues of amino acids into bacterial proteins during their synthesis in vivo. Biochim. Biophys. Acta 1959; 31: 378-390.
38. Koch T, Buchardt O. Synthesis of L-(+)-selenomethionine. Synthesis 1993; 1065-1067.
39. Karnbrock W, Weyher E, Budisa N, Huber R, Moroder L. A new efficient synthesis of acetyltelluro- and acetylselenomethionine and their use in the biosynthesis of heavy-atom protein analogues. J. Am. Chem. Soc. 1996; 118: 913-914.
40. Perutz MF, Rossmann MG, Cullis AF, Muirhead H, Will G, North ACT. Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5 Å resolution, obtained by x-ray analysis. Nature 1960; 185: 416-422.
41. Hendrickson WA. Determination of macromolecular structures from anomalous diffraction of synchroton radiation. Science 1991; 254: 51-58.
42. Hendrickson WA, Horton J, LeMaster D. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD) - A vehicle for direct determination of 3-dimensional structure. EMBO J. 1990; 9: 1665-1672.
43. Budisa N, Minks C, Alefelder S, Wenger W, Dong F, Moroder L, Huber R. Toward the experimental codon reassignment in vivo. Protein building with an expanded amino acid repertoire. FASEB J. 1999; 13: 41-51.
44. Budisa N, Moroder L, Huber R. Structure and evolution of the genetic codes viewed from the perspective of the experimentally expanded amino acid repertoire in vivo. Cell. Mol. Life Sci. 1999: 55: 1626-1635.
45. Minks C, Alefelder S, Moroder L, Huber R, Budisa N. Towards new protein engineering: in vivo building and folding of protein shuttles for drug delivery and targeting by the selective pressure incorporation (SPI) method. Tetrahedron 2000; 56: 9431-9442.
46. Budisa N. Prolegomena to future efforts on genetic code engineering by expanding its amino acid repertoire. Angew. Chem. Int. Ed. 2004; 43: 6425-6463.
47. Smith JL, Thompson A. Reactivity of selenomethionine-dents in the magic bullet? Structure 1998; 6: 815-819.
48. Assmann A, Briviba K, Sies H. Reduction of methionine selenoxide to selenomethionine by glutathione. Arch. Biochem. Biophys. 1998; 349: 201-2003.
49. Sies H, Sharov VS, Klotz LO, Briviba K. Glutathione peroxidase protects against peroxynitrite-mediated oxidations: a new function for selenoproteins as peroxynitrite reductase. J. Biol. Chem. 1997; 272: 27 812-27 817.
50. Sharff AJ, Koronakis E, Luisi B, Koronaki V. Oxidation of selenomethionine: some MADness in the method! Acta Cryst. D. 2000; 56: 785-788.
51. Ali MA, Peisach E, Allen KN, Imperiali B. X-ray structure analysis of a designed oligomeric miniprotein reveals a discrete quaternary architecture. Proc. Natl Acad. Sci. USA 2004; 101: 12 183-12 188.
52. Klayman DL, Günther WHH. Organic Selenium Compounds: Their Chemistry and Biology. Wiley-Interscience: New York; 1973.
53. Padmaja S, Squadrito GL, Lemercier JN, Cueto R, Pryor WA. Peroxynitrite-mediated oxidation of D,L-selenomethionine: kinetics, mechanism and the role of carbon dioxide. Free Radic. Biol. Med. 1997; 23: 917-926.
54. Hubbard SJ, Argos P. Cavities and packing at protein interfaces. Protein Sci. 1994; 3: 2194-2206.
55. Gassner NC, Baase WA, Mooers BH, Busam RD, Weaver LH, Lindstrom JD, Quillin ML, Matthews BW. Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability. Biophys. Chem. 2003; 100: 325-340.
56. Gassner NC, Baase WA, Hausrath AC, Matthews BW. Substitution with selenomethionine can enhance the stability of methionine-rich proteins. J. Mol. Biol. 1999; 294: 17-20.
57. Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moraefi I. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 2000; 101: 199-210.
58. Roelfes G, Hilvert D. Incorporation of selenomethionine into proteins through selenohomocysteine-mediated ligation. Angew. Chem. Int. Ed. 2003; 42: 2275-2277.
59. Zhou ZS, Smith AE, Matthews RG. L-Selenohomocysteine: one-step synthesis from L-selenomethionine and kinetic analysis as substrate for methionine synthases. Bioorg. Med. Chem. Lett. 2000; 10: 2471-2475.
60. 77Se nuclear magnetic resonance spectroscopy. J. Biol. Chem. 1992; 267: 22 217-22 223.
61. Yuan T, Weljie AM, Vogel HJ. Tryptophan fluorescence quenching by methionine and selenomethionine residues of calmodulin: orientation of peptide and protein binding. Biochemistry 1998; 37: 3187-3195.
62. Siebum AHG, Woo WS, Raap J, Lugtenburg J. Access to any site-directed isotopomer of methionine, selenomethionine, cysteine and selenocysteine. Use of simple, efficient modular synthetic reaction schemes for isotope incorporation. Eur. J. Org. Chem. 2004; 2905-2913.
63. Ramadan SE, Razak AA, Ragab AM, El-Meleigy M. Incorporation of tellurium into amino acids and proteins in tellurium-tolerant fungi. Biol. Trace Element Res. 1989; 20: 225-232.
64. Boles JO, Lewinski K, Kunke M, Odom JD, Dunlap RB, Lebioda L, Hatada M. Bio-incorporation of telluromethionine into buried residues of dihydrofolate-reductase. Nature Struct. Biol. 1994; 1: 283-284.
65. Budisa N, Karnbrock W, Steinbacher S, Humm A, Prade L, Neuefeind T, Moroder L, Huber R. Bioincorporation of telluromethionine into proteins. A promising new approach for x-ray structure analysis of proteins. J. Mol. Biol. 1997; 270: 616-623.
66. Knapp FF. Telluroamino acids: synthesis of telluromethionine. J. Org. Chem. 1979; 44: 1007-1009.
67. Silks LA, Boles JO, Modi BP, Dunlap PB, Odom JD. An efficient synthesis of racemic and optically active telluromethionine. Synth. Commun. 1990; 20: 1555-1562.
68. Detty MR. Oxidation of selenides and tellurides with positive halogenating species. J. Org. Chem. 1980; 45: 274-279.
69. Kirsch G, Goodman MM, Knapp FF. Organotellurium compounds of biological interest: unique properties of the N-chlorosuccinimide oxidation product of 9-telluroheptadecanoic acid. Organometallics 1983; 2: 357-363.
70. Stadtman TC. Selenocysteine. Annu. Rev. Biochem. 1996; 65: 83-100.
71. Leinfelder W, Zehelein E, Mandrand-Berthelot MA, Böck A. Gene for a novel tRNA species that accepts L-serine and cotranslationally inserts selenocysteine. Nature 1988; 331: 723-725.
72. Commans S, Böck A. Selenocysteine inserting tRNAs: an overview. FEMS Microbiol. Rev. 1999; 23: 335-351.
73. Oas TG, Kim PS. A peptide model of a protein folding intermediate. Nature 1988; 336: 42-48.
74. Staley JP, Kim PS. Role of a subdomain in the folding of bovine pancreatic trypsin inhibitor. Nature 1990; 344: 685-688.
75. Staley JP, Kim PS. Complete folding of bovine pancreatic trypsin inhibitor with only a single disulfide bond. Proc. Natl Acad. Sci. USA 1992; 89: 1519-1523.
76. 1H nuclear magnetic resonance study. J. Mol. Biol. 1991; 222: 353-371.
77. 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 1991; 222: 373-390.
78. 1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 1994; 235: 1044-1061.
79. Cattani-Scholz A, Renner C, Cabrele C, Behrendt R, Oesterhelt D, Moroder L. Photoresponsive cyclic bis(cysteinyl)peptides as catalysts of oxidative protein folding. Angew. Chem. Int. Ed. 2002; 41: 289-292.
80. Renner C, Behrendt R, Heim N, Moroder L. Photomodulation of conformational states. III. Water-soluble bis-cysteinyl-peptides with (4-aminomethyl)phenylazobenzoic acid as backbone constituent. Biopolymers 2002; 63: 382-393.
81. Holmgren A. Antioxidant function of thioredoxin and glutaredoxin systems. Antioxid. Redox. Signal. 2000; 2: 811-820.
82. Martin JL. Thioredoxin: a fold for all reasons. Structure 1995; 3: 245-250.
83. Ritz D, Beckwith J. Roles of thiol-redox pathways in bacteria. Annu. Rev. Microbiol. 2001; 55: 21-48.
84. Chivers PT, Laboissiere MC, Raines RT. The CXXC motif. imperatives for the formation of native disulfide bonds in the cell. EMBO J. 1996; 15: 2659-2667.
85. Chivers PT, Prehoda KE, Raines RT. The CXXC motif: a rheostat in the active site. Biochemistry 1997; 36: 4061-4066.
86. Lees WJ, Whitesides GM. Equilibrium constants for thiol-disulfide interchange reactions: a coherent, corrected set. J. Org. Chem. 1993; 58: 642-647.
87. Akerboom TP, Bilzer M, Sies H. The relationship of biliary glutathione disulfide efflux and intracellular glutathione disulfide content in perfused rat liver. J. Biol. Chem. 1982; 257: 4248-4252.
88. Meister A, Anderson ME. Glutathione. Annu. Rev. Biochem. 1983; 52: 711-760.
89. Goldberger RF, Epstein CJ, Anfinsen CB. Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver. J. Biol. Chem. 1963; 238: 628-635.
90. Freedman PB. Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins. Cell 1989; 57 1069-1072.
91. Bardwell JC, McGovern K, Beckwith J. Identification of a protein required for disulfide bond formation in vivo. Cell 1991; 67: 581-589.
92. Bardwell JC, Lee JO, Jander G, Martin N, Belin D, Beckwith J. A pathway for disulfide bond formation in vivo. Proc. Natl Acad. Sci. USA 1993; 90: 1038-1042.
93. Frand AR, Kaiser CA. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol. Cell 1999; 4: 469-477.
94. Tu BP, Ho-Schleyer S, Travers KJ, Weissman JS. Biochemical basis of oxidative folding in endoplasmic reticulum. Science 2000; 290: 1571-1574.
95. Rost J, Rapoport S. Reduction-potential of glutathione. Nature 1964; 201: 185.
96. Millis KK, Weaver KH, Rabenstein DL. Oxidation/reduction potential of glutathione. J. Org. Chem. 1993; 58: 4144-4146.
97. Åslund F, Berndt KD, Holmgren A. Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria. J. Biol. Chem. 1997; 272: 30 780-30 786.
98. Siedler F, Rudolph-Böhner S, Doi M, Musiol HJ, Moroder L. Redox potentials of active-site bis(cysteinyl)fragments of thiol-protein oxidoreductases. Biochemistry 1993; 32: 7488-7495.
99. Cabrele C, Fiori S, Pegoraro S, Moroder L. Redox-active bis(cysteinyl)peptides as catalysts for in vitro oxidative protein folding. Chem. Biol. 2002; 9: 731-740.
100. Lin TY, Kim PS. Urea dependence of thiol-disulfide equilibria in thioredoxin: confirmation of the linkage relationship and a sensitive assay for structure. Biochemistry 1989; 28: 5282-5287.
101. Hawkins HC, de Nardi M, Freedman RB. Redox properties and cross-linking of the dithiol/disulphide active sites of mammalian protein disulphide-isomerase. Biochem. J. 1991; 275: 341-348.
102. Darby NJ, Creighton TE. Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase. Biochemistry 1995; 34: 16 770-16 780.
103. O'Donnell ME, Williams CH, Jr. Proton stoichiometry in the reduction of the FAD and disulfide of Escherichia coli thioredoxin reductase. Evidence for a base at the active site. J. Biol. Chem. 1983; 258: 13 795-13 805.
104. Huber-Wunderlich M, Glockshuber R. A single dipeptide sequence modulates the redox properties of a whole enzyme family. Fold. Des. 1998; 3: 161-171.
105. Krause G, Lundstrom J, Barea JL, Pueyo de la Cuesta C, Holmgren A. Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin, J. Biol. Chem. 1991; 266: 9494-9500.
106. Kortemme T, Darby NJ, Creighton TE. Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase. Biochemistry 1996; 35: 14 503-14 511.
107. Yang YF, Wells WW. Identification and characterization of the functional amino acids at the active center of pig liver thioltransferase by site-directed mutagenesis. J. Biol. Chem. 1991; 266: 12 759-12 765.
108. Grauschopf U, Winther JR, Korber P, Zander T, Dallinger P, Bardwell JC. Why is DsbA such an oxidizing disulfide catalyst? Cell 1995; 83: 947-955.
109. Cabrele C, Fiori S, Pegoraro S, Moroder L. In Peptides: The Wave of the Future, Lebl M, Houghton RA (eds). Kluwer Academic Publishers: Dordrecht, 2001; 462-463.
110. Mössner E, Wunderlich-Huber M, Glockshuber R. Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases. Protein Sci. 1998; 7: 1233-1244.
111. a values in proteins of the thioredoxin family. J. Mol. Biol. 1995; 253: 799-812.
112. Otto HH, Schirmeister T. Cysteine proteases and their inhibitors. Chem. Rev. 1997; 97: 133-171.
113. Woo RA, Chae HZ, Hwang SC, Yang KS, Kang SW, Kim K, Rhee SG. Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation. Science 2003; 300: 653-656.
114. Schröder E, Littlechil JA, Lebedev AA, Errington N, Vagin AA, Isupov MN. Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 Å resolution. Structure 2000; 8: 605-615.
115. Ji Y, Bennett BM. Activation of microsomal glutathione S transferase by peroxynitrite. Mol. Pharmacol. 2003; 63: 136-146.
116. Biteau B, Labarre J, Toledano MB. ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 2003; 425: 980-984.
117. Klaassen CD, Boles JW. Sulfation and sulfotransferases 5: the importance of 3′-phosphoadenosine 5′-phosphosulfate (PAPS) in the regulation of sulfation. FASEB J. 1997; 11: 404-418.
118. Hille A, Braulke T, von Figura K, Huttner WB. Occurrence of tyrosine sulfate in proteins - A balance-sheet. 1. Secretory and lysosomal proteins. Eur. J. Biochem. 1990; 188: 577-586.
119. Kimura T. Houben-Weyl, Methods of organic Chemistry, Synthesis of Pepitdes and Peptidomimetics (E 22b), Goodman M, Felix A, Moroder L, Toniolo C (eds). Georg Thieme Verlag: Stuttgart, 2002; 142-161.
120. Xu Y, Wilcox DE. Oxidation of zinc finger cysteines to thiolsulfinate. J. Am. Chem. Soc. 1998; 120: 7375-7376.
121. Musiol HJ, Loidl G, Moroder L. Houben-Weyl, Methods of Organic Chemistry, Synthesis of Peptides and Peptidomimetics (E 22b), Goodman M, Felix A, Moroder L, Toniolo C (eds). Georg Thieme Verlag: Stuttgart, 2002; 179-183.
122. Sahl HG, Bierbaum G. Lantibiotics: biosynthesis and biological activities of uniquely modified peptides from gram-positive bacteria. Annu. Rev. Microbiol. 1998; 52: 41-79.
123. Süssmuth RD, Jack RW, Jung G. Houben-Weyl, Methods of Organic Chemistry, Synthesis of Peptides and Peptidomimetics (E 22b), Goodman M, Felix A, Moroder L, Toniolo C (eds). Georg Thieme Verlag: Stuttgart, 2002; 184-213.
124. Fusetani N, Matsunaga S. Bioactive sponge peptides. Chem. Rev. 1993; 93: 1793-1806.
125. Gilon C, Mang C, Lohof E, Friedler A, Kessler H. Houben-Weyl, Methods of Organic Chemistry, Synthesis of Peptides and Peptidomimetics (E 22b), Goodman M, Felix A, Moroder L, Toniolo C (eds). Georg Thieme Verlag: Stuttgart, 2002; 521-524.
126. Moroder L, Musiol HJ, Schaschke N, Chen L, Hargittai B, Barany G. Houben-Weyl, Methods of organic Chemistry, Synthesis of Peptides and Peptidomimetics (E 22a), Goodman M, Felix A, Moroder L, Toniolo C (eds). Georg Thieme Verlag: Stuttgart, 2002; 384-423.
127. Akaji K, Kiso Y. Houben-Weyl, Methods of Organic Chemistry, Synthesis of Peptides and Peptidomimetics (E 22b), Goodman M, Felix A, Moroder L, Toniolo C (eds). Georg Thieme Verlag: Stuttgart, 2002; 101-141.
128. Babine PE, Bender SL. Molecular recognition of protein-ligand complexes: applications to drug design. Chem. Rev. 1997; 97: 1359-1472.
129. Polgar L, Bender ML. A new enzyme containing a synthetically formed active site. Thiol-subtilisin. J. Am. Chem. Soc. 1966; 88 3153-3154.
130. Neet KE, Koshland DE. Conversion of serine at the active site of subtilisin to cysteine - A chemical mutation. Proc. Natl Acad. Sci. USA 1966; 50: 1606-1611.
131. Nakatsuka T, Sasaki T, Kaiser ET. Peptide segment coupling catalyzed by the semisynthetic enzyme thiolsubtilisin. J. Am. Chem. Soc. 1987; 109: 3808-3810.
132. Abrahmsen L, Tom J, Burnier J, Butcher KA, Kossiakoff A, Wells JA. Engineering subtilisin and its substrates for efficient ligation of peptide-bonds in aqueous solution. Biochemistry 1991; 30: 4151-4159.
133. Chang TK, Jackson DY, Burnier JP, Wells JA. Subtiligase: a tool for semisynthesis of proteins. Proc. Natl Acad. Sci. USA 1994; 91: 12 544-12 548.
134. Jackson DY, Burnier J, Quan C, Stanley M, Tom J, Wells JA. A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues. Science 1994; 266: 243-247.
135. Perler FB, Davis EO, Dean GE, Gimble FS, Jack WE, Neff N, Noren CJ, Thorner J, Belfort M. Protein splicing elements - inteins and exteins - a definition of terms and recommended nomenclature. Nucleic Acids Res. 1994; 22: 1125-1127.
136. Chong S, Shao Y, Paulus H, Brenner J, Perler FB, Xu MQ. Protein splicing involving the Saccharomyces cerevisiae VMA intein: the steps in the splicing pathway, side reactions leading to protein cleavage, and establishment of an in vitro splicing system. J. Biol. Chem. 1996; 271: 22 159-22 168.
137. Brannigan JA, Dodson G, Duggleby HJ, Moody PCE, Smith JL, Tomchick DR, Murzin AG. A protein catalytic framework with an N terminal nucleophile is capable of self-activation. Nature 1995; 378: 416-419.
138. van Poelje PD, Snell EE. Pyruvoyl-dependent enzymes. Annu. Rev. Biochem. 1990; 59: 29-59.
139. Lee JJ, Ekker SC, von Kessler DP, Porter JA, Sun BI, Beachy PA. Autoproteolysis in hedgehog protein biosynthesis. Science 1994; 266: 1528-1537.
140. Porter JA, von Kessler DP, Ekker SC, Young KE, Lee JJ, Moses K, Beachy PA. The product of hedgehog autoproteolytic cleavage active in local and long-range signalling. Nature 1995; 374: 363-366.
141. Li YM, Milne JC, Madison LL, Kolter R, Walsh CT. From peptide precursor to oxazole and thiazole containing peptide antibiotics: microcin B17 synthase. Science 1996; 274: 1188-1193.
142. Perler FB. Protein splicing of inteins and hedgehog autoproteolysis: structure, function, and evolution. Cell 1998; 92: 1-4.
143. Perler FB, Xu MQ, Paulus H. Protein splicing and autoproteolysis mechanisms. Curr. Opin. Chem. Biol. 1997; 1: 292-299.
144. Gogarten JP, Senejani AG, Zhaxybayeva O, Olendzenski L, Hilario E. Inteins: structure, function, and evolution. Annu. Rev. Microbiol. 2002; 56: 263-287.
145. Kawasaki M, Nogami S, Satow Y, Ohya Y, Anraku Y. Identification of three core regions essential for protein splicing of the yeast Vma1 protozyme. A random mutagenesis study of the entire VMA1-derived endonuclease sequence. J. Biol. Chem. 1997; 272: 15 668-15 674.
146. Xu MQ, Perler FB. Identification of three core regions essential for protein splicing of the yeast Vma1 protozyme - A random mutagenesis study of the entire Vma 1-derived endonuclease sequence. EMBO J. 1996; 15: 5146-5153.
147. Bodanszky M, Martinez J. The Peptides: Analysis, Synthesis, Biology, Gross E, Meienhofer J (eds). Academic Press: New York, 1983; 111-218.
148. Geiger T, Clarke S. Deamidation, isomerization and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation. J. Biol. Chem. 1987; 262: 785-794.
149. Blodgett JK, Loudon GM, Collins KD. Specific cleavage of peptides containing an aspartic acid (β-hydroxamic acid) residue. J. Am. Chem. Soc. 1985; 107: 4305-4313.
150. Piszkiewicz D, Landon M, Smith EL. Anomalous cleavage of aspartyl-proline peptide bonds during amino acid sequence determinations. Biochem. Biophys. Res. Commun. 1970; 40: 1173-1178.
151. Wieland T, Bokelmann E, Bauer L, Lang HU, Lau H. Über Peptidsynthesen. 8. Bildung von S-haltigen Peptiden durch intramolekulare Wanderung von Aminoacylresten. Liebigs Ann. Chem. 1953; 583: 129-149.
152. Brenner M, Zimmermann JP, Wehrmüller J, Quitt P, Hardtmann A, Schneider W, Beglinger U. Aminoacyl-Einlagerung. 1. Mitteilung. Definition, Übersicht und Beziehung zur Peptidsynthese. Helv. Chim. Acta 1957; 40: 1497-1517.
153. Brenner M, Zimmermann JP, Wehrmüller J, Quitt P, Photaski I. Eine neue Umlagerungsreaktion und ein neues Prinzip zum Aufbau von Peptidketten. Experientia 1955; 11: 397-399.
154. Kemp DS, Leung SL, Kerkman DJ. Models that demonstrate peptide-bond formation by prior thiol capture. 1. Capture by disulfide formation. Tetrahedron Lett. 1981; 22: 181-184.
155. Dawson PE, Muir TW, Clarke-Lewis I, Kent SBH. Synthesis of proteins by native chemical ligation. Science 1994; 266: 776-779.
156. Tam JP, Lu YA, Liu CF, Shao J. Peptide synthesis using unprotected peptides through orthogonal coupling methods. Proc. Natl Acad. Sci. USA 1995; 92: 12485-12489.
157. Yamashiro D, Blake J. Use of thiol acids in peptide segment coupling in non-aqueous solvents. J. Pept. Prot. Res. 1981; 18 383-392.
158. Hwang PTR, Hancoock CK. Study of the alkaline hydrolysis and nuclear magnetic resonance spectra of some thiol esters. J. Am. Chem. Soc. 1973; 38: 4239-4243.
159. Marahiel MA, Stachelhaus T, Mootz HD. Modular peptide synthetases involved in nonribosomal peptide synthesis. Chem. Rev. 1997; 97: 2651-2673.
160. von Döhren H, Keller U, Vater J, Zocher R. Multifunctional peptide synthetases. Chem. Rev. 1997; 97: 2675-2705.
161. Bang D, Kent SBH. A one-pot total synthesis of crambin. Angew. Chem. Int. Ed. 2004; 43: 2534-2538.
162. Dawson P. Houben-Weyl, Methods of Organic Chemistry, Synthesis of Peptides and Peptidomimetics (E 22a), Goodman M, Felix A, Moroder L, Toniolo C (eds). Georg Thieme Verlag: Stuttgart, 2002; 627-641.
163. Dawson PE, Kent SBH. Synthesis of native proteins by chemical ligation. Annu. Rev. Biochem. 2000; 69: 923-960.
164. Coltart DM. Peptide segment coupling by prior ligation and proximity-induced intramolecular acyl transfer. Tetrahedron 2000; 56: 3449-3491.
165. Tam JP, Xu JX, Eom KD. Methods and strategies of peptide ligation. Biopolymers 2001: 60: 194-205.
166. Casi G, Hilvert D. Convergent protein synthesis. Curr. Opin. Struct. Biol. 2003; 13: 589-594.
167. Canne LE, Bark SJ, Kent SBH. Extending the applicability of native chemical ligation. J. Am. Chem. Soc. 1996; 118: 5891-5896.
168. α-2-Mercaptobenzylamine-assisted chemical ligation. Org. Lett. 2000; 2: 23-26.
169. Offer J, Boddy CNC, Dawson PE. Extending synthetic access to proteins with a removable acyl transfer auxiliary. J. Am. Chem. Soc. 2002; 124: 4642-4646.
170. Evans TC, Brenner J, Xu MQ. Semisynthesis of cytotoxic proteins using a modified protein splicing element. Protein Sci. 1998; 7: 2256-2264.
171. Muir TW, Sondhi D, Cole PA. Expressed protein ligation: a general method for protein engineering. Proc. Natl Acad. Sci. USA 1998; 95: 6705-6710.
172. Evans TC Jr, Xu MQ, Intein-mediated protein ligation: harnessing nature's escape artists. Biopolymers 1999; 51: 333-342.
173. Muir TW. Semisynthesis of proteins by expressed protein ligation. Annu. Rev. Biochem. 2003; 72: 249-289.
174. David R, Richter MPO, Beek-Sickinger AG. Expressed protein ligation - Method and applications. Eur. J. Biochem. 2004; 271 663-677.
175. Creighton TE. Disulfide bonds and protein stability. BioEssays 1988; 8: 57-63.
176. Anfinsen CB, Haber E, Sela M, White FH. Kinetics of formation of native ribonuclease during oxidation of reduced polypeptide chain. Proc. Natl Acad. Sci. USA 1961; 47: 1309-1314.
177. Anfinsen CB. Principles that govern the folding of protein chains. Science 1973; 181: 223-230.
178. Gething MJ, Sambrook J. Protein folding in the cell. Nature 1992; 355: 33-45.
179. Hartl FU. Molecular chaperones in cellular protein folding. Nature 1996; 381: 571-580.
180. Freedman PB, Hirst TR, Tuite MF. Protein disulfide-isomerase - Building bridges in protein folding. Trends Biochem. Sci. 1994; 19: 331-336.
181. Schmid FX. Protein folding: prolyl isomerases join the fold. Curr. Biol. 1995; 5: 993-994.
182. Hwang C, Sinskey AJ, Lodish HF. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 1992; 257: 1496-1502.
183. Tu BP, Weissman JS. Oxidative protein folding in eukaryotes: mechanisms and consequences. J. Cell Biol. 2004; 164: 341-346.
184. Wetlaufer DB, Saxena VP. Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme. Biochemistry 1970; 9: 5015-5023.
185. Creighton TE. Protein folding coupled to disulphide bond formation. Biol. Chem. 1997; 378: 731-744.
186. Rumbley J, Hoang L, Mayne L, Englander SW. An amino acid code for protein folding. Proc. Natl Acad. Sci. USA 2001; 98: 105-112.
187. Lazaridis TZ, Karplus M. 'New view' of protein folding reconciled with the old through multiple unfolding simulations. Science 1997; 278: 1928-1931.
188. Onuchic JN, Luthey-Schulten Z, Wolynes PG. Theory of protein folding: the energy landscape perspective. Annu. Rev. Phys. Chem. 1997; 48: 545-600.
189. Huyghues-Despointes BM, Nelson JW. Stabilities of disulfide bond intermediates in the folding of apamin. Biochemistry 1992; 31: 1476-1483.
190. Chau MH, Nelson JW. Cooperative disulfide bond formation in apamin. Biochemistry 1992; 31: 4445-4450.
191. Zimmerman SS, Scheraga HA. Local interactions in bends of proteins. Proc. Natl Acad. Sci. USA 1977; 74: 4126-4129.
192. Creighton TE. An empirical approach to protein conformation stability and flexibility. Biopolymers 1983; 22: 49-58.
193. Creighton TE. Disulphide bonds as probes of protein folding pathways. Methods Enzymol. 1986; 131: 83-106.
194. Zhang RM, Snyder GH. Dependence of formation of small disulfide loops in two-cysteine peptides on the number and types of intervening amino acids. J. Biol. Chem. 1989; 264: 18 472-18 479.
195. Wedemeyer WJ, Xu X, Welker E, Scheraga HA. Conformational propensities of protein folding intermediates: distribution of species in the 1S, 2S, and 3S ensembles of the [C40A,C95A] mutant of bovine pancreatic ribonuclease A. Biochemistry 2002; 41: 1483-1491.
196. Thornton JM. Disulfide bridges in globular proteins. J. Mol. Biol. 1981; 151: 261-287.
197. Dobson CM, Sali A, Karplus M. Protein folding: a perspective from theory and experiment. Angew. Chem. Int. Ed. Engl. 1998; 37 868-893.
198. Capaldi AP, Kleanthous C, Radford SE. Im7 folding mechanism: misfolding on a path to the native state. Nat. Stract. Biol. 2002; 9: 209-216.
199. Hunter HN, Fulton DB, Ganz T, Vogel HJ. The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis. J. Biol. Chem. 2002; 277: 37 597-37 603.
200. Wang XH, Connor M, Smith R, Maciejewski MW, Howden MEH, Nicholson GM, Christie MJ, King GF. Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge. Nat. Struct. Biol. 2000; 7: 505-513.
201. Capasso S, Mattia C, Mazarella L, Puliti R. Structure of a cispeptide unit: molecular conformation of the cyclic disulphide L-cysteinyl-L-cysteine. Acta Crystallogr. 1977; B33: 2080-2083.
202. Čemažar M, Zahariev S, Lopez JJ, Carugo O, Jones JA, Hore PJ, Pongor S. Oxidative folding intermediates with nonnative disulfide bridges between adjacent cysteine residues. Proc. Natl Acad. Sci. USA 2003; 100: 5754-5759.
203. Rudolph R, Böhm G, Lilie H, Jaenicke R. Protein Function: A Practical Approach, Creighton TE (ed.). IRL Press/Oxford University Press: Oxford, 1997; 57-99.
204. Daugherty DL, Rozema D, Hanson PE, Gellman SH. Artificial chaperone-assisted refolding of citrate synthase. J. Biol. Chem. 1998; 273: 33961-33971.
205. Rattenholl A, Ruoppolo M, Flagiello A, Monti M, Vinci F, Marino G, Lilie H, Schwarz E, Rudolph R. Prosequence assisted folding and disulfide bond formation of human nerve growth factor. J. Mol. Biol. 2001; 305: 523-533.
206. Weissman JS, Kim PS. The pro-region of BPTI facilitates folding. Cell 1992; 711: 841-851.
207. Moroder L, Besse D, Musiol HJ, Rudolph-Böhner S, Siedler F. Oxidative folding of cystine-rich peptides vs regioselective cysteine pairing strategies. Biopolymers 1996; 40: 207-234.
208. Dimarcq JL, Bulet P, Hetru C, Hoffmann J. Cysteine-rich antimicrobial peptides in invertebrates. Biopolymers 1998; 47 465-477.
209. García-Olmedo F, Molina A, Alamillo JM, Rodríguez-Palenzuéla P. Plant defense peptides. Biopolymers 1998; 47: 479-491.
210. Terlau H, Olivera BM. Conus venoms: a rich source of novel ion channel-targeted peptides. Physiol. Rev. 2004; 84: 41-68.
211. Loughnan ML, Alewood PF. Physico-chemical characterization and synthesis of neuronally active α-conotoxins. Eur. J. Biochem. 2004; 271: 2294-2304.
212. Tamaoki H, Miura R, Kusunoki M, Kyogoku Y, Kobayashi Y, Moroder L. Folding motifs induced and stabilized by distinct cystine frameworks. Protein Eng. 1998; 11: 649-659.
213. Cornet B, Bonmatin JM, Hetru C, Hoffmann JA, Ptak M, Vovelle F. Refined 3-dimensional solution structure of insect defensin-A. Structure 1995; 3: 435-448.
214. Narasimhan L, Singh J, Humblet C, Guruprasad K, Blundell T. Snail and spider toxins share a similar tertiary structure and 'cystine motif'. Nat. Struct. Biol. 1994; 1: 850-852.
215. Carugo O, Lu SY, Luo JC, Gu XC, Liang SP, Strobl S, Pongor S. Structural analysis of free and enzyme-bound amaranth alpha-amylase inhibitor: classification within the knottin fold superfamily and analysis of its functional flexibility. Protein Eng. 2001; 14 639-646.
216. Tang YQ, Yuan J, Ösapay G, Ösapay K, Tran D, Miller CJ, Quellette AJ, Selsted ME. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated α-defensins. Science 1999; 286: 498-502.
217. Trabi M, Schirra HJ, Craik DJ. Three-dimensional structure of RTD-1, a cyclic antimicrobial defensin from rhesus macaque leukocytes. Biochemistry 2001; 40: 4211-4221.
218. Altamirano MM, Golbik R, Zahn R, Buckle AM, Fersht AR. Refolding chromatography with immobilized mini-chaperones. Proc. Natl Acad. Sci. USA 1997; 94: 3576-3578.
219. Karadimitris A, Gadola S, Altamirano M, Brown D, Woolfson A, Klenerman P, Chen JL, Koezuka Y, Roberts IAG, Price DA, Dusheiko G, Milstein C, Fersht A, Luzzatto L, Cerundolo V. Human CD1d-glycolipid tetramers generated by in vitro oxidative refolding chromatography. Proc. Natl Acad. Sci. USA 2001; 98: 3294-3298.
220. Woycechowsky KJ, Hook BA, Raines RT. Catalysis of protein folding by an immobilized small-molecule dithiol. Biotechnol. Prog. 2003; 19: 1307-1314.
221. Annis I, Chen L, Barany G. Novel solid-phase reagents for facile formation of intramolecular disulfide bridges in peptides under mild conditions. J. Am. Chem. Soc. 1998; 120: 7226-7238.
222. Woycechowsky KJ, Wittrup KD, Raines RT. A small-molecule catalyst of protein folding in vitro and in vivo. Chem. Biol. 1999; 6: 871-879.
223. Lyles MM, Gilbert HF. Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer. Biochemistry 1991; 30: 613-619.
224. Gilbert HF. Protein disulfide isomerase and assisted protein folding. J. Biol. Chem. 1997; 272: 29399-29402.
225. Bergmann M, Brand ME, Weinmann F. Umlagerungen peptidähnlicher Stoffe. Hoppe Seyler's Z. Physiol. Chem. 1923; 131: 1-17.
226. Sakakibara S, Shin KH, Hess GP. An approach to specific cleavage of peptide bonds. 1. Acyl migration in dipeptides containing hydroxyamino acids in anhydrous hydrogen fluoride. J. Am. Chem. Soc. 1962; 84: 4921-4928.
227. Reissmann S, Steinmetzer T, Greiner G, Seyfart L, Besser D, Schumann C. Houben-Weyl, Methods of Organic Chemistry, Synthesis of Peptides and Peptidomimetics (E 22a), Goodman M, Felix A, Moroder L, Toniolo C (eds). Georg Thieme Verlag: Stuttgart, 2002; 347-378.
228. Merrifield RB, Vizioli LD, Boman HG. Synthesis of the antibacterial peptide cecropin-A(1-33). Biochemistry 1982; 21 5020-5031.
229. Fujino M, Wakimasu M, Shinagawa S, Kitada C, Yajima H. Synthesis of nonacosapeptide corresponding to mammalian glucagon. Chem. Pharm. Bull. 1978; 26: 539-548.
230. Kent SB, Michell AR, Engelhard M, Merrifield PB. Mechanisms and prevention of trifluoroacetylation in solid-phase peptide synthesis. Proc. Natl Acad. Sci. USA 1979; 76: 2180-2184.
231. Quibell M, Turnell WG, Johnson T. Synthesis of azapeptides by the Fmoc tert-butyl polyamide technique. J. Chem. Soc. Perkin Trans. I 1993; 2843-2849.
232. Hübener G, Göhring W, Musiol HJ, Moroder L. N α-Trifluoroacetylation of N-terminal hydroxyamino acids: a new side reaction in peptide synthesis. Pept. Res. 1992; 5: 287-292.
233. Kemp DS. The amine capture strategy for peptide-bond formation - An outline of progress. Biopolymers 1981; 20: 1793-1804.
234. Johnson T, Quibell M, Sheppard RC. N, O-bisFmoc derivatives of N-(2-hydroxy-4-metboxybenzyl)-amino acids: useful intermediates in peptide synthesis. J. Pept. Sci. 1995; 1: 11-25.
235. Thamm P, Kolbeck W, Musiol HJ, Moroder L. Houben-Weyl, Methods of Organic Chemistry, Synthesis of Peptides and Peptidomimetics (E 22a), Goodman M, Felix A, Moroder L, Toniolo C (eds). Georg Thieme Verlag: Stuttgart, 2002; 260-275.
236. Hurley TR, Colson CE, Hicks G, Ryan MJ. Orally active watersoluble N,O-acyl transfer products of a β,γ-bishydroxyl amide containing renin inhibitor. J. Med. Chem. 1993; 36: 1496-1498.
237. Hamada Y, Matsumoto H, Yamaguchi T, Kimura T, Hayashi Y, Kiso Y. Water-soluble prodrugs of dipeptide HIV protease inhibitors based on o → N intramolecular acyl migration: design, synthesis and kinetic study. Bioorg. Med. Chem. 2004; 12: 159-170.
238. Horikawa M, Shigeri Y, Yumoto N, Yoshikawa S, Nakajima T, Ohfune Y. Synthesis of potent Leu-enkephalin analogues possessing β-hydroxy-α,α-disubstituted α-amino acid and their characterization to opioid receptors. Bioorg. Med. Chem. Lett. 1998; 8: 2027-2032.
239. Sohma Y, Sasaki M, Hayashi Y, Kimura T, Kiso Y. Novel and efficient synthesis of difficult sequence-containing peptides through O → N intramolecular acyl migration reaction of O-acyl isopeptides. Chem. Commun. 2004; 124-125.
240. Sohma Y, Sasaki M, Hayashi Y, Kimura T, Kiso Y. Design and synthesis of a novel water-soluble Aβ1-42 isopeptide: an efficient strategy for the preparation of Alzheimer's disease-related peptide, Aβ1-42, via O-N intramolecular acyl migration reaction. Tetrahedron Lett. 2004; 45: 5965-5968.
241. Carpino LA, Krause E, Sferdan CD, Schümann M, Fabian H, Bienert M, Beyermann M. Synthesis of 'difficult' peptide sequences: application of a depsipeptide technique to the Jung-Redemann 10- and 26-mers and the amyloid peptide Aβ(1-42). Tetrahedron Lett. 2004; 45: 7519-7523.
242. Mutter M. Chandravarkar A, Boyat C, Lopez J, Dos Santos S, Mandal B, Mimna R, Murat K, Patiny L, Saucede L, Tuchscherer G. Switch peptides in statu nascendi: induction of conformational transitions relevant to degenerative diseases. Angew. Chem. Int. Ed. 2004; 43: 4172-4178.
243. Kryukov GV, Castellano S, Novoselov SV, Lobanov V, Zehtab O, Guigá R, Gladyshev VN. Characterization of mammalian selenoproteomes. Science 2003; 300: 1439-1443.
244. Köhrle J, Brigelius-Flohé R, Böck A, Gartner R, Meyer O, Flohé L. Selenium in biology: facts and medical perspectives. Biol. Chem. 2000; 381: 849-864.
245. Hatfield DL, Gladyshev VN. How selenium has altered our understanding of the genetic code. Mol. Cell. Biol. 2002; 22: 3565-3576.
246. Huber RE, Criddle RS. Comparison of chemical properties of selenocysteine and selenocystine with their sulfur analogues. Arch. Biochem. Biophys. 1967; 122: 164-173.
247. Arnold AP, Tan KS, Rabenstein DL. Nuclear-magnetic-resonance studies of the solution chemistry of metal complexes. 23. Complexation of methylmercury by selenohydryl-containing amino-acids and related molecules. Inorg. Chem. 1986; 25: 2433-2437.
248. Köhrle J. Local activation and inactivation of thyroid hormones: the deiodinase family. Mol. Cell. Endocrinol.1999; 151 103-119.
249. Szajewski RP, Whitesides GM. Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione. J. Am. Chem. Soc. 1980; 102: 2011-2026.
250. Singh R, Whitesides GM. Selenols catalyze the interchange reactions of dithiols and disulfides in water. J. Org. Chem. 1991; 56: 6931-6933.
251. Besse D, Moroder L. Synthesis of selenocysteine-peptides and their oxidation to diselenide-bridged compounds. J. Pept. Sci. 1997; 3: 442-453.
252. Besse D, Siedler F, Diercks T, Kessler H, Moroder L. The redox potential of selenocystine in unconstrained cyclic peptides. Angew. Chem. Int. Ed. Engl. 1997; 36: 883-885.
253. Tanaka H, Soda K. Selenocysteine. Methods Enzymol. 1987; 143: 240-243.
254. 77Se-]selenocystine and L-tellurocystine. J. Chem. Soc. Perkin Trans. I. 1997; 2443-2447.
255. Gieselman MD, Xie L, van der Donk WA. Synthesis of a selenocysteine-containing peptide by native chemical ligation. Org. Lett. 2001; 3: 1331-1334.
256. Tamura T, Oikawa T, Ohtaka A, Fujii N, Esaki N, Soda K. Synthesis and characterization of the selenium analogue of glutathione disulfide. Anal. Blochem. 1993; 208: 151-154.
257. Koide T, Itoh H, Otaka A, Yasui H, Kuroda M, Esaki N, Soda K, Fujii N. Synthetic study on selenocystine-containing peptides. Chem. Pharm. Bull. 1993; 41: 502-506.
258. Oikawa T, Esaki N, Tanaka H, Soda K. Metalloselenonein, the selenium analogue of metallothionein: synthesis and characterization of its complex with copper ions. Proc. Natl Acad. Sci. USA 1991; 88 3057-3059.
259. Chocat P, Esaki N, Tanaka H, Soda K. Synthesis of L-selenodjenkolate and its degradation with methionine γ-lyase. Anal. Biochem. 1985; 148: 485-489.
260. Pegoraro S, Moroder L. Houben-Weyl, Methods of Organic Chemistry, Synthesis of Peptides and Peptidomimetics (E 22b), Goodman M, Felix A, Moroder L, Toniolo C (eds). Georg Thieme Verlag: Stuttgart, 2002; 214-223.
261. Rajarathnam K, Sykes BD, Dewald B, Baggiolini M, Clark-Lewis I. Disulfide bridges in interleukin-8 probed using non-natural disulfide analogues: dissociation of roles in structure from function. Biochemistry 1999; 38: 7653-7658.
262. Koide T, Itoh H, Otaka A, Furuya M, Kitajima Y, Fujii N. Synthesis and biological activities of selenium analogues of α-rat atrialnatriuretic peptide. Chem. Pharm. Bull. 1993; 41: 1596-1600.
263. Ralle M, Berry SM, Nilges MJ, Gieselman MD, van der Donk WA, Lu Y, Blackburn NJ. The selenocysteine-substituted blue copper center: spectroscopic investigations of Cys112SeCys Pseudomonas aeruginosa azurin. J. Am. Chem. Soc. 2004; 126: 7244-7256.
264. Moroder L, Marchiori F, Borin G, Scoffone E. Studies on cytochrome c. Part II. Synthesis of the protected heptapeptide (sequence 17-23) of bakers yeast iso-I-cytochrome c. Biopolymers 1973; 12 493-505.
265. Arnér ESJ, Sarioglu H, Lottspeich F, Holmgren A, Böck A. High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with the selA, selB and selC genes. J. Mol. Biol. 1999; 292: 1003-1016.
266. Wu ZP, Hilvert D. Conversion of a protease into an acyl transferase - selenosubtilisin. J. Am. Chem. Soc. 1989; 111: 4513-4514.
267. Chu Sh, Mautner HG. Analogues of neuroeffectors. V. Neighboring-group effects in reactions of esters, thiolesters and selenolesters. Hydrolysis and aminolysis of benzoylcholine, benzoylthiolcholine, benzoylselenolcholine and of their dimethylamino analogues. J. Org. Chem. 1966; 31: 308-312.
268. Mautner HG, Chu SH, Günther WHH. Aminolysis of thioacyl and selenoacyl analogues. J. Am. Chem. Soc. 1963; 85: 3458-3462.
269. 2-thioredoxin. Biochemistry 1994; 33: 3404-3412.
270. Boschi-Müller S, Müller S, van Dorsselaer A, Böck A, Branlant G. Substituting selenocysteine for active site cysteine 149 of phosphorylating glyceraldehyde 3-phosphate dehydrogenase reveals a peroxidase activity. FEBS Lett. 1998; 439: 241-245.
271. Hondal RJ, Nilsson BL, Raines RT. Selenocysteine in native chemical ligation and expressed protein ligation. J. Am. Chem. Soc. 2001; 123: 5140-5141.
272. Quaderer R, Sewing A, Hilvert D. Selenocysteine-mediated native chemical ligation. Helv. Chim. Acta 2001; 84: 1197-1206.
273. Berry SM, Gieselman MD, Nilges MJ, van der Donk WA, Lu Y. An engineered azurin variant containing a selenocysteine copper ligand. J. Am. Chem. Soc. 2002; 124: 2084-2085.
274. Gieselman MD, Zhu Y, Zhou H, Galonic D, vander Donk WA. Selenocysteine derivatives for chemoselective ligations. ChemBioChem 2002; 3: 709-716.
275. Harpp DN, Gleason JG. Organic sulfur chemistry. 10. Selective desulfurization of disulfides - scope and mechanism. J. Am. Chem. Soc. 1971; 93: 2437-2445.
276. Fukase K, Kitazawa M, Sano A, Shimbo K, Horimoto S, Fujita H, Kubo A, Wakamiya T, Shiba T. Synthetic study on peptide antibiotic nisin. 5. Total synthesis of nisin. Bull. Chem. Soc. Jpn 1992; 65: 2227-2240.
277. 7]-endothelin-1. J. Mol. Biol. 1998; 284 779-792.
278. Fiori S, Pegoraro S, Rudolph-Böhner S, Cramer J, Moroder L. Synthesis and conformational analysis of apamin analogues with natural and non-natural cystine/selenocystine connectivities. Biopolymers 2000; 53: 550-564.
279. Müller JCD, Graf von Roedern E, Grams F, Nagase H, Moroder L. Non-peptidic cysteine derivatives as inhibitors of matrix metalloproteinases. Biol. Chem. 1997; 378: 1475-1480.
280. Pegoraro S, Fiori S, Cramer J, Rudolph-Böhner S, Moroder L. The disulfide-coupled folding pathway of apamin as derived from diselenide-quenched analogues and intermediates. Prot. Sci. 1999; 8; 1605-1613.
281. Bae JH, Alefelder S, Kaiser JT, Friedrich R, Moroder L, Huber R, Budisa N. Incorporation of β-selenolo[3,2-b]pyrrolyl-alanine into proteins for phase determination in protein x-ray crystallography. J. Mol. Biol. 2001; 309: 925-936.
282. Boles JO, Henderson J, Hatch D, Silks LAP. Synthesis and incorporation of [6,7]-selenatryptophan into dihydrofolate reductase. Biochem. Biophys. Res. Commun. 2002; 298: 257-261.
283. Sanchez JF, Hoh F, Strub MP, Aumelas A, Dumas C. Structure of the cathelicidin motif of protegrin-3 precursor: structural insights into the activation mechanism of an antimicrobial protein. Structure 2002; 10: 1363-1370.
284. Strub MP, Hoh F, Sanchez JF, Strub JM, Böck A, Aumelas A, Dumas C. Selenomethionine and selenocysteine double labeling strategy for crystallographic phasing. Structure 2003; 11: 1359-1367.
285. Besse D. Synthese and Redoxeigenschaften von Selenocystein-peptiden. Dissertation, Technical University of Munich, Munich 1997.
286. Chen Y, Barkley MD. Toward understanding tryptophan fluorescene in proteins. Biochemistry 1998; 37: 9976-9982.
287. Neves-Petersen MT, Gryczynski Z, Lakowicz J, Fojan P, Pedersen S, Petersen E, Petersen SB. High probability of disrupting a disulfide bridge mediated by an endogenous excited tryptophan residue. Protein Sci. 2002; 11: 588-600.
288. Lapidus LJ, Steinbach PJ, Eaton WA, Szabo A, Hofrichter J. Effects of chain stiffness on the dynamics of loop formation in polypeptides. Appendix: Testing a 1-dimensional diffusion model of peptide dynamics. J. Phys. Chem. B 2002; 106: 11628-11640.
289. Weljie AM, Vogel HJ. Tryptophan fluorescence of calmodulin binding domain peptides interacting with calmodulin containing unnatural methionine analogues. Protein Engineer. 2000; 13: 59-66.
290. Garberg P, Engman L, Tolmachev V, Lundqvist H, Gerdes RG, Cotgreave IA. Binding of tellurium to hepatocellular selenoproteins during incubation with inorganic tellurite: consequences for the activity of selenium-dependent glutathione peroxidase. Int. J. Biochem. Cell Biol. 1999; 31: 291-301.
291. 2- species. J. Am. Chem. Soc. 1982; 47:1641-1647.
292. Esaki N, Soda K. Te-phenyltellurohomocysteine and Te phenyltellutrocysteine. Methods Enzymol. 1987; 143: 245.
293. Rooseboom M, Vermeulen NPE, Durgut F, Commandeur JNM. Comparative study on the bioactivation mechanisms and cytotoxicity of Te-phenyl-L-tellurocysteine, Se-phenyl-L-selenocysteine and S phenyl-L-cysteine. Chem. Res. Toxicol. 2002; 15: 1610-1618.
294. Müller S. Design neuer Selenoproteine. Dissertation, Technical University of Munich, Munich, 1997.
295. Srinivasan N, Sowdhamini R, Ramakrishnan C, Balaram P. Conformation of disulfide bridges in proteins. Int. J. Pept. Protein Res. 1991; 36: 147-155.
296. Zahn H, Otten HG. Über unsymmetrische, offenkettige Cystinpeptide. Liebigs Ann. Chem. 1992; 653: 139-148.