Advances in Fmoc solid-phase peptide synthesis

Journal of Peptide Science

Volumn 22, Issue 1, 2016, Pages 4-27

  Behrendt, Raymond ^a   White, Peter ^b   Offer, John ^c  

^a Merck and Cie   (Switzerland)

^b Novabiochem   (United Kingdom)

^c THE FRANCIS CRICK INSTITUTE   (United Kingdom)

Author keywords

aspartimide; Fmoc tBu; peptide thioester; post translational modification; protecting group; racemisation; solid phase peptide synthesis

Indexed keywords

9 FLUORENYLMETHOXYCARBONYL; AMINO ACID; AMINO ACID DERIVATIVE; AMMONIUM ACETATE; ARGININE; ASPARAGINE; ASPARTIC ACID; CARBONYL DERIVATIVE; CYSTEINE; DIPEPTIDE; GLYCOPEPTIDE; HISTIDINE; HYDROXYAMINO ACID; HYDROXYL GROUP; MEMBRANE PROTEIN; ORGANIC SOLVENT; PEPTIDE; PEPTIDE DERIVATIVE; PEPTIDE FRAGMENT; PHOSPHOAMINO ACID; PHOSPHORAMIDOUS ACID; PHOSPHOSERINE; PHOSPHOTHREONINE; POLYARGININE; POLYLYSINE; RESIN; SODIUM AZIDE; SYNTHETIC PEPTIDE; THIOESTER; THIOL DERIVATIVE; UNCLASSIFIED DRUG; ASPARTIMIDE; FLUORENE DERIVATIVE;

ACYLATION; AMINO ACID SEQUENCE; CITRULLATION; FARNESYLATION; HEATING; METHYLATION; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN CARBONYLATION; PROTEIN GLYCOSYLATION; PROTEIN MODIFICATION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PURIFICATION; REVIEW; SOLID PHASE SYNTHESIS; SULFATION; ANALOGS AND DERIVATIVES; CELL LINE; CHEMISTRY; CYTOLOGY; DRUG EFFECTS; EPITHELIUM CELL; GLYCOSYLATION; HUMAN; METABOLISM; PHOSPHORYLATION; PROCEDURES; PROTEIN PRENYLATION; SYNTHESIS;

AMINO ACIDS; ASPARTIC ACID; CELL LINE; EPITHELIAL CELLS; FLUORENES; GLYCOSYLATION; HUMANS; METHYLATION; PEPTIDES; PHOSPHORYLATION; PROTEIN PRENYLATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; SOLID-PHASE SYNTHESIS TECHNIQUES;

EID: 84955256043     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.2836     Document Type: Review

References (288)

1. Fosgerau K, Hoffmann T,. Peptide therapeutics: current status and future directions. Drug Discov. Today 2015; 20: 122.
2. Kaspar AA, Reichert JM,. Future directions for peptide therapeutics development. Drug Discov. Today 2013; 18: 807.
3. Boyle AL, Woolfson DN,. De novo designed peptides for biological applications. Chem. Soc. Rev. 2011; 40: 4295.
4. Sheppard R,. The fluorenylmethoxycarbonyl group in solid phase synthesis. J. Pept. Sci. 2003; 9: 545.
5. Walter G,. Production and use of antibodies against synthetic peptides. J. Immun. Meth. 1986; 88: 149.
6. Dryland A, Sheppard RC,. Peptide synthesis. Part 8. A system for solid-phase synthesis under low pressure flow conditions. J. Chem. Soc., Perkin Trans. 1 1986; 125.
7. Chan WC, White PD,. Fmoc Solid Phase Peptide Synthesis, Oxford University Press: Oxford, UK, 2000.
8. Carpino LA, Han GY,. 9-Fluorenylmethoxycarbonyl amino-protecting group. J. Org. Chem. 1972; 37: 3404.
9. Bodanszky M, Deshmane SS, Martinez J,. Side reactions in peptide synthesis. 11. Possible removal of the 9-fluorenylmethyloxycarbonyl group by the amino components during coupling. J. Org. Chem. 1979; 44: 1622.
10. Atherton E, Logan CJ, Sheppard RC,. Peptide synthesis. Part 2. Procedures for solid-phase synthesis using N α-fluorenylmethoxycarbonylamino-acids on polyamide supports. Synthesis of substance P and of acyl carrier protein 65-74 decapeptide. J. Chem. Soc., Perkin Trans. 1 1981; 538.
11. Chang CD, Meienhofer J,. Solid phase peptide synthesis using mild base cleavage of Nalpha-fluorenylmethyloxycarbonylamino acids, exemplified by a synthesis of dihydrosomatostatin. Int. J. Pept. Protein Res. 1978; 11: 246.
12. Cameron L, Meldal M, Sheppard RC,. Feedback control in organic synthesis. A system for solid phase peptide synthesis with true automation. J. Chem. Soc., Chem. Commun. 1987; 4: 270.
13. White P, Keyte JW, Bailey K, Bloomberg G,. Expediting the Fmoc solid phase synthesis of long peptides through the application of dimethyloxazolidine dipeptides. J. Pept. Sci. 2004; 10: 18.
14. Wöhr T, Mutter M,. Pseudo-prolines in peptide synthesis: direct insertion of serine and threonine derived oxazolidines in dipeptides. Tetrahedron Lett. 1995; 36: 3847.
15. Cardona V, Eberle I, Barthelemy S, Beythien J, Doerner B, Schneeberger P, Keyte J, White PD,. Application of DMB-dipeptides in the Fmoc SPPS of difficult and aspartimide-prone sequences. Int. J. Pept. Res. Ther. 2008; 14: 285.
16. Kent SBH, in Peptides, structure and function, Proceedings of the 9th American Peptide Symposium (Eds.: Deber CM, Hruby VJ, Kopple KD), Pierce Chemical Company, Rockford, 1985, pp. 407.
17. Zompra AA, Galanis AS, Werbitzky O, Albericio F,. Manufacturing peptides as active pharmaceutical ingredients. Future Med. Chem. 2009; 1: 361.
18. Sabatino G, Papini AM,. Advances in automatic, manual and microwave-assisted solid-phase peptide synthesis. Curr. Opin. Drug. Discovery Dev. 2008; 11: 762.
19. Pires DAT, Bemquerer MP, do Nascimento CJ,. Some mechanistic aspects on Fmoc solid phase peptide synthesis. Int. J. Pept. Res. Ther. 2014; 20: 53.
20. Fields GB,. Molecular Biomethods Handbook, Humana: Totowa, NJ, 1998; 527.
21. Isidro-Llobet A, Alvarez M, Albericio F,. Amino acid-protecting groups. Chem. Rev. 2009; 109: 2455.
22. Carpino LA, Shroff H, Triolo SA, Mansour E-SM, Wenschuh H, Albericio F,. The 2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl group (Pbf) as arginine side chain protectant. Tetrahedron Lett. 1993; 34: 7829.
23. Sieber P, Riniker R,. Protection of carboxamide functions by the trityl residue: application to peptide synthesis. Tetrahedron Lett. 1991; 32: 739.
24. Photaki J, Taylor-Papadimitriou J, Sakarellos C, Mazarakis P, Zervas L,. On cysteine and cystine peptides. V. S-trityl and S-diphenylmethyl-cysteine and -cysteine peptides. J. Chem. Soc., Perkin 1 1970; 19: 2683.
25. Sieber P, Riniker B,. Protection of histidine in peptide synthesis: a reassessment of the trityl group. Tetrahedron Lett. 1987; 28: 6031.
26. Anderson GW, Callahan M,. tert-Butyl esters of amino-acids and peptides and their use in peptide synthesis. J. Am. Chem. Soc. 1960; 82: 3359.
27. Beyermann HC, Bontekoe JS,. The t-butoxy group, a novel hydroxyl-protecting group for use in peptide synthesis with hydroxy-amino acids. Recl. Trav. Chim. Pays-Bas 1961; 81: 691.
28. White P, in Peptides, chemistry & biology. Proceedings of the 12th American Peptide Symposium (Eds.: Smith JA, Rivier JE), ESCOM, Leiden, 1992, pp. 537.
29. Eggen I, Gregg B, Rode H, Swietlow A, Verlander M, Szajek A,. Control strategies for synthetic therapeutic peptide APIs part II: raw material considerations. Bio. Pharm. International. 2014; 27: 24.
30. Obkircher M, Stähelin C, Dick F,. Formation of Fmoc-β-alanine during Fmoc-protections with Fmoc-OSu. J. Pept. Sci. 2008; 14: 763.
31. Hlebowicz E, Andersen A, Andersson L, Moss B,. Identification of Fmoc-β-Ala-OH and Fmoc-β-Ala-amino acid-OH as new impurities in Fmoc-protected amino acid derivatives. J. Pept. Res. 2005; 65: 90.
32. Sigler GF, Fuller WD, Chaturvedi NC, Goodman M, Verlander M,. Formation of oligopeptides during the synthesis of 9-fluorenylmethyloxycarbonyl amino acid derivatives. Biopolymers 1983; 22: 2157.
33. Tessier M, Albericio F, Pedroso E, Grandas A, Eritja R, Giralt E, Granier C, Rietschoten J,. Amino-acids condensations in the preparation of Nα-9-fluorenylrnethyloxycarbonylamino-acids with 9-fluorenylmethylchloroformate. Int. J. Pept. Protein Res. 1983; 22: 125.
34. Bolin DR, Sytwu I-I, Humiec F, Meienhofer J,. Preparation of oligomer-free Nα-Fmoc and Nα-urethane amino acids. Int. J. Pept. Protein Res. 1989; 33: 353.
35. Khattab SN, Subirõs-Funosas R, El-Faham A, Albericio F,. Oxime carbonates: novel reagents for the introduction of fmoc and Alloc protecting groups, free of side reactions. Eur. J. Org. Chem. 2010; 2010: 3275.
36. Khattab SN, Subiros-Funosas R, El-Faham A, Albericio F,. Cyanoacetamide-based oxime carbonates: an efficient, simple alternative for the introduction of Fmoc with minimal dipeptide formation. Tetrahedron 2012; 68: 3056.
37. The International Conference on Harmonisation of Technical Requirements for Registration of Pharmaceuticals for Human Use (ICH), http://www.ich.org
38. Gerhardt J, Nicholson GJ, in Peptides 2000, Proceedings of the 26th European Peptide Symposium (Eds.: Martinez J, Fehrentz A), Editions EDK, Paris, 2001, pp. 563.
39. Subirõs-Funosas R, El-Faham A, Albericio F,. Aspartimide formation in peptide chemistry: occurrence, prevention strategies and the role of N-hydroxylamines. Tetrahedron 2011; 67: 8595.
40. Tickler AK, Barrow CJ, Wade JD,. Improved preparation of amyloid-β peptides using DBU as Nα-Fmoc deprotection reagent. J. Pept. Sci. 2001; 7: 488.
41. Bodanszky M, Kwei JZ,. Side reactions in peptide synthesis. Int. J. Pept. Protein Res. 1978; 12: 69.
42. Martinez J, Bodanszky M,. Side reactions in peptide synthesis. Int. J. Pept. Protein Res. 1978; 12: 277.
43. Chandra K, Roy TK, Shalev DE, Loyter A, Gilon C, Gerber RB, Friedler A,. A tandem in situ peptide cyclization through trifluoroacetic acid cleavage. Angew. Chem. Int. Ed. 2014; 53: 9450.
44. Michels T, Doelling R, Haberkorn U, Mier W,. Acid-mediated prevention of aspartimide formation in solid phase peptide synthesis. Org. Lett. 2012; 14: 5218.
45. Lauer JL, Fields CG, Fields GB,. Sequence dependence of aspartimide formation during 9-fluorenylmethoxycarbonyl solid-phase peptide synthesis. Lett. Pept. Sci. 1995; 1: 197.
46. Mergler M, Dick F, Sax B, Staehelin C, Vorherr T,. The aspartimide problem in Fmoc-based SPPS. Part II. J. Pept. Sci. 2003; 9: 518.
47. Quibell M, Owen D, Packman LC, Johnson T,. Suppression of piperidine-mediated side product formation for Asp(OBut) containing peptides by the use of N-(2-hydroxy-4-methoxybenzyl)(Hmb) backbone amide protection. J. Chem. Soc., Chem. Commun. 1994; 20: 2343.
48. Offer J, Quibell M, Johnson T,. On-resin solid-phase synthesis of asparagine N-linked glycopeptides: use of N-(2-acetoxy-4-methoxybenzyl)(AcHmb) aspartyl amide-bond protection to prevent unwanted aspartimide formation. J. Chem. Soc., Perkin Trans. 1 1996; 2: 175.
49. Mergler M, Dick F,. The aspartimide problem in Fmoc-based SPPS. Part III. J. Pept. Sci. 2005; 11: 650.
50. Karlström A, Undén A,. A new protecting group for aspartic acid that minimizes piperidine-catalyzed aspartimide formation in Fmoc solid phase peptide synthesis. Tetrahedron Lett. 1996; 37: 4243.
51. Mergler M, Dick F, Sax B, Weiler P, Vorherr T,. The aspartimide problem in Fmoc-based SPPS. Part I. J. Pept. Sci. 2003; 9: 36.
52. Karlström A, Undén A,. Design of protecting groups for the β-carboxylic group of aspartic acid that minimize base-catalyzed aspartimide formation. Int. J. Pept. Protein Res. 1996; 48: 305.
53. Bodanszky M, Martinez J,. Side reactions in peptide synthesis. 8. On the phenacyl group in the protection of the beta-carboxyl function of aspartyl residues. J. Org. Chem. 1978; 43: 3071.
54. Dölling R, Beyermann M, Haenel J, Kernchen F, Krause E, Franke P, Brudel M, Bienert M,. Piperidine-mediated side product formation for Asp(OBut)-containing peptides. J. Chem. Soc., Chem. Commun. 1994; 7: 853.
55. Ullmann V, Raedisch M, Boos I, Freund J, Poehner C, Schwarzinger S, Unverzagt C,. Convergent solid-phase synthesis of N-glycopeptides facilitated by pseudoprolines at consensus-sequence Ser/Thr residues. Angew. Chem. Int. Ed. 2012; 51: 11566.
56. Wang P, Aussedat B, Vohra Y, Danishefsky SJ,. An advance in the chemical synthesis of homogeneous N-linked glycopolypeptides by convergent aspartylation. Angew. Chem. Int. Ed. 2012; 51: 11571.
57. Behrendt R, Huber S, Martí R, White P,. New t-butyl based aspartate protecting groups preventing aspartimide formation in Fmoc SPPS. J. Pept. Sci. 2015; 21: 680.
58. Subirõs-Funosas R, El-Faham A, Albericio F,. Use of Oxyma as pH modulatory agent to be used in the prevention of base-driven side reactions and its effect on 2-chlorotrityl chloride resin. Pept. Sci. 2012; 98: 89.
59. Packman LC,. N-2-Hydroxy-4-methoxybenzyl(Hmb) backbone protection strategy prevents double aspartimide formation in a 'difficult' peptide sequence. Tetrahedron Lett. 1995; 36: 7523.
60. Röder R, Henklein P, Weißhoff H, Mügge C, Pätzel M, Schubert U, Carpino LA, Henklein P,. On the use of N-dicyclopropylmethyl aspartyl-glycine synthone for backbone amide protection. J. Pept. Sci. 2010; 16: 65.
61. Conroy T, Jolliffe KA, Payne RJ,. Synthesis of N-linked glycopeptides via solid-phase aspartylation. Org. Biomol. Chem. 2010; 8: 3723.
62. El Oualid F, Merkx R, Ekkebus R, Hameed DS, Smit JJ, de Jong A, Hilkmann H, Sixma TK, Ovaa H,. Chemical synthesis of ubiquitin, ubiquitin-based probes, and diubiquitin. Angew. Chem. Int. Ed. 2010; 49: 10149.
63. Ramage R, Green J,. NG-2,2,5,7,8-pentamethylchroman-6-sulfonyl- l -arginine: a new acid labile derivative for peptide synthesis. Tetrahedron Lett. 1987; 28: 2287.
64. Green J, Ogunjobi O, Ramage R, Stewart A, McCurdy S, Noble R,. Application of the NG-(2,2,5,7,8-pentamethylchroman-6-sulphonyl) derivative of FMOC-arginine to peptide synthesis. Tetrahedron Lett. 1988; 29: 4341.
65. Isidro A, Latassa D, Giraud M, Alvarez M, Albericio F,. 1,2-Dimethylindole-3-sulfonyl (MIS) as protecting group for the side chain of arginine. Org. Biomol. Chem. 2009; 7: 2565.
66. Noda M, Kiffe M,. New mild acid-labile protecting groups for the guanidino function of Nα-fluorenylmethoxycarbonyl- l -arginine in solid-phase peptide synthesis: 10, 11-dihydro-5H-dibenzo [a, d]. cyclohepten-5-yl, 2-methoxy-10, 11-dihydoro-5H-dibenzo [a, d]. cyclohepten-5-yl and 5H-dibenzo [a, d]. cyclohepten-5-yl groups. J. Pept. Res. 1997; 50: 329.
67. Paul R, Anderson GW, Callahan FM,. Some side reactions of nitro- l -arginine. J. Org. Chem. 1961; 26: 3347.
68. Fields GB, Noble RL,. Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int. J. Pept. Protein Res. 1990; 35: 161.
69. Rink H, Sieber P, Raschdorf F,. Conversion of N G urethane protected arginine to ornithine in peptide solid phase synthesis. Tetrahedron Lett. 1984; 25: 621.
70. Musiol HJ, Siedler F, Quarzago D, Moroder L,. Redox-active bis-cysteinyl peptides. I. Synthesis of cyclic cystinyl peptides by conventional methods in solution and on solid supports. Biopolymers 1994; 34: 1553.
71. Kaiser T, Nicholson G, Kohlbau H, Voelter W,. Racemization studies of Fmoc-Cys (Trt)-OH during stepwise Fmoc-solid phase peptide synthesis. Tetrahedron Lett. 1996; 37: 1187.
72. Palasek SA, Cox ZJ, Collins JM,. Limiting racemization and aspartimide formation in microwave-enhanced Fmoc solid phase peptide synthesis. J. Pept. Sci. 2007; 13: 143.
73. Han Y, Albericio F, Barany G,. Occurrence and minimization of cysteine racemization during stepwise solid-phase peptide synthesis. J. Org. Chem. 1997; 62: 4307.
74. Collins JM, Porter KA, Singh SK, Vanier GS,. High-efficiency solid phase peptide synthesis (HE-SPPS). Org. Lett. 2014; 16: 940.
75. Hibino H, Miki Y, Nishiuchi Y,. Evaluation of acid-labile S-protecting groups to prevent Cys racemization in Fmoc solid-phase peptide synthesis. J. Pept. Sci. 2014; 20: 30.
76. Mitchell MA, Runge TA, Mathews WR, Ichhpurani AK, Harn NK, Dobrowolski PJ, Eckenrode FM,. Problems associated with use of the benzyloxymethyl protecting group for histidines. Formaldehyde adducts formed during cleavage by hydrogen fluoride 1. Int. J. Pept. Protein Res. 1990; 36: 350.
77. Kumiko YK, Ishizu T, Isaka S, Tamura M, Rumi OT, Nishiuchi Y, Kimura T, in Peptide Science 2005: Proceedings of the 42nd Japanese Peptide Symposium (Ed.: Wakamiya T), Japanese Peptide Society, Osaka, 2006, pp. 163.
78. Hibino H, Nishiuchi Y,. 4-Methoxybenzyloxymethyl group as an Nπ-protecting group for histidine to eliminate side-chain-induced racemization in the Fmoc strategy. Tetrahedron Lett. 2011; 52: 4947.
79. Ramos-Tomillero I, Rodríguez H, Albericio F,. Tetrahydropyranyl, a nonaromatic acid-labile Cys protecting group for Fmoc peptide chemistry. Org. Lett. 2015, 17, 1680.
80. Atherton E, Hardy P, Harris DE, Matthews BH, in Peptides 1990: Proceedings of the Twenty First European Peptide Symposium (Eds.: Giralt E, Andreu D), Escom, Leiden, 1991, pp. 243.
81. Windridge G, Jorgensen EC,. 1-Hydroxybenzotriazole as a racemization-suppressing reagent for the incorporation of im-benzyl- l -histidine into peptides. J. Am. Chem. Soc. 1971; 93: 6318.
82. Jones JH, Ramage WI,. An approach to the prevention of racemization in the synthesis of histidine-containing peptides. J. Chem. Soc., Chem. Commun. 1978; 11: 472.
83. Jones JH, Ramage WI, Witty MJ,. Mechanism of racemisation of histidine derivatives in peptide synthesis. Int. J. Pept. Protein Res. 1980; 15: 301.
84. Brown T, Jones JH,. Protection of histidine side-chains with π-benzyloxymethyl or π-bromobenzyloxymethyl groups. J. Chem. Soc., Chem. Commun. 1981; 13: 648.
85. Brown T, Jones JH, Richards JD,. Further studies on the protection of histidine side chains in peptide synthesis: the use of the π-benzyloxymethyl group. J. Chem. Soc., Perkin Trans. 1 1982; 1553.
86. Colombo R, Colombo F, Jones JH,. Acid-labile histidine side-chain protection: the N(π)-tert-butoxymethyl group. J. Chem. Soc., Chem. Commun. 1984; 5: 292.
87. Okada Y, Wang J, Yamamoto T, Mu Y, Yokoi T,. Amino acids and peptides. Part 45. Development of a new Nπ-protecting group of histidine, Nπ-(1-adamantyloxymethyl) histidine, and its evaluation for peptide synthesis. J. Chem. Soc., Perkin Trans. 1 1996; 2139.
88. Hibino H, Miki Y, Nishiuchi Y,. Synthesis and application of Nα-Fmoc-Nπ-4-methoxybenzyloxymethylhistidine in solid phase peptide synthesis. J. Pept. Sci. 2012; 18: 763.
89. Narita M, Ishikawa K, Chen JY, Kim Y,. Prediction and improvement of protected peptide solubility in organic solvents. Int. J. Pept. Protein Res. 1984; 24: 580.
90. Narita M, Fukunaga T, Wakabayashi A, Ishikawa K, Nakano H,. Syntheses and properties of tertiary peptide bond-containing polypeptides. Int. J. Pept. Protein Res. 1984; 23: 306.
91. Meyer DE, Chilkoti A,. Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nat. Biotechnol. 1999; 17: 1112.
92. Chiti F, Dobson CM,. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006; 75: 333.
93. Nishiuchi Y, Inui T, Nishio H, Bõdi J, Kimura T, Tsuji FI, Sakakibara S,. Chemical synthesis of the precursor molecule of the Aequorea green fluorescent protein, subsequent folding, and development of fluorescence. Proc. Natl. Acad. Sci. 1998; 95: 13549.
94. Sakakibara S,. Chemical synthesis of proteins in solution. Pept. Sci. 1999; 51: 279.
95. Hancock WS, Prescott DJ, Vagelos PR, Marshall GR,. Solvation of the polymer matrix. Source of truncated and failure sequences in solid phase synthesis. J. Org. Chem. 1973; 38: 774.
96. Bedford J, Hyde C, Johnson T, Jun W, Owen D, Quibell M, Sheppard RC,. Amino acid structure and 'difficult sequences' in solid phase peptide synthesis. Int. J. Pept. Protein Res. 1992; 40: 300.
97. Van Woerkom W, Van Nispen J,. Difficult couplings in stepwise solid phase peptide synthesis: predictable or just a guess? Int. J. Pept. Protein Res. 1991; 38: 103.
98. Lahiri S, Brehs M, Olschewski D, Becker CF,. Total chemical synthesis of an integral membrane enzyme: diacylglycerol kinase from Escherichia coli. Angew. Chem. Int. Ed. 2011; 50: 3988.
99. Johnson EC, Malito E, Shen Y, Rich D, Tang W-J, Kent SB,. Modular total chemical synthesis of a human immunodeficiency virus type 1 protease. J. Am. Chem. Soc. 2007; 129: 11480.
100. Hossain MA, Belgi A, Lin F, Zhang S, Shabanpoor F, Chan L, Belyea C, Truong H-T, Blair AR, Andrikopoulos S, Tregear GW, Wade JD,. Use of a temporary 'solubilizing' peptide tag for the Fmoc solid-phase synthesis of human insulin glargine via use of regioselective disulfide bond formation. Bioconjugate Chem. 2009; 20: 1390.
101. Wu C-R, Stevens VC, Tregear GW, Wade JD,. Continuous-flow solid-phase synthesis of a 74-peptide fragment analogue of human β-chorionic gonadotropin. J. Chem. Soc., Perkin Trans. 1 1989; 81.
102. Weygand F, Steglich W, Bjarnason J, Akhtar R, Khan NM,. Leicht abspaltbare schutzgruppen für säureamidfunktionen 1. Mitteilung. Tetrahedron Lett. 1966; 7: 3483.
103. Narita M, Ishikawa K, Nakano H, Isokawa S,. Tertiary peptide bond containing-oligo (Leu) s. Int. J. Pept. Protein Res. 1984; 24: 14.
104. Hyde C, Johnson T, Owen D, Quibell M, Sheppard R,. Some 'difficult sequences' made easy. Int. J. Pept. Protein Res. 1994; 43: 431.
105. Blaakmeer J, Tijsse-Klasen T, Tesser GI,. Enhancement of solubility by temporary dimethoxybenzyl-substitution of peptide bonds. Towards the synthesis of defined oligomers of alanine and of lysyl-glutamyl-glycine. Int. J. Pept. Protein Res. 1991; 37: 556.
106. Johnson T, Quibell M, Owen D, Sheppard RC,. A reversible protecting group for the amide bond in peptides. Use in the synthesis of difficult sequences. J. Chem. Soc., Chem. Commun. 1993; 4: 369.
107. Quibell M, Turnell WG, Johnson T,. Reversible modification of the acid labile 2-hydroxy-4-methoxybenzyl (Hmb) amide protecting group: a simple scheme yielding backbone substituted free peptides. Tetrahedron Lett. 1994; 35: 2237.
108. Quibell M, Turnell W, Johnson T,. Preparation and purification of beta-amyloid (1-43) via soluble, amide backbone protected intermediates. J. Org. Chem. 1994; 59: 1745.
109. Clippingdale A, Macris M, Wade J, Barrow C,. Synthesis and secondary structural studies of penta (acetyl-Hmb) Aβ (1-40). J. Pept. Res. 1999; 53: 665.
110. Carpino LA, Nasr K, Abdel-Maksoud AA, El-Faham A, Ionescu D, Henklein P, Wenschuh H, Beyermann M, Krause E, Bienert M,. Dicyclopropylmethyl peptide backbone protectant. Org. Lett. 2009; 11: 3718.
111. Isidro-Llobet A, Just-Baringo X, Alvarez M, Albericio F,. EDOTn and MIM, new peptide backbone protecting groups. Pept. Sci. 2008; 90: 444.
112. Ede NJ, Ang KH, James IW, Bray AM,. Incorporation of 2-hydroxy-4-methoxybenzyl protection during peptide synthesis via reductive alkylation on the solid phase. Tetrahedron Lett. 1996; 37: 9097.
113. Wöhr T, Wahl F, Nefzi A, Rohwedder B, Sato T, Sun X, Mutter M,. Pseudo-prolines as a solubilizing, structure-disrupting protection technique in peptide synthesis. J. Am. Chem. Soc. 1996; 118: 9218.
114. Offer J, Johnson T, Quibell M,. Application of reversible amide-bond protection to suppress peptide segment epimerization. Tetrahedron Lett. 1997; 38: 9047.
115. Abdel-Aal AM, Papageorgiou G, Quibell M, Offer J,. Automated synthesis of backbone protected peptides. Chem. Commun. 2014; 50: 8316.
116. Miranda LP, Meutermans WD, Smythe ML, Alewood PF,. An activated O → N acyl transfer auxiliary: efficient amide-backbone substitution of hindered 'difficult' peptides. J. Org. Chem. 2000; 65: 5460.
117. Paradís-Bas M, Tulla-Puche J, Albericio F,. 2-Methoxy-4-methylsulfinylbenzyl: a backbone amide safety-catch protecting group for the synthesis and purification of difficult peptide sequences. Chem. Eur. J. 2014; 20: 15031.
118. Huang Y-C, Guan C-J, Tan X-L, Chen C-C, Guo Q-X, Li Y-M,. Accelerated Fmoc solid-phase synthesis of peptides with aggregation-disrupting backbones. Org. Biomol. Chem. 2015; 13: 1500.
119. Kemp D, Carey RI,. Boc-L-Dmt-OH as a fully N,S-blocked cysteine derivative for peptide synthesis by prior thiol capture. Facile conversion of N-terminal Boc- l -Dmt-peptides to H-Cys (Scm)-peptides. J. Org. Chem. 1989; 54: 3640.
120. Barber M, Jones JH,. An alternative synthesis of [7-(thiazolidine-4-carboxylic acid)] oxytocin. Int. J. Pept. Protein Res. 1977; 9: 269.
121. Goncalves V, Gautier B, Huguenot F, Leproux P, Garbay C, Vidal M, Inguimbert N,. Total chemical synthesis of the D2 domain of human VEGF receptor 1. J. Pept. Sci. 2009; 15: 417.
122. Mutter M, Chandravarkar A, Boyat C, Lopez J, Santos SD, Mandal B, Mimna R, Murat K, Patiny L, Saucède L, Tuchscherer G,. Switch peptides in statu nascendi: induction of conformational transitions relevant to degenerative diseases. Angew. Chem. Int. Ed. 2004; 43: 4172.
123. Carpino LA, Krause E, Sferdean 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.
124. 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; 1: 124.
125. Sohma Y, Kiso Y,. Synthesis of O-acyl isopeptides. The Chemical Record 2013; 13: 218.
126. Coin I,. The depsipeptide method for solid-phase synthesis of difficult peptides. J. Pept. Sci. 2010; 16: 223.
127. Miranda LP, Alewood PF,. Challenges for protein chemical synthesis in the 21st century: bridging genomics and proteomics. Biopolymers 2000; 55: 217.
128. Burlina F, Papageorgiou G, Morris C, White PD, Offer J,. In situ thioester formation for protein ligation using α-methylcysteine. Chem. Sci. 2014; 5: 766.
129. Zheng J-S, Yu M, Qi Y-K, Tang S, Shen F, Wang Z-P, Xiao L, Zhang L, Tian C-L, Liu L,. Expedient total synthesis of small to medium-sized membrane proteins via Fmoc chemistry. J. Am. Chem. Soc. 2014; 136: 3695.
130. Asahina Y, Kamitori S, Takao T, Nishi N, Hojo H,. Chemoenzymatic synthesis of the immunoglobulin domain of Tim-3 carrying a complex-type N-glycan by using a one-pot ligation. Angew. Chem. Int. Ed. 2013; 52: 9733.
131. Prabakaran S, Lippens G, Steen H, Gunawardena J,. Post-translational modification: nature's escape from genetic imprisonment and the basis for dynamic information encoding. Wiley Interdiscip. Rev. Syst. Biol. Med. 2012; 4: 565.
132. Walsh CT, Garneau-Tsodikova S, Gatto GJ,. Protein posttranslational modifications: the chemistry of proteome diversifications. Angew. Chem. Int. Ed. 2005; 44: 7342.
133. Lothrop AP, Torres MP, Fuchs SM,. Deciphering post-translational modification codes. FEBS Lett. 2013; 587: 1247.
134. Kouzarides T,. Chromatin modifications and their function. Cell 2007; 128: 693.
135. 3Bzl, H)-OH. Lett. Pept. Sci. 1999; 6: 91.
136. Wakamiya T, Saruta K, Yasuoka J-i, Kusumoto S,. An efficient procedure for solid-phase synthesis of phosphopeptides by the Fmoc strategy. Chem. Lett. 1994; 6: 1099.
137. White P, Beythien J, in Innovations & perspectives in solid phase synthesis & combinatorial libraries, 4th International Symposium (Ed.: Epton R), Mayflower Scientific Ltd, Birmingham, 1996, pp. 557.
138. Kitas E, Perich J, Wade J, Johns R, Tregear G,. Fmoc-polyamide solid phase synthesis of an O-phosphotyrosine-containing tridecapeptide. Tetrahedron Lett. 1989; 30: 6229.
139. Perich JW, Reynolds EC,. The facile one-pot synthesis of Nα-(9-fluorenylmethoxycarbonyl)-O-(O′,O-dialkylphosphoro)- l -tyrosines using dialkyl N,N-diethylphosphoramidites. Synlett 1991; 1991: 577.
140. Ottinger EA, Shekels LL, Bernlohr DA, Barany G,. Synthesis of phosphotyrosine-containing peptides and their use as substrates for protein tyrosine phosphatases. Biochemistry 1993; 32: 4354.
141. Chao H-G, Leiting B, Reiss PD, Burkhardt AL, Klimas CE, Bolen JB, Matsueda GR,. Synthesis and application of Fmoc-O-[bis (dimethylamino)phosphono] tyrosine, a versatile protected phosphotyrosine equivalent. J. Org. Chem. 1995; 60: 7710.
142. Chao H-G, Bernatowicz MS, Reiss PD, Matsueda GR,. Synthesis and application of bis-silylethyl-derived phosphate-protected Fmoc-phosphotyrosine derivatives for peptide synthesis. J. Org. Chem. 1994; 59: 6687.
143. Chauhan SS, Varshney A, Verma B, Pennington MW,. Efficient synthesis of protected l -phosphonophenylalanine (Ppa) derivatives suitable for solid phase peptide synthesis. Tetrahedron Lett. 2007; 48: 4051.
144. Marseigne I, Roques BP,. Synthesis of new amino acids mimicking sulfated and phosphorylated tyrosine residues. J. Org. Chem. 1988; 53: 3621.
145. Gordeev MF, Patel DV, Barker PL, Gordon EM,. N-α-Fmoc-4-phosphono (difluoromethyl)- l -phenylalanine: a new O-phosphotyrosine isosteric building block suitable for direct incorporation into peptides. Tetrahedron Lett. 1994; 35: 7585.
146. Simpson LS, Widlanski TS,. A comprehensive approach to the synthesis of sulfate esters. J. Am. Chem. Soc. 2006; 128: 1605.
147. Simpson LS, Zhu JZ, Widlanski TS, Stone MJ,. Regulation of chemokine recognition by site-specific tyrosine sulfation of receptor peptides. Chem. Biol. 2009; 16: 153.
148. Ali AM, Taylor SD,. Efficient solid-phase synthesis of sulfotyrosine peptides using a sulfate protecting-group strategy. Angew. Chem. Int. Ed. 2009; 48: 2024.
149. Ali AM, Hill B, Taylor SD,. Trichloroethyl group as a protecting group for sulfonates and its application to the synthesis of a disulfonate analog of the tyrosine sulfated PSGL-143-50 peptide. J. Org. Chem. 2009; 74: 3583.
150. White P, in Novabiochem innovations, 2006.
151. Rothbart SB, Krajewski K, Strahl BD, Fuchs SM,. Peptide microarrays to interrogate the 'histone code'. Methods Enzymol. 2012; 512: 107.
152. Meldal M, Bock K,. Pentafluorophenyl esters for temporary carboxyl group protection in solid phase synthesis of N-linked glycopeptides. Tetrahedron Lett. 1990; 31: 6987.
153. Meinjohanns E, Meldal M, Paulsen H, Dwek RA, Bock K,. Novel sequential solid-phase synthesis of N-linked glycopeptides from natural sources. J. Chem. Soc., Perkin Trans. 1 1998; 549.
154. Paulsen H, Adermann K,. Synthese von O-Glycopeptid-Sequenzen des N-Terminus von Interleukin-2. Liebigs Ann. Chem. 1989; 1989: 751.
155. Irazoqui FJ, Vides MA, Nores GA,. Structural requirements of carbohydrates to bind Agaricus bisporus lectin. Glycobiology 1999; 9: 59.
156. Liebe B, Kunz H,. Solid-phase synthesis of a tumor-associated sialyl-tn antigen glycopeptide with a partial sequence of the 'tandem repeat' of the MUC-1 mucin. Angew. Chem. Int. Ed. 1997; 36: 618.
157. Komba S, Meldal M, Werdelin O, Jensen T, Bock K,. Convenient synthesis of Thr and Ser carrying the tumor associated sialyl-(2 → 3)-T antigen as building blocks for solid-phase glycopeptide synthesis. J. Chem. Soc., Perkin Trans. 1 1999; 415.
158. Zhang Y, Muthana SM, Farnsworth D, Ludek O, Adams K, Barchi JJ, Jr, Gildersleeve JC,. Enhanced epimerization of glycosylated amino acids during solid-phase peptide synthesis. J. Am. Chem. Soc. 2012; 134: 6316.
159. Arsequell G, Krippner L, Dwek RA, Wong SYC,. Building blocks for solid-phase glycopeptide synthesis: 2-acetamido-2-deoxy- β- d -glycosides of FmocSerOH and FmocThrOH. J. Chem. Soc., Chem. Commun. 1994; 2383.
160. Cohen P,. The regulation of protein function by multisite phosphorylation-a 25 year update. Trends Biochem. Sci. 2000; 25: 596.
161. Besant PG, Attwood PV,. Histidine phosphorylation in histones and in other mammalian proteins. Methods Enzymol. 2010; 471: 403.
162. Cies̈la J, Frączyk T, Rode W,. Phosphorylation of basic amino acid residues in proteins: important but easily missed. Acta Biochim. Pol. 2011; 58: 137.
163. Perich JW, in Houben-Weyl Methods of Organic Synthesis, Synthesis of Peptides and Peptidomimetics, Vol. E22b (Eds.:, Goodman M, Felix A, Moroder L, Toniolo C,), Georg Thieme, Stuttgart, 2002, pp. 375.
164. Andrews D, Kitchin J, Seale P,. Solid-phase synthesis of a range of O-phosphorylated peptides by post-assembly phosphitylation and oxidation. Int. J. Pept. Protein Res. 1991; 38: 469.
165. Petrillo DE, Mowrey DR, Allwein SP, Bakale RP,. A general preparation of protected phosphoamino acids. Org. Lett. 2012; 14: 1206.
166. Ottinger EA, Xu Q, Barany G,. Intramolecular pyrophosphate formation during N: α-9-fluorenylmethyloxycarbonyl (Fmoc) solid-phase synthesis of peptides containing adjacent phosphotyrosine residues. Pept. Res. 1995; 9: 223.
167. 2)-OH in solid-phase peptide synthesis. Lett. Pept. Sci. 1995; 2: 93.
168. α-fluorenylmethoxycarbonyl-O-dibenzylphosphono- l -tyrosine in continuous flow solid phase peptide synthesis. J. Chem. Soc., Chem. Commun. 1991; 5: 338.
169. 4-phospho- l -tyrosine-containing peptides. Helv. Chim. Acta 1991; 74: 1314.
170. Pascal R, in Peptides 2000, Proceedings of the 26th European Peptide Symposium (Eds.: Martinez J, Fehrentz A), Editions EDK, Paris, 2001, pp. 263.
171. 2+/calmodulin-dependent protein kinases: from biochemistry to pharmacology. Pharm. Ther. 2003; 100: 291.
172. Lacombe J, Andriamanampisoa F, Pavia A,. Solid-phase synthesis of peptides containing phosphoserine using phosphate tert-butyl protecting group. Int. J. Pept. Protein Res. 1990; 36: 275.
173. Harris PW, Williams GM, Shepherd P, Brimble MA,. The synthesis of phosphopeptides using microwave-assisted solid phase peptide synthesis. Int. J. Pept. Res. Ther. 2008; 14: 387.
174. Vorherr T, Bannwarth W,. Phospho-serine and phospho-threonine building blocks for the synthesis of phosphorylated peptides by the Fmoc solid phase strategy. Bioorg. Med. Chem. Lett. 1995; 5: 2661.
175. 3Bzl, H)-OH in peptide synthesis. Int. J. Pept. Res. Ther. 2009; 15: 69.
176. Burke TRJ, Smyth MS, Otaka A, Nomizu M, Roller PP, Wolf G, Case R, Shoelson SE,. Nonhydrolyzable phosphotyrosyl mimetics for the preparation of phosphatase-resistant SH2 domain inhibitors. Biochemistry 1994; 33: 6490.
177. Engel R,. Phosphonates as analogues of natural phosphates. Chem. Rev. 1977; 77: 349.
178. Berkowitz DB, Shen Q, Maeng J-H,. Synthesis of the (α,α-difluoroalkyl) phosphonate analogue of phosphoserine. Tetrahedron Lett. 1994; 35: 6445.
179. Ruiz M, Ojea V, Shapiro G, Weber H-P, Pombo-Villar E,. Asymmetric synthesis of a protected phosphonate isostere of phosphothreonine for solid-phase peptide synthesis. Tetrahedron Lett. 1994; 35: 4551.
180. Berkowitz DB, Eggen M, Shen Q, Shoemaker RK,. Ready access to fluorinated phosphonate mimics of secondary phosphates. Synthesis of the (α,α-difluoroalkyl) phosphonate analogues of l-phosphoserine, l-phosphoallothreonine, and l-phosphothreonine. J. Org. Chem. 1996; 61: 4666.
181. Burke TR, Jr, Smyth MS, Nomizu M, Otaka A, Roller PR,. Preparation of fluoro-and hydroxy-4-(phosphonomethyl)- d, l -phenylalanine suitably protected for solid-phase synthesis of peptides containing hydrolytically stable analogs of O-phosphotyrosine. J. Org. Chem. 1993; 58: 1336.
182. Burke TR, Smyth MS, Otaka A, Roller PP,. Synthesis of 4-phosphono (difluoromethyl)- d, l -phenylalanine and N-Boc and N-Fmoc derivatives suitably protected for solid-phase synthesis of nonhydrolyzable phosphotyrosyl peptide analogues. Tetrahedron Lett. 1993; 34: 4125.
183. Liu W-Q, Olszowy C, Bischoff L, Garbay C,. Enantioselective synthesis of (2S)-2-(4-phosphonophenylmethyl)-3-aminopropanoic acid suitably protected for peptide synthesis. Tetrahedron Lett. 2002; 43: 1417.
184. Schenkels C, Erni B, Reymond J-L,. Phosphofurylalanine, a stable analog of phosphohistidine. Bioorg. Med. Chem. Lett. 1999; 9: 1443.
185. Yang SH, Lee DJ, Brimble MA,. Synthesis of an NDPK phosphocarrier domain peptide containing a novel triazolylalanine analogue of phosphohistidine using click chemistry. Org. Lett. 2011; 13: 5604.
186. Kee J-M, Villani B, Carpenter LR, Muir TW,. Development of stable phosphohistidine analogues. J. Am. Chem. Soc. 2010; 132: 14327.
187. Domchek SM, Auger KR, Chatterjee S, Burke TR, Jr, Shoelson SE,. Inhibition of SH2 domain/phosphoprotein association by a nonhydrolyzable phosphonopeptide. Biochemistry 1992; 31: 9865.
188. Burke TR, Jr,. Design and synthesis of phosphonodifluoromethyl phenylalanine (F2Pmp): a useful phosphotyrosyl mimetic. Curr. Top. Med. Chem. 2006; 6: 1465.
189. Burke TR, Jr,. Development of Grb2 SH2 domain signaling antagonists: a potential new class of antiproliferative agents. Int. J. Pept. Res. Ther. 2006; 12: 33.
190. Attwood P, Piggott M, Zu X, Besant P,. Focus on phosphohistidine. Amino Acids 2007; 32: 145.
191. McAllister TE, Webb ME,. Triazole phosphohistidine analogues compatible with the Fmoc-strategy. Org. Biomol. Chem. 2012; 10: 4043.
192. McAllister TE, Horner KA, Webb ME,. Evaluation of the interaction between phosphohistidine analogues and phosphotyrosine binding domains. ChemBioChem 2014; 15: 1088.
193. McAllister TE, Nix MG, Webb ME,. Fmoc-chemistry of a stable phosphohistidine analogue. Chem. Commun. 2011; 47: 1297.
194. Kee J-M, Muir TW,. Chasing phosphohistidine, an elusive sibling in the phosphoamino acid family. ACS Chem. Biol. 2011; 7: 44.
195. Kee J-M, Oslund RC, Perlman DH, Muir TW,. A pan-specific antibody for direct detection of protein histidine phosphorylation. Nature Chem. Biol. 2013; 9: 416.
196. Bertran-Vicente J, Schümann M, Schmieder P, Krause E, Hackenberger CPR,. Direct access to site-specifically phosphorylated-lysine peptides from a solid-support. Org. Biomol. Chem. 2015; 13: 6839.
197. Yates LM, Marmelstein AM, Fiedler D,. Synthetic pyrophosphorylation methods and their use in chemical Biology. Synlett 2014; 25: 2239.
198. Wu M, Chong LS, Capolicchio S, Jessen HJ, Resnick AC, Fiedler D,. Elucidating diphosphoinositol polyphosphate function with nonhydrolyzable analogues. Angew. Chem. 2014; 126: 7320.
199. Seibert C, Sakmar TP,. Toward a framework for sulfoproteomics: synthesis and characterization of sulfotyrosine-containing peptides. Pept. Sci. 2008; 90: 459.
200. Sasaki N,. Current status and future prospects for research on tyrosine sulfation. Curr. Pharm. Biotech. 2012; 13: 2632.
201. Kehoe JW, Bertozzi CR,. Tyrosine sulfation: a modulator of extracellular protein-protein interactions. Chem. Biol. 2000; 7: R57.
202. Ludeman JP, Stone MJ,. The structural role of receptor tyrosine sulfation in chemokine recognition. Br. J. Pharmacol. 2014; 171: 1167.
203. Moore KL,. The biology and enzymology of protein tyrosine O-sulfation. J. Biol. Chem. 2003; 278: 24243.
204. Stone ML, Payne RJ,. Homogenous sulfopeptides and sulfoproteins: synthetic approaches and applications to characterize the effects of tyrosine sulfation on biochemical function. Acc. Chem. Res. 2015; 48: 2251.
205. Musiol HJ, Escherich A, Moroder L, in Houben-Weyl Methods of Organic Synthesis, Synthesis of Peptides and Peptidomimetics, Vol. E22b (Eds.:, Goodman M, Felix A, Moroder L, Toniolo C,), Georg Thieme, Stuttgart, 2002, pp. 424.
206. Young T, Kiessling LL,. A strategy for the synthesis of sulfated peptides. Angew. Chem. 2002; 114: 3599.
207. Bunschoten A, Kruijtzer JA, Ippel JH, de Haas CJ, van Strijp JA, Kemmink J, Liskamp RM,. A general sequence independent solid phase method for the site specific synthesis of multiple sulfated-tyrosine containing peptides. Chem. Commun. 2009; 21: 2999.
208. Peters C, Wagner M, Völkert M, Waldmann H,. Bridging the gap between cell biology and organic chemistry: chemical synthesis and biological application of lipidated peptides and proteins. Naturwissenschaften 2002; 89: 381.
209. Novelli G, D'Apice MR,. Protein farnesylation and disease. J. Inherit. Metab. Dis. 2012; 35: 917.
210. Naider FR, Becker JM,. Synthesis of prenylated peptides. Biopolymers 1997; 43: 3.
211. Kragol G, Lumbierres M, Palomo JM, Waldmann H,. Protein synthesis: solid-phase synthesis of lipidated peptides. Angew. Chem. Int. Ed. 2004; 43: 5839.
212. Pegoraro S, Moroder L, in Houben-Weyl Methods of Organic Synthesis, Synthesis of Peptides and Peptidomimetics, Vol. E22b (Eds.:, Goodman M, Felix A, Moroder L, Toniolo C,), Georg Thieme, Stuttgart, 2002, pp. 333.
213. O'Reilly N, Charbin A, Lopez-Serra L, Uhlmann F,. Facile synthesis of budding yeast a-factor and its use to synchronize cells of α mating type. Yeast 2012; 29: 233.
214. Kadereit D, Deck P, Heinemann I, Waldmann H,. Acid-labile protecting groups for the synthesis of lipidated peptides. Chem. Eur. J. 2001; 7: 1184.
215. Millington CR, Quarrell R, Lowe G,. Aryl hydrazides as linkers for solid phase synthesis which are cleavable under mild oxidative conditions. Tetrahedron Lett. 1998; 39: 7201.
216. Diaz-Rodriguez V, Mullen DG, Ganusova E, Becker JM, Distefano MD,. Synthesis of peptides containing C-terminal methyl esters using trityl side-chain anchoring: application to the synthesis of a-factor and a-factor analogs. Org. Lett. 2012; 14: 5648.
217. Paik WK, Paik DC, Kim S,. Historical review: the field of protein methylation. Trends Biochem. Sci. 2007; 32: 146.
218. Tian X, Fang J,. Current perspectives on histone demethylases. Acta Biochim. Biophys. Sin. 2007; 39: 81.
219. Clarke SG,. Protein methylation at the surface and buried deep: thinking outside the histone box. Trends Biochem. Sci. 2013; 38: 243.
220. Bedford MT, Clarke SG,. Protein arginine methylation in mammals: who, what, and why. Mol. Cell 2009; 33: 1.
221. Martin C, Zhang Y,. The diverse functions of histone lysine methylation. Nat. Rev. Mol. Cell Biol. 2005; 6: 838.
222. Chirivi RG, Jenniskens GJ, Raats JM,. Anti-citrullinated protein antibodies as novel therapeutic drugs in rheumatoid arthritis. J. Clin. Cell Immunol. 2013; 4: 2.
223. Dalziel M, Crispin M, Scanlan CN, Zitzmann N, Dwek RA,. Emerging principles for the therapeutic exploitation of glycosylation. Science 2014; 343: 1235681.
224. Culyba EK, Price JL, Hanson SR, Dhar A, Wong C-H, Gruebele M, Powers ET, Kelly JW,. Protein native-state stabilization by placing aromatic side chains in N-glycosylated reverse turns. Science 2011; 331: 571.
225. Piontek C, Varõn Silva D, Heinlein C, Pöhner C, Mezzato S, Ring P, Martin A, Schmid FX, Unverzagt C,. Semisynthesis of a homogeneous glycoprotein enzyme: ribonuclease C: part 2. Angew. Chem. Int. Ed. 2009; 48: 1941.
226. Aussedat B, Vohra Y, Park PK, Fernández-Tejada A, Alam SM, Dennison SM, Jaeger FH, Anasti K, Stewart S, Blinn JH,. Chemical synthesis of highly congested gp120 V1V2 N-glycopeptide antigens for potential HIV-1-directed vaccines. J. Am. Chem. Soc. 2013; 135: 13113.
227. Jamsson AM, Hilaire PMS, Meldal M, in Houben-Weyl Methods of Organic Synthesis, Synthesis of Peptides and Peptidomimetics, Vol. E22b (Eds.:, Goodman M, Felix A, Moroder L, Toniolo C,), Georg Thieme, Stuttgart, 2002, pp. 235.
228. Unverzagt C, Kajihara Y,. Chemical assembly of N-glycoproteins: a refined toolbox to address a ubiquitous posttranslational modification. Chem. Soc. Rev. 2013; 42: 4408.
229. Wang L-X, Amin MN,. Chemical and chemoenzymatic synthesis of glycoproteins for deciphering functions. Chem. Biol. 2014; 21: 51.
230. Okamoto R, Mandal K, Ling M, Luster AD, Kajihara Y, Kent SB,. Total chemical synthesis and biological activities of glycosylated and non-glycosylated forms of the chemokines CCL1 and Ser-CCL1. Angew. Chem. 2014; 126: 5288.
231. Wilson RM, Stockdill JL, Wu X, Li X, Vadola PA, Park PK, Wang P, Danishefsky SJ,. A fascinating journey into history: exploration of the world of isonitriles en route to complex amides. Angew. Chem. Int. Ed. 2012; 51: 2834.
232. Sharon N, Lis H, in Glycosciences: Status & Perspectives (Eds.:, Gabius H-J, Gabius S,), Chapman& Hall, Weinheim, 1997, pp. 133.
233. Sjölin P, Elofsson M, Kihlberg J,. Removal of acyl protective groups from glycopeptides: base does not epimerize peptide stereocenters, and β-elimination is slow. J. Org. Chem. 1996; 61: 560.
234. Takano Y, Kojima N, Nakahara Y, Hojo H, Nakahara Y,. Solid-phase synthesis of core 2 O-linked glycopeptide and its enzymatic sialylation. Tetrahedron 2003; 59: 8415.
235. Leppänen A, Mehta P, Ouyang Y-B, Ju T, Helin J, Moore KL, van Die I, Canfield WM, McEver RP, Cummings RD,. A novel glycosulfopeptide binds to P-selectin and inhibits leukocyte adhesion to P-selectin. J. Biol. Chem. 1999; 274: 24838.
236. Galan MC, Benito-Alifonso D, Watt GM,. Carbohydrate chemistry in drug discovery. Org. Biomol. Chem. 2011; 9: 3598.
237. Otvos L, Jr, Wroblewski K, Kollat E, Perczel A, Hollosi M, Fasman G, Ertl H, Thurin J,. Coupling strategies in solid-phase synthesis of glycopeptides. Pept. Res. 1988; 2: 362.
238. Otvos L, Urge L, Hollosi M, Wroblewski K, Graczyk G, Fasman GD, Thurin J,. Automated solid-phase synthesis of glycopeptides. Incorporation of unprotected mono-and disaccharide units of N-glycoprotein antennae into T cell epitopic peptides. Tetrahedron Lett. 1990; 31: 5889.
239. Cohen-Anisfeld ST, Lansbury PT, Jr,. A practical, convergent method for glycopeptide synthesis. J. Am. Chem. Soc. 1993; 115: 10531.
240. Vetter D, Tumelty D, Singh SK, Gallop MA,. A versatile solid-phase synthesis of N-linked glycopeptides. Angew. Chem. Int. Ed. 1995; 34: 60.
241. Hojo H, Kwon Y, Kakuta Y, Tsuda S, Tanaka I, Hikichi K, Aimoto S,. Development of a linker with an enhanced stability for the preparation of peptide thioesters and its application to the synthesis of a stable-isotope-labelled HU-type DNA-binding protein. Bull. Chem. Soc. Jpn. 1993; 66: 2700.
242. Hackeng TM, Griffin JH, Dawson PE,. Protein synthesis by native chemical ligation: expanded scope by using straightforward methodology. Proc. Natl. Acad. Sci. 1999; 96: 10068.
243. Clippingdale AB, Barrow CJ, Wade JD,. Peptide thioester preparation by Fmoc solid phase peptide synthesis for use in native chemical ligation. J. Pept. Sci. 2000; 6: 225.
244. Ingenito R, Bianchi E, Fattori D, Pessi A,. Solid phase synthesis of peptide C-terminal thioesters by Fmoc/t-Bu chemistry. J. Am. Chem. Soc. 1999; 121: 11369.
245. Hiedler P, Link A,. N-Acyl-N-alkyl-sulfonamide anchors derived from Kenner's safety catch linker: powerful tools in bioorganic and medicinal chemistry. Biorg. Med. Chem. 2005; 13: 585.
246. Mende F, Beisswenger M, Seitz O,. Automated Fmoc-based solid-phase synthesis of peptide thioesters with self-purification effect and application in the construction of immobilized SH3 domains. J. Am. Chem. Soc. 2010; 132: 11110.
247. Macmillan D, Bertozzi CR,. Modular assembly of glycoproteins: towards the synthesis of GlyCAM-1 by using expressed protein ligation. Angew. Chem. 2004; 116: 1379.
248. Flavell RR, Huse M, Goger M, Trester-Zedlitz M, Kuriyan J, Muir TW,. Efficient semisynthesis of a tetraphosphorylated analogue of the type I TGFβ receptor. Org. Lett. 2002; 4: 165.
249. Burlina F, Morris C, Behrendt R, White P, Offer J,. Simplifying native chemical ligation with an N-acylsulfonamide linker. Chem. Commun. 2012; 48: 2579.
250. Blanco-Canosa JB, Dawson PE,. An efficient Fmoc-SPPS approach for the generation of thioester peptide precursors for use in native chemical ligation. Angew. Chem. Int. Ed. 2008; 47: 6851.
251. Pascal R, Chauvey D, Sola R,. Carboxyl-protecting groups convertible into activating groups. Carbamates of O-aminoanilides are precursors of reactive N-acyl ureas. Tetrahedron Lett. 1994; 35: 6291.
252. Pascal R, Sola R, Labéguère F, Jouin P,. Synthesis of the novel amino acid 4-amino-3-(aminomethyl) benzoic acid (AmAbz) and its protected derivatives as building blocks for pseudopeptide synthesis. Eur. J. Org. Chem. 2000; 2000: 3755.
253. Blanco-Canosa JB, Nardone B, Albericio F, Dawson PE,. Chemical protein synthesis using a second-generation N-acyl urea linker for the preparation of peptide-thioester precursors. J. Am. Chem. Soc. 2015; 137: 7197.
254. Meienhofer J, in The Peptides Analysis, Synthesis, Biology, Vol. 1 (Eds.:, Meienhofer J, Gross E,), Academic Press: NY, 1979, pp. 197.
255. Zheng J-S, Tang S, Huang Y-C, Liu L,. Development of new thioester equivalents for protein chemical synthesis. Acc. Chem. Res. 2013; 46: 2475.
256. Zheng J-S, Tang S, Qi Y-K, Wang Z-P, Liu L,. Chemical synthesis of proteins using peptide hydrazides as thioester surrogates. Nat. Protoc. 2013; 8: 2483.
257. Reif A, Siebenhaar S, Tröster A, Schmälzlein M, Lechner C, Velisetty P, Gottwald K, Pöhner C, Boos I, Schubert V,. Semisynthesis of biologically active glycoforms of the human cytokine interleukin 6. Angew. Chem. Int. Ed. 2014; 53: 12125.
258. Siman P, Karthikeyan SV, Nikolov M, Fischle W, Brik A,. Convergent chemical synthesis of histone H2B protein for the site-specific ubiquitination at Lys34. Angew. Chem. Int. Ed. 2013; 52: 8059.
259. Adams AL, Cowper B, Morgan RE, Premdjee B, Caddick S, Macmillan D,. Cysteine promoted C-terminal hydrazinolysis of native peptides and proteins. Angew. Chem. Int. Ed. 2013; 52: 13062.
260. Kang J, Richardson JP, Macmillan D,. 3-Mercaptopropionic acid-mediated synthesis of peptide and protein thioesters. Chem. Commun. 2009; 4: 407.
261. Offer J,. Native chemical ligation with Nα acyl transfer auxiliaries. Pept. Sci. 2010; 94: 530.
262. Kawakami T, Sumida M, Vorherr T, Aimoto S,. Peptide thioester preparation based on an N-S acyl shift reaction mediated by a thiol ligation auxiliary. Tetrahedron Lett. 2005; 46: 8805.
263. Szabõ J, Vinkler E, Varga I,. Chemical properties of 4H-benzo [e]-1,3-thiazine derivatives. I. Hydrolysis of 2-phenyl-6,7-dimethoxy-4H-benzo [e]-1,3-thiazine. Acta Chim. Acad. Sci. Hung. 1968; 58: 179.
264. Nakamura K, Kanao T, Uesugi T, Hara T, Sato T, Kawakami T, Aimoto S,. Synthesis of peptide thioesters via an N-S acyl shift reaction under mild acidic conditions on an N-4, 5-dimethoxy-2-mercaptobenzyl auxiliary group. J. Pept. Sci. 2009; 15: 731.
265. Hojo H, Onuma Y, Akimoto Y, Nakahara Y, Nakahara Y,. N-Alkyl cysteine-assisted thioesterification of peptides. Tetrahedron Lett. 2007; 48: 25.
266. Kang J, Macmillan D,. Peptide and protein thioester synthesis via N → S acyl transfer. Org. Biomol. Chem. 2010; 8: 1993.
267. Botti P, Villain M, Manganiello S, Gaertner H,. Native chemical ligation through in situ O to S acyl shift. Org. Lett. 2004; 6: 4861.
268. Johnson EC, Kent SB,. Insights into the mechanism and catalysis of the native chemical ligation reaction. J. Am. Chem. Soc. 2006; 128: 6640.
269. Ollivier N, Dheur J, Mhidia R, Blanpain A, Melnyk O,. Bis (2-sulfanylethyl) amino native peptide ligation. Org. Lett. 2010; 12: 5238.
270. Boll E, Drobecq H, Ollivier N, Blanpain A, Raibaut L, Desmet R, Vicogne J, Melnyk O,. One-pot chemical synthesis of small ubiquitin-like modifier protein-peptide conjugates using bis (2-sulfanylethyl) amido peptide latent thioester surrogates. Nat. Protoc. 2015; 10: 269.
271. Tsuda S, Shigenaga A, Bando K, Otaka A,. N → S acyl-transfer-mediated synthesis of peptide thioesters using anilide derivatives. Org. Lett. 2009; 11: 823.
272. Sato K, Shigenaga A, Tsuji K, Tsuda S, Sumikawa Y, Sakamoto K, Otaka A,. N-Sulfanylethylanilide peptide as a crypto-thioester peptide. ChemBioChem 1840; 2011: 12.
273. Sato K, Shigenaga A, Kitakaze K, Sakamoto K, Tsuji D, Itoh K, Otaka A,. Chemical synthesis of biologically active monoglycosylated GM2-activator protein analogue using N-sulfanylethylanilide peptide. Angew. Chem. Int. Ed. 2013; 125: 8009.
274. Cowper B, Shariff L, Chen W, Gibson SM, Di W-L, Macmillan D,. Expanding the scope of N → S acyl transfer in native peptide sequences. Org. Biomol. Chem. 2015; 13: 7469.
275. Terrier VP, Adihou H, Arnould M, Delmas AF, Aucagne V,. A straightforward method for automated Fmoc-based synthesis of bio-inspired peptide crypto-thioesters. Chem. Sci 2015. DOI: 10.1039/C5SC02630J.
276. Ruff Y, Garavini V, Giuseppone N,. Reversible native chemical ligation: a facile access to dynamic covalent peptides. J. Am. Chem. Soc. 2014; 136: 6333.
277. Yu HM, Chen ST, Wang KT,. Enhanced coupling efficiency in solid-phase peptide synthesis by microwave irradiation. J. Org. Chem. 1992; 57: 4781.
278. Pedersen SL, Tofteng AP, Malik L, Jensen KJ,. Microwave heating in solid-phase peptide synthesis. Chem. Soc. Rev. 2012; 41: 1826.
279. Echalier C, Al-Halifa S, Kreiter A, Enjalbal C, Sanchez P, Ronga L, Puget K, Verdié P, Amblard M, Martinez J,. Heating and microwave assisted SPPS of C-terminal acid peptides on trityl resin: the truth behind the yield. Amino Acids 2013; 45: 1395.
280. Yang X, Lin H, Lu W, Wang D,. Compatibility study of Merrifield linker in Fmoc strategy peptide synthesis. Prot. Pept. Lett. 2013; 20: 140.
281. Loffredo C, Assuncao NA, Gerhardt J, Miranda M,. Microwave-assisted solid-phase peptide synthesis at 60 'C: alternative conditions with low enantiomerization. J. Pept. Sci. 2009; 15: 808.
282. Bacsa B, Horváti K, Bõsze S, Andreae F, Kappe CO,. Solid-phase synthesis of difficult peptide sequences at elevated temperatures: a critical comparison of microwave and conventional heating technologies. J. Org. Chem. 2008; 73: 7532.
283. Bacsa B, Bsze S, Kappe CO,. Direct solid-phase synthesis of the β-amyloid (1-42) peptide using controlled microwave heating. J. Org. Chem. 2010; 75: 2103.
284. Roodbeen R, Pedersen SL, Hosseini M, Jensen KJ,. Microwave heating in the solid-phase synthesis of N-methylated peptides: when is room temperature better? Eur. J. Org. Chem. 2012; 2012: 7106.
285. Nissen F, Kraft TE, Ruppert T, Eisenhut M, Haberkorn U, Mier W,. Hot or not-the influence of elevated temperature and microwave irradiation on the solid phase synthesis of an affibody. Tetrahedron Lett. 2010; 51: 6216.
286. Tofteng AP, Jensen KJ, Schäffer L, Hoeg-Jensen T,. Total synthesis of desB30 insulin analogues by biomimetic folding of single-chain precursors. ChemBioChem 2008; 9: 2989.
287. Marek P, Woys AM, Sutton K, Zanni MT, Raleigh DP,. Efficient microwave-assisted synthesis of human islet amyloid polypeptide designed to facilitate the specific incorporation of labeled amino acids. Org. Lett. 2010; 12: 4848.
288. Harris PWR, Kowalczyk R, Hay DL, Brimble MA,. A single pseudoproline and microwave solid phase peptide synthesis facilitates an efficient synthesis of human amylin 1-37. Int. J. Pept. Res. Ther. 2013; 19: 147.