22
1 Introduction
78. Leduc A-M, Trent JO, Wittliff JL, Bramlett KS, Briggs SL, Chirgadze NY, Wang Y, Burris TP,
Spatola AF (2003) Helix-stabilized cyclic peptides as selective inhibitors of steroid receptor–
coactivator interactions. Proc Natl Acad Sci 100:11273–11278
79. Galande AK, Bramlett KS, Trent JO, Burris TP, Wittliff JL, Spatola AF (2005) Potent
inhibitors of LXXLL-based protein-protein interactions. ChemBioChem 6:1991–1998
80. Galande AK, Bramlett KS, Burris TP, Wittliff JL, Spatola AF (2004) Thioether side
chain cyclization for helical peptide formation: inhibitors of estrogen receptor–coactivator
interactions. J Pept Res 63:297–302
81. Sia SK, Carr PA, Cochran AG, Malashkevich VN, Kim PS (2002) Short constrained peptides
that inhibit HIV-1 entry. Proc Natl Acad Sci 99:14664–14669
82. Harrison RS, Shepherd NE, Hoang HN, Ruiz-Gómez G, Hill TA, Driver RW, Desai VS, Young
PR, Abbenante G, Fairlie DP (2010) Downsizing human, bacterial, and viral proteins to short
water-stable alpha helices that maintain biological potency. Proc Natl Acad Sci 107:11686–
11691
83. Taylor JW (2002) The synthesis and study of side-chain lactam-bridged peptides. Pept Sci
66:49–75
84. Baskin JM, Prescher JA, Laughlin ST, Agard NJ, Chang PV, Miller IA, Lo A, Codelli JA,
Bertozzi CR (2007) Copper-free click chemistry for dynamic in vivo imaging. Proc Natl Acad
Sci 104:16793–16797
85. Cantel S, Le Chevalier Isaad A, Scrima M, Levy JJ, DiMarchi RD, Rovero P, Halperin JA,
D’Ursi AM, Papini AM, Chorev M (2008) Synthesis and conformational analysis of a cyclic
peptide obtained via i to i + 4 intramolecular side-chain to side-chain azide − alkyne 1,3dipolar cycloaddition. J Org Chem 73:5663–5674
86. Kawamoto SA, Coleska A, Ran X, Yi H, Yang C-Y, Wang S (2012) Design of triazolestapled BCL9 α-helical peptides to target the β-catenin/B-Cell CLL/lymphoma 9 (BCL9)
protein-protein interaction. J Med Chem 55:1137–1146
87. Torres O, Yüksel D, Bernardina M, Kumar K, Bong D (2008) Peptide tertiary structure nucleation by side-chain crosslinking with metal complexation and double “click” cycloaddition.
ChemBioChem 9:1701–1705
88. Lau YH, de Andrade P, Quah ST, Rossmann M, Laraia L, Skold N, Sum TJ, Rowling PJE,
Joseph TL, Verma C, Hyvonen M, Itzhaki LS, Venkitaraman AR, Brown CJ, Lane DP, Spring
DR (2014) Functionalised staple linkages for modulating the cellular activity of stapled
peptides. Chem Sci 5:1804–1809
89. Kim YW, Kutchukian PS, Verdine GL (2010) Introduction of all-hydrocarbon i, i + 3 staples
into alpha-Helices via ring-closing olefin metathesis. Org Lett 12:3046–3049
90. Shim SY, Kim YW, Verdine GL (2013) A new i, i + 3 peptide stapling system for alpha-helix
stabilization. Chem Biol Drug Des 82:635–642
91. Bird GH, Madani N, Perry AF, Princiotto AM, Supko JG, He XY, Gavathiotis E, Sodroski
JG, Walensky LD (2010) Hydrocarbon double-stapling remedies the proteolytic instability of
a lengthy peptide therapeutic. Proc Natl Acad Sci U S A 107:14093–14098
92. Hilinski GJ, Kim YW, Hong J, Kutchukian PS, Crenshaw CM, Berkovitch SS, Chang A, Ham
S, Verdine GL (2014) Stitched alpha-helical peptides via bis ring-closing metathesis. J Am
Chem Soc 136:12314–12322
93. Grossmann TN, Yeh JTH, Bowman BR, Chu Q, Moellering RE, Verdine GL (2012) Inhibition
of oncogenic Wnt signaling through direct targeting of beta-catenin. Proc Natl Acad Sci U S
A 109:17942–17947
94. Cui HK, Zhao B, Li YH, Guo Y, Hu H, Liu L, Chen YG (2013) Design of stapled alpha-helical
peptides to specifically activate Wnt/beta-catenin signaling. Cell Res 23:581–584
95. Aurora R, Rosee GD (1998) Helix capping. Protein Sci 7:21–38
96. Koch O, Cole J (2011) An automated method for consistent helix assignment using turn
information. Proteins: Struct, Funct, Bioinform 79:1416–1426
97. Penel S, Hughes E, Doig AJ (1999) Side-chain structures in the first turn of the α-helix1. J
Mol Biol 287:127–143
1 Introduction
78. Leduc A-M, Trent JO, Wittliff JL, Bramlett KS, Briggs SL, Chirgadze NY, Wang Y, Burris TP,
Spatola AF (2003) Helix-stabilized cyclic peptides as selective inhibitors of steroid receptor–
coactivator interactions. Proc Natl Acad Sci 100:11273–11278
79. Galande AK, Bramlett KS, Trent JO, Burris TP, Wittliff JL, Spatola AF (2005) Potent
inhibitors of LXXLL-based protein-protein interactions. ChemBioChem 6:1991–1998
80. Galande AK, Bramlett KS, Burris TP, Wittliff JL, Spatola AF (2004) Thioether side
chain cyclization for helical peptide formation: inhibitors of estrogen receptor–coactivator
interactions. J Pept Res 63:297–302
81. Sia SK, Carr PA, Cochran AG, Malashkevich VN, Kim PS (2002) Short constrained peptides
that inhibit HIV-1 entry. Proc Natl Acad Sci 99:14664–14669
82. Harrison RS, Shepherd NE, Hoang HN, Ruiz-Gómez G, Hill TA, Driver RW, Desai VS, Young
PR, Abbenante G, Fairlie DP (2010) Downsizing human, bacterial, and viral proteins to short
water-stable alpha helices that maintain biological potency. Proc Natl Acad Sci 107:11686–
11691
83. Taylor JW (2002) The synthesis and study of side-chain lactam-bridged peptides. Pept Sci
66:49–75
84. Baskin JM, Prescher JA, Laughlin ST, Agard NJ, Chang PV, Miller IA, Lo A, Codelli JA,
Bertozzi CR (2007) Copper-free click chemistry for dynamic in vivo imaging. Proc Natl Acad
Sci 104:16793–16797
85. Cantel S, Le Chevalier Isaad A, Scrima M, Levy JJ, DiMarchi RD, Rovero P, Halperin JA,
D’Ursi AM, Papini AM, Chorev M (2008) Synthesis and conformational analysis of a cyclic
peptide obtained via i to i + 4 intramolecular side-chain to side-chain azide − alkyne 1,3dipolar cycloaddition. J Org Chem 73:5663–5674
86. Kawamoto SA, Coleska A, Ran X, Yi H, Yang C-Y, Wang S (2012) Design of triazolestapled BCL9 α-helical peptides to target the β-catenin/B-Cell CLL/lymphoma 9 (BCL9)
protein-protein interaction. J Med Chem 55:1137–1146
87. Torres O, Yüksel D, Bernardina M, Kumar K, Bong D (2008) Peptide tertiary structure nucleation by side-chain crosslinking with metal complexation and double “click” cycloaddition.
ChemBioChem 9:1701–1705
88. Lau YH, de Andrade P, Quah ST, Rossmann M, Laraia L, Skold N, Sum TJ, Rowling PJE,
Joseph TL, Verma C, Hyvonen M, Itzhaki LS, Venkitaraman AR, Brown CJ, Lane DP, Spring
DR (2014) Functionalised staple linkages for modulating the cellular activity of stapled
peptides. Chem Sci 5:1804–1809
89. Kim YW, Kutchukian PS, Verdine GL (2010) Introduction of all-hydrocarbon i, i + 3 staples
into alpha-Helices via ring-closing olefin metathesis. Org Lett 12:3046–3049
90. Shim SY, Kim YW, Verdine GL (2013) A new i, i + 3 peptide stapling system for alpha-helix
stabilization. Chem Biol Drug Des 82:635–642
91. Bird GH, Madani N, Perry AF, Princiotto AM, Supko JG, He XY, Gavathiotis E, Sodroski
JG, Walensky LD (2010) Hydrocarbon double-stapling remedies the proteolytic instability of
a lengthy peptide therapeutic. Proc Natl Acad Sci U S A 107:14093–14098
92. Hilinski GJ, Kim YW, Hong J, Kutchukian PS, Crenshaw CM, Berkovitch SS, Chang A, Ham
S, Verdine GL (2014) Stitched alpha-helical peptides via bis ring-closing metathesis. J Am
Chem Soc 136:12314–12322
93. Grossmann TN, Yeh JTH, Bowman BR, Chu Q, Moellering RE, Verdine GL (2012) Inhibition
of oncogenic Wnt signaling through direct targeting of beta-catenin. Proc Natl Acad Sci U S
A 109:17942–17947
94. Cui HK, Zhao B, Li YH, Guo Y, Hu H, Liu L, Chen YG (2013) Design of stapled alpha-helical
peptides to specifically activate Wnt/beta-catenin signaling. Cell Res 23:581–584
95. Aurora R, Rosee GD (1998) Helix capping. Protein Sci 7:21–38
96. Koch O, Cole J (2011) An automated method for consistent helix assignment using turn
information. Proteins: Struct, Funct, Bioinform 79:1416–1426
97. Penel S, Hughes E, Doig AJ (1999) Side-chain structures in the first turn of the α-helix1. J
Mol Biol 287:127–143