References
21
56. Muppidi A, Zhang HT, Curreli F, Li N, Debnath AK, Lin Q (2014) Design of antiviral stapled
peptides containing a biphenyl cross-linker. Bioorg Med Chem Lett 24:1748–1751
57. Wang Y, Chou DH-C (2015) A thiol–ene coupling approach to native peptide stapling and
macrocyclization. Angew Chem Int Ed n/a-n/a
58. Spokoyny AM, Zou YK, Ling JJ, Yu HT, Lin YS, Pentelute BL (2013) A perfluoroaryl-cysteine
snar chemistry approach to unprotected peptide stapling. J Am Chem Soc 135:5946–5949
59. Vinogradov AA, Choo ZN, Totaro KA, Pentelute BL (2016) Macrocyclization of unprotected
peptide isocyanates. Org Lett 18:1226–1229
60. Lau YH, de Andrade P, McKenzie GJ, Venkitaraman AR, Spring DR (2014) Linear
aliphatic dialkynes as alternative linkers for double-click stapling of p53-derived peptides.
ChemBioChem 15:2680–2683
61. Lau YH, de Andrade P, Skold N, McKenzie GJ, Venkitaraman AR, Verma C, Lanef DP, Spring
DR (2014) Investigating peptide sequence variations for ‘double-click’ stapled p53 peptides.
Org Biomol Chem 12:4074–4077
62. Lau YH, Wu YT, Rossmann M, Tan BX, de Andrade P, Tan YS, Verma C, McKenzie GJ,
Venkitaraman AR, Hyvonen M, Spring DR (2015) Double strain-promoted macrocyclization
for the rapid selection of cell-active stapled peptides. Angew Chem Int Edit 54:15410–15413
63. Hu K, Geng H, Zhang Q, Liu Q, Xie M, Sun C, Li W, Lin H, Jiang F, Wang T, Wu Y-D, Li Z
(2016) An in-tether chiral center modulates the helicity, cell permeability, and target binding
affinity of a peptide. Angew Chem Int Ed 55:8013–8017
64. Hou Z, Sun C, Geng H, Hu K, Xie M, Ma Y, Jiang F, Yin F, Li Z (2018) Facile chemoselective
modification of thio-ethers generates chiral center-induced helical peptides. Bioconjug Chem
29:2904–2908
65. Hu K, Sun C, Li Z (2017) Reversible and versatile on-tether modification of chiral-centerinduced helical peptides. Bioconjug Chem 28:2001–2007
66. Hu K, Sun C, Yu M, Li W, Lin H, Guo J, Jiang Y, Lei C, Li Z (2017) Dual in-tether chiral
centers modulate peptide helicity. Bioconjug Chem 28:1537–1543
67. Vasco AV, Pérez CS, Morales FE, Garay HE, Vasilev D, Gavín JA, Wessjohann LA, Rivera
DG (2015) Macrocyclization of peptide side chains by the ugi reaction: achieving peptide
folding and exocyclic n-functionalization in one shot. J Org Chem 80:6697–6707
68. Assem N, Ferreira DJ, Wolan DW, Dawson PE (2015) Acetone-linked peptides: a convergent
approach for peptide macrocyclization and labeling. Angew Chem Int Ed 54:8665–8668
69. Martín-Quirós A, Nevola L, Eckelt K, Madurga S, Gorostiza P, Giralt E (2015) Absence of
a stable secondary structure is not a limitation for photoswitchable inhibitors of β-arrestin/βadaptin 2 protein-protein interaction. Chem Biol 22:31–37
70. Zhang F, Timm KA, Arndt KM, Woolley GA (2010) Photocontrol of coiled-coil proteins in
living cells. Angew Chem Int Ed 49:3943–3946
71. Bellotto S, Chen S, Rentero Rebollo I, Wegner HA, Heinis C (2014) Phage selection of
photoswitchable peptide ligands. J Am Chem Soc 136:5880–5883
72. Miller SE, Kallenbach NR, Arora PS (2012) Reversible α-helix formation controlled by a
hydrogen bond surrogate. Tetrahedron 68:4434–4437
73. Marqusee S, Baldwin RL (1987) Helix stabilization by Glu-…Lys + salt bridges in short
peptides of de novo design. Proceedings of the National Academy of Sciences 84:8898–8902
74. Jackson DY, King DS, Chmielewski J, Singh S, Schultz PG (1991) General approach to the
synthesis of short .alpha.-helical peptides. J Am Chem Soc 113:9391–9392
75. Toniolo C, Bonora GM, Bavoso A, Benedetti E, di Blasio B, Pavone V, Pedone C (1983)
Preferred conformations of peptides containing α, α-disubstituted α-amino acids. Biopolym
22:205–215
76. Schafmeister CE, Po J, Verdine GL (2000) An all-hydrocarbon cross-linking system for
enhancing the helicity and metabolic stability of peptides. J Am Chem Soc 122:5891–5892
77. Chen X-H, Xiang Z, Hu YS, Lacey VK, Cang H, Wang L (2014) Genetically encoding an
electrophilic amino acid for protein stapling and covalent binding to native receptors. ACS
Chem Biol 9:1956–1961
21
56. Muppidi A, Zhang HT, Curreli F, Li N, Debnath AK, Lin Q (2014) Design of antiviral stapled
peptides containing a biphenyl cross-linker. Bioorg Med Chem Lett 24:1748–1751
57. Wang Y, Chou DH-C (2015) A thiol–ene coupling approach to native peptide stapling and
macrocyclization. Angew Chem Int Ed n/a-n/a
58. Spokoyny AM, Zou YK, Ling JJ, Yu HT, Lin YS, Pentelute BL (2013) A perfluoroaryl-cysteine
snar chemistry approach to unprotected peptide stapling. J Am Chem Soc 135:5946–5949
59. Vinogradov AA, Choo ZN, Totaro KA, Pentelute BL (2016) Macrocyclization of unprotected
peptide isocyanates. Org Lett 18:1226–1229
60. Lau YH, de Andrade P, McKenzie GJ, Venkitaraman AR, Spring DR (2014) Linear
aliphatic dialkynes as alternative linkers for double-click stapling of p53-derived peptides.
ChemBioChem 15:2680–2683
61. Lau YH, de Andrade P, Skold N, McKenzie GJ, Venkitaraman AR, Verma C, Lanef DP, Spring
DR (2014) Investigating peptide sequence variations for ‘double-click’ stapled p53 peptides.
Org Biomol Chem 12:4074–4077
62. Lau YH, Wu YT, Rossmann M, Tan BX, de Andrade P, Tan YS, Verma C, McKenzie GJ,
Venkitaraman AR, Hyvonen M, Spring DR (2015) Double strain-promoted macrocyclization
for the rapid selection of cell-active stapled peptides. Angew Chem Int Edit 54:15410–15413
63. Hu K, Geng H, Zhang Q, Liu Q, Xie M, Sun C, Li W, Lin H, Jiang F, Wang T, Wu Y-D, Li Z
(2016) An in-tether chiral center modulates the helicity, cell permeability, and target binding
affinity of a peptide. Angew Chem Int Ed 55:8013–8017
64. Hou Z, Sun C, Geng H, Hu K, Xie M, Ma Y, Jiang F, Yin F, Li Z (2018) Facile chemoselective
modification of thio-ethers generates chiral center-induced helical peptides. Bioconjug Chem
29:2904–2908
65. Hu K, Sun C, Li Z (2017) Reversible and versatile on-tether modification of chiral-centerinduced helical peptides. Bioconjug Chem 28:2001–2007
66. Hu K, Sun C, Yu M, Li W, Lin H, Guo J, Jiang Y, Lei C, Li Z (2017) Dual in-tether chiral
centers modulate peptide helicity. Bioconjug Chem 28:1537–1543
67. Vasco AV, Pérez CS, Morales FE, Garay HE, Vasilev D, Gavín JA, Wessjohann LA, Rivera
DG (2015) Macrocyclization of peptide side chains by the ugi reaction: achieving peptide
folding and exocyclic n-functionalization in one shot. J Org Chem 80:6697–6707
68. Assem N, Ferreira DJ, Wolan DW, Dawson PE (2015) Acetone-linked peptides: a convergent
approach for peptide macrocyclization and labeling. Angew Chem Int Ed 54:8665–8668
69. Martín-Quirós A, Nevola L, Eckelt K, Madurga S, Gorostiza P, Giralt E (2015) Absence of
a stable secondary structure is not a limitation for photoswitchable inhibitors of β-arrestin/βadaptin 2 protein-protein interaction. Chem Biol 22:31–37
70. Zhang F, Timm KA, Arndt KM, Woolley GA (2010) Photocontrol of coiled-coil proteins in
living cells. Angew Chem Int Ed 49:3943–3946
71. Bellotto S, Chen S, Rentero Rebollo I, Wegner HA, Heinis C (2014) Phage selection of
photoswitchable peptide ligands. J Am Chem Soc 136:5880–5883
72. Miller SE, Kallenbach NR, Arora PS (2012) Reversible α-helix formation controlled by a
hydrogen bond surrogate. Tetrahedron 68:4434–4437
73. Marqusee S, Baldwin RL (1987) Helix stabilization by Glu-…Lys + salt bridges in short
peptides of de novo design. Proceedings of the National Academy of Sciences 84:8898–8902
74. Jackson DY, King DS, Chmielewski J, Singh S, Schultz PG (1991) General approach to the
synthesis of short .alpha.-helical peptides. J Am Chem Soc 113:9391–9392
75. Toniolo C, Bonora GM, Bavoso A, Benedetti E, di Blasio B, Pavone V, Pedone C (1983)
Preferred conformations of peptides containing α, α-disubstituted α-amino acids. Biopolym
22:205–215
76. Schafmeister CE, Po J, Verdine GL (2000) An all-hydrocarbon cross-linking system for
enhancing the helicity and metabolic stability of peptides. J Am Chem Soc 122:5891–5892
77. Chen X-H, Xiang Z, Hu YS, Lacey VK, Cang H, Wang L (2014) Genetically encoding an
electrophilic amino acid for protein stapling and covalent binding to native receptors. ACS
Chem Biol 9:1956–1961