20
1 Introduction
33. Hill TA, Shepherd NE, Diness F, Fairlie DP (2014) Constraining cyclic peptides to mimic
protein structure motifs. Angew Chem Int Ed 53:13020–13041
34. Walensky LD, Bird GH (2014) Hydrocarbon-stapled peptides: principles, practice, and
progress. J Med Chem 57:6275–6288
35. Lau YH, De Andrade P, Wu YT, Spring DR (2015) Peptide stapling techniques based on
different macrocyclisation chemistries. Chem Soc Rev 44:91–102
36. Nero TL, Morton CJ, Holien JK, Wielens J, Parker MW (2014) Oncogenic protein interfaces:
small molecules, big challenges. Nat Rev Cancer 14:248–262
37. Góngora-Benítez M, Tulla-Puche J, Albericio F (2014) Multifaceted roles of disulfide bonds.
peptides as therapeutics. Chem Rev 114:901–926
38. Cromm PM, Spiegel J, Grossmann TN (2015) Hydrocarbon stapled peptides as modulators
of biological function. ACS Chem Biol 10:1362–1375
39. Tan YS, Lane DP, Verma CS (2016) Stapled peptide design: principles and roles of
computation. Drug Discov, Today
40. Xie X, Gao L, Shull AY, Teng Y (2016) Stapled peptides: providing the best of both worlds
in drug development. Future Med Chem 8:1969–1980
41. Milroy L-G, Grossmann TN, Hennig S, Brunsveld L, Ottmann C (2014) Modulators of proteinprotein interactions. Chem Rev 114:4695–4748
42. Nevola L, Giralt E (2015) Modulating protein-protein interactions: the potential of peptides.
Chem Commun 51:3302–3315
43. Sperandio O, Reynès CH, Camproux A-C, Villoutreix BO (2010) Rationalizing the chemical
space of protein–protein interaction inhibitors. Drug Discov Today 15:220–229
44. Ramachandran GN, Sasisekharan V (1968) Conformation of polypeptides and proteins**The
literature survey for this review was completed in September 1967, with the journals which
were then available in Madras and the preprinta which the authors had received.††By the
authors’ request, the publishers have left certain matters of usage and spelling in the form in
which they wrote them. Adv Protein Chem 23:283–437
45. Chou PY, Fasman GD (1977) β-turns in proteins. J Mol Biol 115:135–175
46. Koch O, Klebe G (2009) Turns revisited: a uniform and comprehensive classification of
normal, open, and reverse turn families minimizing unassigned random chain portions.
Proteins: Struct, Funct, Bioinform 74:353–367
47. Pelay-Gimeno M, Glas A, Koch O, Grossmann TN (2015) Structure-based design of inhibitors
of protein-protein interactions: mimicking peptide binding epitopes. Angew Chem Int Ed Engl
54:8896–8927
48. Sozzani P, Comotti A, Bracco S, Simonutti R (2004) A family of supramolecular frameworks
of polyconjugated molecules hosted in aromatic nanochannels. Angew Chem Int Ed 43:2792–
2797
49. Banerjee R, Basu G, Chene P, Roy S (2002) Aib-based peptide backbone as scaffolds for
helical peptide mimics. J Pept Res 60:88–94
50. Phelan JC, Skelton NJ, Braisted AC, McDowell RS (1997) A general method for constraining
short peptides to an α-helical conformation. J Am Chem Soc 119:455–460
51. Chorev M, Roubini E, McKee RL, Gibbons SW, Goldman ME, Caulfield MP, Rosenblatt M
(1991) Cyclic parathyroid hormone related protein antagonists: lysine 13 to aspartic acid 17
[i to (i + 4)] side chain to side chain lactamization. Biochem 30:5968–5974
52. Kutchukian PS, Yang JS, Verdine GL, Shakhnovich EI (2009) All-atom model for stabilization
of α-helical structure in peptides by hydrocarbon staples. J Am Chem Soc 131:4622–4627
53. Jo H, Meinhardt N, Wu Y, Kulkarni S, Hu X, Low KE, Davies PL, DeGrado WF, Greenbaum
DC (2012) Development of α-helical calpain probes by mimicking a natural protein-protein
interaction. J Am Chem Soc 134:17704–17713
54. Muppidi A, Wang Z, Li X, Chen J, Lin Q (2011) Achieving cell penetration with distancematching cysteine cross-linkers: a facile route to cell-permeable peptide dual inhibitors of
Mdm2/Mdmx. Chem Commun 47:9396–9398
55. Muppidi A, Doi K, Edwardraja S, Drake EJ, Gulick AM, Wang H-G, Lin Q (2012) Rational
design of proteolytically stable, cell-permeable peptide-based selective Mcl-1 inhibitors. J
Am Chem Soc 134:14734–14737
1 Introduction
33. Hill TA, Shepherd NE, Diness F, Fairlie DP (2014) Constraining cyclic peptides to mimic
protein structure motifs. Angew Chem Int Ed 53:13020–13041
34. Walensky LD, Bird GH (2014) Hydrocarbon-stapled peptides: principles, practice, and
progress. J Med Chem 57:6275–6288
35. Lau YH, De Andrade P, Wu YT, Spring DR (2015) Peptide stapling techniques based on
different macrocyclisation chemistries. Chem Soc Rev 44:91–102
36. Nero TL, Morton CJ, Holien JK, Wielens J, Parker MW (2014) Oncogenic protein interfaces:
small molecules, big challenges. Nat Rev Cancer 14:248–262
37. Góngora-Benítez M, Tulla-Puche J, Albericio F (2014) Multifaceted roles of disulfide bonds.
peptides as therapeutics. Chem Rev 114:901–926
38. Cromm PM, Spiegel J, Grossmann TN (2015) Hydrocarbon stapled peptides as modulators
of biological function. ACS Chem Biol 10:1362–1375
39. Tan YS, Lane DP, Verma CS (2016) Stapled peptide design: principles and roles of
computation. Drug Discov, Today
40. Xie X, Gao L, Shull AY, Teng Y (2016) Stapled peptides: providing the best of both worlds
in drug development. Future Med Chem 8:1969–1980
41. Milroy L-G, Grossmann TN, Hennig S, Brunsveld L, Ottmann C (2014) Modulators of proteinprotein interactions. Chem Rev 114:4695–4748
42. Nevola L, Giralt E (2015) Modulating protein-protein interactions: the potential of peptides.
Chem Commun 51:3302–3315
43. Sperandio O, Reynès CH, Camproux A-C, Villoutreix BO (2010) Rationalizing the chemical
space of protein–protein interaction inhibitors. Drug Discov Today 15:220–229
44. Ramachandran GN, Sasisekharan V (1968) Conformation of polypeptides and proteins**The
literature survey for this review was completed in September 1967, with the journals which
were then available in Madras and the preprinta which the authors had received.††By the
authors’ request, the publishers have left certain matters of usage and spelling in the form in
which they wrote them. Adv Protein Chem 23:283–437
45. Chou PY, Fasman GD (1977) β-turns in proteins. J Mol Biol 115:135–175
46. Koch O, Klebe G (2009) Turns revisited: a uniform and comprehensive classification of
normal, open, and reverse turn families minimizing unassigned random chain portions.
Proteins: Struct, Funct, Bioinform 74:353–367
47. Pelay-Gimeno M, Glas A, Koch O, Grossmann TN (2015) Structure-based design of inhibitors
of protein-protein interactions: mimicking peptide binding epitopes. Angew Chem Int Ed Engl
54:8896–8927
48. Sozzani P, Comotti A, Bracco S, Simonutti R (2004) A family of supramolecular frameworks
of polyconjugated molecules hosted in aromatic nanochannels. Angew Chem Int Ed 43:2792–
2797
49. Banerjee R, Basu G, Chene P, Roy S (2002) Aib-based peptide backbone as scaffolds for
helical peptide mimics. J Pept Res 60:88–94
50. Phelan JC, Skelton NJ, Braisted AC, McDowell RS (1997) A general method for constraining
short peptides to an α-helical conformation. J Am Chem Soc 119:455–460
51. Chorev M, Roubini E, McKee RL, Gibbons SW, Goldman ME, Caulfield MP, Rosenblatt M
(1991) Cyclic parathyroid hormone related protein antagonists: lysine 13 to aspartic acid 17
[i to (i + 4)] side chain to side chain lactamization. Biochem 30:5968–5974
52. Kutchukian PS, Yang JS, Verdine GL, Shakhnovich EI (2009) All-atom model for stabilization
of α-helical structure in peptides by hydrocarbon staples. J Am Chem Soc 131:4622–4627
53. Jo H, Meinhardt N, Wu Y, Kulkarni S, Hu X, Low KE, Davies PL, DeGrado WF, Greenbaum
DC (2012) Development of α-helical calpain probes by mimicking a natural protein-protein
interaction. J Am Chem Soc 134:17704–17713
54. Muppidi A, Wang Z, Li X, Chen J, Lin Q (2011) Achieving cell penetration with distancematching cysteine cross-linkers: a facile route to cell-permeable peptide dual inhibitors of
Mdm2/Mdmx. Chem Commun 47:9396–9398
55. Muppidi A, Doi K, Edwardraja S, Drake EJ, Gulick AM, Wang H-G, Lin Q (2012) Rational
design of proteolytically stable, cell-permeable peptide-based selective Mcl-1 inhibitors. J
Am Chem Soc 134:14734–14737