Peptide stapling techniques based on different macrocyclisation chemistries

The growing applications of click chemistry

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Activation of Apoptosis in Vivo by a Hydrocarbon-Stapled BH3 Helix

Walensky, L. D., Kung, A. L., Escher, I., Malia, T. J., Barbuto, S., Wright, R. D., Wagner, G., Verdine, G. L., & Korsmeyer, S. J. (2004) · Science · doi:10.1126/science.1099191 · Cited by 1,349

Contemporary strategies for peptide macrocyclization

White, C. J., & Yudin, A. K. (2011) · Nature Chemistry · doi:10.1038/nchem.1062 · Cited by 1,088

An All-Hydrocarbon Cross-Linking System for Enhancing the Helicity and Metabolic Stability of Peptides

Schafmeister, C. E., Po, J., & Verdine, G. L. (2000) · Journal of the American Chemical Society · doi:10.1021/ja000563a · Cited by 1,037

Hydrocarbon-Stapled Peptides: Principles, Practice, and Progress: Miniperspective

Walensky, L. D., & Bird, G. H. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm4011675 · Cited by 795

Inhibition of α-helix-mediated protein–protein interactions using designed molecules

Azzarito, V., Long, K., Murphy, N. S., & Wilson, A. J. (2013) · Nature Chemistry · doi:10.1038/nchem.1568 · Cited by 727

Stapled α−helical peptide drug development: A potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy

Chang, Y. S., Graves, B., Guerlavais, V., Tovar, C., Packman, K., To, K.-H., Olson, K. A., Kesavan, K., Gangurde, P., Mukherjee, A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303002110 · Cited by 660

Highly Efficient Synthesis of Covalently Cross-Linked Peptide Helices by Ring-Closing Metathesis

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Reactivation of the p53 Tumor Suppressor Pathway by a Stapled p53 Peptide

Bernal, F., Tyler, A. F., Korsmeyer, S. J., Walensky, L. D., & Verdine, G. L. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0693587 · Cited by 556

A Perfluoroaryl-Cysteine S N Ar Chemistry Approach to Unprotected Peptide Stapling

Spokoyny, A. M., Zou, Y., Ling, J. J., Yu, H., Lin, Y.-S., & Pentelute, B. L. (2013) · Journal of the American Chemical Society · doi:10.1021/ja400119t · Cited by 474

Single Turn Peptide Alpha Helices with Exceptional Stability in Water

Shepherd, N. E., Hoang, H. N., Abbenante, G., & Fairlie, D. P. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0456003 · Cited by 326

General approach to the synthesis of short .alpha.-helical peptides

Jackson, D. Y., King, D. S., Chmielewski, J., Singh, S., & Schultz, P. G. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00024a067 · Cited by 313

Assessing Helical Protein Interfaces for Inhibitor Design

Bullock, B. N., Jochim, A. L., & Arora, P. S. (2011) · Journal of the American Chemical Society · doi:10.1021/ja206074j · Cited by 300

Photo-control of helix content in a short peptide

Kumita, J. R., Smart, O. S., & Woolley, G. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.8.3803 · Cited by 291

Development of α-Helical Calpain Probes by Mimicking a Natural Protein–Protein Interaction

Jo, H., Meinhardt, N., Wu, Y., Kulkarni, S., Hu, X., Low, K. E., Davies, P. L., DeGrado, W. F., & Greenbaum, D. C. (2012) · Journal of the American Chemical Society · doi:10.1021/ja307599z · Cited by 261

Design of Triazole-Stapled BCL9 α-Helical Peptides to Target the β-Catenin/B-Cell CLL/lymphoma 9 (BCL9) Protein–Protein Interaction

Kawamoto, S. A., Coleska, A., Ran, X., Yi, H., Yang, C.-Y., & Wang, S. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm201125d · Cited by 249

Helix-stabilized cyclic peptides as selective inhibitors of steroid receptor–coactivator interactions

Leduc, A.-M., Trent, J. O., Wittliff, J. L., Bramlett, K. S., Briggs, S. L., Chirgadze, N. Y., Wang, Y., Burris, T. P., & Spatola, A. F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1934759100 · Cited by 222

Synthesis, biological activity and conformational analysis of cyclic GRF analogs

FELIX, A. M., HEIMER, E. P., WANG, C., LAMBROS, T. J., FOURNIER, A., MOWLES, T. F., MAINES, S., CAMPBELL, R. M., WEGRZYNSKI, B. B., TOOME, V., et al. (1988) · International Journal of Peptide and Protein Research · doi:10.1111/j.1399-3011.1988.tb01375.x · Cited by 221

Functionalised staple linkages for modulating the cellular activity of stapled peptides

Lau, Y. H., de Andrade, P., Quah, S.-T., Rossmann, M., Laraia, L., Sköld, N., Sum, T. J., Rowling, P. J. E., Joseph, T. L., Verma, C., et al. (2014) · Chem. Sci. · doi:10.1039/c4sc00045e · Cited by 214

Stapled Peptides with Improved Potency and Specificity That Activate p53

Brown, C. J., Quah, S. T., Jong, J., Goh, A. M., Chiam, P. C., Khoo, K. H., Choong, M. L., Lee, M. A., Yurlova, L., Zolghadr, K., et al. (2013) · ACS Chemical Biology · doi:10.1021/cb3005148 · Cited by 209

The synthesis and study of side‐chain lactam‐bridged peptides

Taylor, J. W. (2002) · Peptide Science · doi:10.1002/bip.10203 · Cited by 190

Downsizing human, bacterial, and viral proteins to short water-stable alpha helices that maintain biological potency

Harrison, R. S., Shepherd, N. E., Hoang, H. N., Ruiz-Gómez, G., Hill, T. A., Driver, R. W., Desai, V. S., Young, P. R., Abbenante, G., & Fairlie, D. P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002498107 · Cited by 182

A General Method for Constraining Short Peptides to an α-Helical Conformation

Phelan, J. C., Skelton, N. J., Braisted, A. C., & McDowell, R. S. (1997) · Journal of the American Chemical Society · doi:10.1021/ja9611654 · Cited by 177

Comparative α‐Helicity of Cyclic Pentapeptides in Water

de Araujo, A. D., Hoang, H. N., Kok, W. M., Diness, F., Gupta, P., Hill, T. A., Driver, R. W., Price, D. A., Liras, S., & Fairlie, D. P. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201310245 · Cited by 174

Using an Azobenzene Cross-Linker to Either Increase or Decrease Peptide Helix Content upon Trans-to-Cis Photoisomerization

Flint, D. G., Kumita, J. R., Smart, O. S., & Woolley, G. A. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00109-6 · Cited by 167

Rational Design of Proteolytically Stable, Cell-Permeable Peptide-Based Selective Mcl-1 Inhibitors

Muppidi, A., Doi, K., Edwardraja, S., Drake, E. J., Gulick, A. M., Wang, H.-G., & Lin, Q. (2012) · Journal of the American Chemical Society · doi:10.1021/ja306864v · Cited by 156

Structure-Function Analysis of the Epitope for 4E10, a Broadly Neutralizing Human Immunodeficiency Virus Type 1 Antibody

Brunel, F. M., Zwick, M. B., Cardoso, R. M. F., Nelson, J. D., Wilson, I. A., Burton, D. R., & Dawson, P. E. (2006) · Journal of Virology · doi:10.1128/jvi.80.4.1680-1687.2006 · Cited by 137

Stabilizing the Pro-Apoptotic BimBH3 Helix (BimSAHB) Does Not Necessarily Enhance Affinity or Biological Activity

Okamoto, T., Zobel, K., Fedorova, A., Quan, C., Yang, H., Fairbrother, W. J., Huang, D. C. S., Smith, B. J., Deshayes, K., & Czabotar, P. E. (2013) · ACS Chemical Biology · doi:10.1021/cb3005403 · Cited by 136

CuI‐Catalyzed Azide–Alkyne Intramolecular i‐to‐(i+4) Side‐Chain‐to‐Side‐Chain Cyclization Promotes the Formation of Helix‐Like Secondary Structures

Scrima, M., Isaad, A. L. C., Rovero, P., Papini, A. M., Chorev, M., & Papini, A. M. (2009) · European Journal of Organic Chemistry · doi:10.1002/ejoc.200901157 · Cited by 120

Synthesis of constrained helical peptides by thioether ligation: application to analogs of gp41

Brunel, F. M., & Dawson, P. E. (2005) · Chemical Communications · doi:10.1039/b419015g · Cited by 108

Synthesis of cell-permeable stapled peptide dual inhibitors of the p53-Mdm2/Mdmx interactions via photoinduced cycloaddition

Madden, M. M., Muppidi, A., Li, Z., Li, X., Chen, J., & Lin, Q. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.01.004 · Cited by 104

Light‐Regulated Stapled Peptides to Inhibit Protein–Protein Interactions Involved in Clathrin‐Mediated Endocytosis

Nevola, L., Martín‐Quirós, A., Eckelt, K., Camarero, N., Tosi, S., Llobet, A., Giralt, E., & Gorostiza, P. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201303324 · Cited by 102

Stabilization of Folded Peptide and Protein Structures via Distance Matching with a Long, Rigid Cross-Linker

Zhang, F., Sadovski, O., Xin, S. J., & Woolley, G. A. (2007) · Journal of the American Chemical Society · doi:10.1021/ja075829t · Cited by 96

Photocontrollable Peptide‐Based Switches Target the Anti‐Apoptotic Protein Bcl‐xL

Kneissl, S., Loveridge, E. J., Williams, C., Crump, M. P., & Allemann, R. K. (2008) · ChemBioChem · doi:10.1002/cbic.200800502 · Cited by 93

Promoting peptide α-helix formation with dynamic covalent oxime side-chain cross-links

Haney, C. M., Loch, M. T., & Horne, W. S. (2011) · Chemical Communications · doi:10.1039/c1cc12010g · Cited by 86

Development of a Series of Cross‐Linking Agents that Effectively Stabilize α‐Helical Structures in Various Short Peptides

Fujimoto, K., Kajino, M., & Inoûye, M. (2007) · Chemistry - A European Journal · doi:10.1002/chem.200700843 · Cited by 71

Lactam-Stabilized Helical Analogues of the Analgesic μ-Conotoxin KIIIA

Khoo, K. K., Wilson, M. J., Smith, B. J., Zhang, M.-M., Gulyas, J., Yoshikami, D., Rivier, J., Bulaj, G. W., & Norton, R. S. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200839a · Cited by 65

Investigating peptide sequence variations for ‘double-click’ stapled p53 peptides

Lau, Y. H., de Andrade, P., Sköld, N., McKenzie, G. J., Venkitaraman, A. R., Verma, C. S., Lane, D. P., & Spring, D. R. (2014) · Organic & Biomolecular Chemistry · doi:10.1039/c4ob00742e · Cited by 62

Monosubstituted alkenyl amino acids for peptide “stapling”

Yeo, D. J., Warriner, S. L., & Wilson, A. J. (2013) · Chemical Communications · doi:10.1039/c3cc45231j · Cited by 56

Peptide Tertiary Structure Nucleation by Side‐Chain Crosslinking with Metal Complexation and Double “Click” Cycloaddition

Torres, O. B., Yüksel, D., Bernardina, M., Kumar, K., & Bong, D. T.-Y. (2008) · ChemBioChem · doi:10.1002/cbic.200800040 · Cited by 54

Stapled peptides in the p53 pathway: Computer simulations reveal novel interactions of the staples with the target protein

Joseph, T. L., Lane, D. P., & Verma, C. S. (2010) · Cell Cycle · doi:10.4161/cc.9.22.13816 · Cited by 49

Stapled Vasoactive Intestinal Peptide (VIP) Derivatives Improve VPAC2Agonism and Glucose-Dependent Insulin Secretion

Giordanetto, F., Revell, J. D., Knerr, L., Hostettler, M., Paunovic, A., Priest, C., Janefeldt, A., & Gill, A. L. (2013) · ACS Medicinal Chemistry Letters · doi:10.1021/ml400257h · Cited by 44

Novel Helix-Constrained Nociceptin Derivatives Are Potent Agonists and Antagonists of ERK Phosphorylation and Thermal Analgesia in Mice

Harrison, R. S., Ruiz‐Gómez, G., Hill, T. A., Chow, S. Y., Shepherd, N. E., Lohman, R., Abbenante, G., Hoang, H. N., & Fairlie, D. P. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm101139f · Cited by 40

Dynamic covalent side‐chain cross‐links via intermolecular oxime or hydrazone formation from bifunctional peptides and simple organic linkers

Haney, C. M., & Horne, W. S. (2014) · Journal of Peptide Science · doi:10.1002/psc.2596 · Cited by 38

From Peptides to Non‐Peptide Alpha‐Helix Inducers and Mimetics

Haridas, V. (2009) · European Journal of Organic Chemistry · doi:10.1002/ejoc.200900280 · Cited by 38

Synthesis of cell-permeable stapled BH3 peptide-based Mcl-1 inhibitors containing simple aryl and vinylaryl cross-linkers

Muppidi, A., Doi, K., Ramil, C. P., Wang, H., & Lin, Q. (2014) · Tetrahedron · doi:10.1016/j.tet.2014.05.104 · Cited by 32

Stabilisation of a short α‐helical VIP fragment by side chain to side chain cyclisation: a comparison of common cyclisation motifs by circular dichroism

Frankiewicz, Ł., Betti, C., Guillemyn, K., Tourwé, D., Jacquot, Y., & Ballet, S. (2013) · Journal of Peptide Science · doi:10.1002/psc.2515 · Cited by 21

Macrocyclic Peptides as Drug Candidates: Recent Progress and Remaining Challenges

Vinogradov, A. A., Yin, Y., & Suga, H. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.8b13178 · Cited by 848

A Comprehensive Review on Current Advances in Peptide Drug Development and Design

Lee, A. C.-L., Harris, J. L., Khanna, K. K., & Hong, J.-H. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20102383 · Cited by 686

Residue-Specific Peptide Modification: A Chemist’s Guide

deGruyter, J. N., Malins, L. R., & Baran, P. S. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00536 · Cited by 573

Organometallic palladium reagents for cysteine bioconjugation

Vinogradova, E. V., Zhang, C., Spokoyny, A. M., Pentelute, B. L., & Buchwald, S. L. (2015) · Nature · doi:10.1038/nature15739 · Cited by 502

Cell penetrating peptide: A potent delivery system in vaccine development

Hasannejad-Asl, B., Pooresmaeil, F., Takamoli, S., Dabiri, M., & Bolhassani, A. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1072685 · Cited by 40