α,β-Unsaturated γ-Peptide Foldamers
Corresponding Author
Dr. Baptiste Legrand
Institut des Biomolécules Max Mousseron, IBMM, University of Montpellier, ENSCM, CNRS, Montpellier, France., 15 Av. Charles Flahault BP 14 491, 34093 Montpellier Cedex 5, France
Search for more papers by this authorCorresponding Author
Dr. Ludovic T. Maillard
Institut des Biomolécules Max Mousseron, IBMM, University of Montpellier, ENSCM, CNRS, Montpellier, France., 15 Av. Charles Flahault BP 14 491, 34093 Montpellier Cedex 5, France
Search for more papers by this authorCorresponding Author
Dr. Baptiste Legrand
Institut des Biomolécules Max Mousseron, IBMM, University of Montpellier, ENSCM, CNRS, Montpellier, France., 15 Av. Charles Flahault BP 14 491, 34093 Montpellier Cedex 5, France
Search for more papers by this authorCorresponding Author
Dr. Ludovic T. Maillard
Institut des Biomolécules Max Mousseron, IBMM, University of Montpellier, ENSCM, CNRS, Montpellier, France., 15 Av. Charles Flahault BP 14 491, 34093 Montpellier Cedex 5, France
Search for more papers by this authorGraphical Abstract
Foldamer science has far highlighted the use of pre-organized scaffolds to impose a strict control of the backbone torsional angles and stabilize discrete secondary structures. In this context, oligomers with α,β-unsaturated γ-amino acids have attracted attention because of their conformational stability in both organic solvent and aqueous medium. This Review provides a comprehensive overview of α,β-unsaturated γ-peptide foldamers.
Abstract
Despite their concomitant emergence in the 1990s, γ-peptide foldamers have not developed as fast as β-peptide foldamers and to date, only a few γ-oligomer structures have been reported, and with sparse applications. Among these examples, sequences containing α,β-unsaturated γ-amino acids have recently drawn attention since the Z/E configurations of the double bond provide opposite planar restrictions leading to divergent conformational behaviors, from helix to extended structures. In this Review, we give a comprehensive overview of the developments of γ-peptide foldamers containing α,β-unsaturated γ-amino acids with examples of applications for health and catalysis, as well as materials science.
Conflict of interest
The authors declare no conflict of interest.
References
- 1
- 1aD. J. Hill, M. J. Mio, R. B. Prince, T. S. Hughes, J. S. Moore, Chem. Rev. 2001, 101, 3893–4012;
- 1bS. H. Gellman, Acc. Chem. Res. 1998, 31, 173–180;
- 1cG. Guichard, I. Huc, Chem. Commun. 2011, 47, 5933–5941;
- 1dC. M. Goodman, S. Choi, S. Shandler, W. F. DeGrado, Nat. Chem. Biol. 2007, 3, 252–262;
- 1eS. H. Yoo, H. S. Lee, Acc. Chem. Res. 2017, 50, 832–841.
- 2
- 2aP. G. Vasudev, S. Chatterjee, N. Shamala, P. Balaram, Chem. Rev. 2011, 111, 657–687;
- 2bT. A. Martinek, F. Fulop, Chem. Soc. Rev. 2012, 41, 687–702;
- 2cF. Bouillere, S. Thetiot-Laurent, C. Kouklovsky, V. Alezra, Amino Acids 2011, 41, 687–707.
- 3
- 3aP. Armand, K. Kirshenbaum, R. A. Goldsmith, S. Farr-Jones, A. E. Barron, K. T. V. Truong, K. A. Dill, D. F. Mierke, F. E. Cohen, R. N. Zuckermann, E. K. Bradley, Proc. Natl. Acad. Sci. USA 1998, 95, 4309–4314;
- 3bO. Roy, C. Caumes, Y. Esvan, C. Didierjean, S. Faure, C. Taillefumier, Org. Lett. 2013, 15, 2246–2249;
- 3cB. C. Gorske, J. R. Stringer, B. L. Bastian, S. A. Fowler, H. E. Blackwell, J. Am. Chem. Soc. 2009, 131, 16555–16567;
- 3dC. Caumes, O. Roy, S. Faure, C. Taillefumier, J. Am. Chem. Soc. 2012, 134, 9553–9556;
- 3eN. Gangloff, J. Ulbricht, T. Lorson, H. Schlaad, R. Luxenhofer, Chem. Rev. 2016, 116, 1753–1802;
- 3fH. R. Reese, C. C. Shanahan, C. Proulx, S. Menegatti, Acta Biomater. 2020, 102, 35–74;
- 3gL. Fischer, G. Guichard, Org. Biomol. Chem. 2010, 8, 3101–3117;
- 3hN. Pendem, C. Douat, P. Claudon, M. Laguerre, S. Castano, B. Desbat, D. Cavagnat, E. Ennifar, B. Kauffmann, G. Guichard, J. Am. Chem. Soc. 2013, 135, 4884–4892.
- 4
- 4aD. Seebach, J. Gardiner, Acc. Chem. Res. 2008, 41, 1366–1375;
- 4bR. P. Cheng, S. H. Gellman, W. F. DeGrado, Chem. Rev. 2001, 101, 3219–3232;
- 4cL. M. Johnson, S. H. Gellman, Methods Enzymol. 2013, 523, 407–429;
- 4dP. Milbeo, J. Martinez, M. Amblard, M. Calmes, B. Legrand, Acc. Chem. Res. 2021, 54, 685–696.
- 5L. Kiss, I. M. Mándity, F. Fülöp, Amino Acids 2017, 49, 1441–1455.
- 6T. Hintermann, K. Gademann, B. Jaun, D. Seebach, Helv. Chim. Acta 1998, 81, 983–1002.
- 7
- 7aS. Hanessian, X. Luo, R. Schaum, S. Michnick, J. Am. Chem. Soc. 1998, 120, 8569–8570;
- 7bS. Hanessian, X. H. Luo, R. Schaum, Tetrahedron Lett. 1999, 40, 4925–4929.
- 8
- 8aD. Seebach, M. Brenner, M. Rueping, B. Schweizer, B. Jaun, Chem. Commun. 2001, 207–208;
- 8bD. Seebach, M. Brenner, M. Rueping, B. Jaun, Chem. Eur. J. 2002, 3, 573–584.
- 9P. G. Vasudev, N. Shamala, K. Ananda, P. Balaram, Angew. Chem. Int. Ed. 2005, 44, 4972–4975.
- 10M. G. Woll, J. R. Lai, I. A. Guzei, S. J. Taylor, M. E. Smith, S. H. Gellman, J. Am. Chem. Soc. 2001, 123, 11077–11078.
- 11
- 11aJ. Farrera-Sinfreu, L. Zaccaro, D. Vidal, X. Salvatella, E. Giralt, M. Pons, F. Albericio, M. Royo, J. Am. Chem. Soc. 2004, 126, 6048–6057;
- 11bJ. Farrera-Sinfreu, E. Giralt, S. Castel, F. Albericio, M. Royo, J. Am. Chem. Soc. 2005, 127, 9459–9468.
- 12A. A. Edwards, G. J. Sanjayan, S. Hachisu, G. E. Tranter, G. W. J. Fleet, Tetrahedron 2006, 33, 7718–7725.
- 13A. Kothari, M. K. Qureshi, E. M. Beck, M. D. Smith, Chem. Commun. 2007, 2814–2816.
- 14
- 14aM. Khurram, N. Qureshi, M. D. Smith, Chem. Commun. 2006, 5006–5008;
- 14bC. R. Jones, M. Khurram, N. Qureshi, F. R. Truscott, S.-T. D. Hsu, A. J. Morrison, M. D. Smith, Angew. Chem. Int. Ed. Engl. 2008, 47.
- 15B. Nizami, D. Bereczki-Szakál, N. Varró, K. E. Battioui, V. U. Nagaraj, I. C. Szigyártó, I. Mándity, T. Beke-Somfai, Nucleic Acids Res. 2020, 48, D1122-D1128.
- 16
- 16aL. Guo, Y. Chi, A. M. Almeida, I. A. Guzei, B. K. Parker, S. H. Gellman, J. Am. Chem. Soc. 2009, 131, 16018–16020;
- 16bB. F. Fisher, S. H. Gellman, J. Am. Chem. Soc. 2016, 138, 10766–10769.
- 17L. Guo, W. Zhang, I. A. Guzei, L. C. Spencer, S. H. Gellman, Tetrahedron 2012, 68, 4413–4417.
- 18L. Guo, A. M. Almeida, W. Zhang, A. G. Reidenbach, S. H. Choi, I. A. Guzei, S. H. Gellman, J. Am. Chem. Soc. 2010, 132, 7868–7869.
- 19B. F. Fisher, L. Guo, B. S. Dolinar, I. A. Guzei, S. H. Gellman, J. Am. Chem. Soc. 2015, 137, 6484–6487.
- 20L. Guo, W. Zhang, I. A. Guzei, L. C. Spencer, S. H. Gellman, Org. Lett. 2012, 14, 2582–2585.
- 21M. W. Giuliano, S. J. Maynard, A. M. Almeida, L. Guo, I. A. Guzei, L. C. Spencer, S. H. Gellman, J. Am. Chem. Soc. 2014, 136, 15046–15053.
- 22R. Fanelli, D. Berta, T. Földes, E. Rosta, R. A. Atkinson, H.-J. Hofmann, K. Shankland, A. J. A. Cobb, J. Am. Chem. Soc. 2020, 142, 1382–1393.
- 23
- 23aN. Fusetani, S. Matsunaga, H. Matsumoto, Y. Takebayashi, J. Am. Chem. Soc. 1990, 112, 7053–7054;
- 23bJ. E. Coleman, E. D. d Silva, F. Kong, R. J. Andersen, T. M. Allen, Tetrahedron 1995, 51, 10653–10662;
- 23cN. Schaschke, Bioorg. Med. Chem. Lett. 2004, 14, 855–857;
- 23dR. G. Linington, B. R. Clark, E. E. Trimble, A. Almanza, L.-D. Ureña, D. E. Kyle, W. H. Gerwick, J. Nat. Prod. 2009, 72, 14–17;
- 23eX. Bian, A. Plaza, Y. Zhang, R. Müller, J. Nat. Prod. 2012, 75, 1652–1655;
- 23fJ. A. Nieman, J. E. Coleman, D. J. Wallace, E. Piers, L. Y. Lim, M. Roberge, R. J. Andersen, J. Nat. Prod. 2003, 66, 183–199.
- 24P. Tabares, B. Degel, N. Schaschke, U. Hentschel, T. Schirmeister, Pharmacognosy Res. 2012, 4, 63–66.
- 25B. Miller, A. J. Friedman, H. Choi, J. Hogan, J. A. McCammon, V. Hook, W. H. Gerwick, J. Nat. Prod. 2014, 77, 92–99.
- 26A. Y. Lee, M. Hagihara, R. Karmacharya, M. W. Albers, S. L. Schreiber, J. Clardy, J. Am. Chem. Soc. 1993, 115, 12619–12620.
- 27B. E. Maryanoff, X. Qiu, K. P. Padmanabhan, A. Tulinsky, H. R. A. Jr, P. Andrade-Gordon, M. N. Greco, J. A. Kauffman, K. C. Nicolaou, A. Liu, P. H. Brungs, N. Fusetani, Proc. Natl. Acad. Sci. USA 1993, 90, 8048–8052.
- 28V. Ganesh, A. Y. Lee, J. Clardy, A. Tulinsky, Protein Sci. 1996, 5, 825–835.
- 29J. Jurczak, A. Golebiowski, Chem. Rev. 1989, 89, 149–164.
- 30
- 30aA. D. Abell, M. K. Edmonds, in Modern Carbonyl Olefination (Ed.: T. Takeda), Wiley-VCH, Weinheim, Germany, 2004, pp. 1–17;
- 30bR. Robiette, J. Richardson, V. K. Aggarwal, J. N. Harvey, J. Am. Chem. Soc. 2006, 128, 2394–2409.
- 31T. Itaya, T. Fujii, A. Evidente, G. Randazzo, G. Surico, N. S. Lacobellis, Tetrahedron Lett. 1986, 27, 6349–6352.
- 32
- 32aM. Hagihara, N. J. Anthony, T. J. Stout, J. Clardy, S. L. Schreiber, J. Am. Chem. Soc. 1992, 114, 6568–6570;
- 32bS. M. Mali, A. Bandyopadhyay, S. V. Jadhav, M. G. Kumar, H. N. Gopi, Org. Biomol. Chem. 2011, 9, 6566–6574.
- 33M. J. Hensel, P. L. Fuchs, Synth. Commun. 1986, 16, 1285–1295.
- 34H. Kogen, T. Nishi, J. Chem. Soc. Chem. Commun. 1987, 4, 311–312.
- 35
- 35aP. Coutrot, C. Grison, S. Genève, C. Didierjean, A. Aubry, A. Vicherat, M. Marraud, Lett. Pept. Sci. 1997, 4, 415–422;
- 35bC. Grison, S. Genève, E. Halbin, P. Coutrot, Tetrahedron 2001, 57, 4903–4923.
- 36J. M. Concellon, C. Méjica, Eur. J. Org. Chem. 2007, 31, 5250–5255.
- 37Q.-S. Wang, J.-H. Xie, L.-C. Guo, Q.-L. Zhou, Org. Biomol. Chem. 2012, 10, 43–45.
- 38R. Kudirka, S. K. J. Devine, C. S. Adams, D. L. V. Vranken, Angew. Chem. Int. Ed. Engl. 2009, 48, 36–77–3680.
- 39J. H. Lee, S. Lee, Chem. Sci. 2013, 4, 2922–2927.
- 40
- 40aG. Srikanth, K. V. S. Ramakrishna, G. V. M. Sharma, Org. Lett. 2015, 17, 4576–4579;
- 40bM. Zhang, K. Watanabe, M. Tsukamoto, R. Shibuya, H. Morimoto, T. Ohshima, Chem. Eur. J. 2015, 21, 3937–3941.
- 41
- 41aM. Sasaki, K. Tanino, A. Hirai, M. Miyashita, Org. Lett. 2003, 5, 1789–1791;
- 41bA. Kondoh, Y. Kamata, M. Terada, Org. Lett. 2017, 19, 1682–1685.
- 42Y.-Q. Fang, P. M. Tadross, E. N. Jacobsen, J. Am. Chem. Soc. 2014, 136, 17966–17968.
- 43E. Mann, H. Kessler, Org. Lett. 2003, 5, 4567–4570.
- 44L. Mathieu, B. Legrand, C. Deng, L. Vezenkov, E. Wenger, C. Didierjean, M. Amblard, M. C. Averlant-Petit, N. Masurier, V. Lisowski, J. Martinez, L. T. Maillard, Angew. Chem. Int. Ed. Engl. 2013, 52, 6006–6010.
- 45L. Mathieu, C. Bonnel, N. Masurier, L. T. Maillard, J. Martinez, V. Lisowski, Eur. J. Org. Chem. 2015, 2015, 2262–2270.
- 46Y. Krishna, S. Sharma, R. S. Ampapathi, D. Koley, Org. Lett. 2014, 16, 2084–2087.
- 47F. Garcia Gonzalez, Adv. Carbohydr. Chem. 1956, 11, 97–143.
10.1016/S0096-5332(08)60117-4 Google Scholar
- 48G. Bartoli, J. G. Fernández-Bolaños, G. D. Antonio, G. Foglia, S. Giuli, R. Gunnella, M. Mancinelli, E. Marcantoni, M. Paoletti, J. Org. Chem. 2007, 72 6029–6036.
- 49
- 49aA. Bandyopadhyay, S. M. Mali, P. Lunawat, K. M. P. Raja, H. N. Gopi, Org. Lett. 2011, 13, 4482–4485;
- 49bA. Bandyopadhyay, R. Misra, H. N. Gopi, Chem. Commun. 2016, 52, 4938–4941.
- 50
- 50aC. Baldauf, R. Gunther, H. J. Hofmann, J. Org. Chem. 2005, 70, 5351–5361;
- 50bC. Baldauf, R. Günther, H. J. Hofmann, Helv. Chim. Acta 2003, 2003, 2573–2588.
- 51
- 51aK. Veeresh, M. Singh, H. N. Gopi, Org. Biomol. Chem. 2019, 17, 9226–9231;
- 51bR. Misra, S. Dey, R. M. Reja, H. N. Gopi, Angew. Chem. Int. Ed. 2018, 57, 1057–1061.
- 52
- 52aE. Benedetti, B. D. Blasio, C. Pedone, G. P. Lorenzi, L. Tomasic, V. Gramlich, Nature 1979, 282, 620;
- 52bB. D. Blasio, E. Benedetti, V. Pavone, C. Pedone, C. Gerber, G. P. Lorenzi, Biopolymers 1989, 28, 203–214.
- 53T. K. Chakraborty, A. Ghosh, S. K. Kumar, A. C. Kunwar, J. Org. Chem. 2003, 68, 6459–6462.
- 54
- 54aC. Grison, S. Genève, S. Claudel, P. Coutrot, M. Marraud, Tetrahedron Lett. 2003, 44, 2297–2300;
- 54bC. Grison, P. Coutrot, S. Geneve, C. Didierjean, M. Marraud, J. Org. Chem. 2005, 70, 10753–10764.
- 55B. Legrand, L. Mathieu, A. Lebrun, S. Andriamanarivo, V. Lisowski, N. Masurier, S. Zirah, Y. K. Kang, J. Martinez, L. T. Maillard, Chem. Eur. J. 2014, 20, 6713–6720.
- 56B. R. Beno, K. S. Yeung, M. D. Bartberger, L. D. Pennington, N. A. Meanwell, J. Med. Chem. 2015, 58, 4383–4438.
- 57
- 57aA. Bandyopadhyay, H. N. Gopi, Org. Lett. 2012, 14, 2770–2773;
- 57bK. Veeresh, H. N. Gopi, Org. Lett. 2019, 21, 4500–4504.
- 58M. G. Kumar, S. N. Benke, K. M. P. Raja, H. N. Gopi, Chem. Commun. 2015, 51, 13397–13399.
- 59M. Ganesh Kumar, V. J. Thombare, M. M. Katariya, K. Veeresh, K. M. Raja, H. N. Gopi, Angew. Chem. Int. Ed. Engl. 2016, 55, 7847–7851.
- 60C. Baldauf, R. Günther, H.-J. Hofmann, J. Org. Chem. 2006, 71, 1200–1208.
- 61C. Bonnel, B. Legrand, M. Simon, J. Martinez, J. L. Bantignies, Y. K. Kang, E. Wenger, F. Hoh, N. Masurier, L. T. Maillard, Chem. Eur. J. 2017, 23, 17584–17591.
- 62S. V. Jadhav, A. Bandyopadhyay, H. N. Gopi, Org. Biomol. Chem. 2013, 11, 509–514.
- 63
- 63aM. Pasco, C. Dolain, G. Guichard, Comprehensive Supramolecular Chemistry II. 2017, 89–125;
10.1016/B978-0-12-409547-2.12565-X Google Scholar
- 63bA. D. Bautista, C. J. Craig, E. A. Harker, A. Schepartz, Curr. Opin. Chem. Biol. 2007, 11, 685–692;
- 63cH. M. Werner, W. S. Horne, Curr. Opin. Chem. Biol. 2015, 28, 75–82;
- 63dT. Kodadek, P. McEnaney, Chem. Commun. 2016, 52, 6038–6059.
- 64L. Pauling, R. B. Corey, H. R. Branson, Proc. Natl. Acad. Sci. USA 1951, 37, 205–211.
- 65M. N. Fodje, S. Al-Karadaghi, Protein Eng. 2002, 15, 353–358.
- 66
- 66aC. Le, C. Fang, S. D. Sekaran, Antimicrob. Agents Chemother. 2017, 6 e02340–02316;
- 66bW. C. Wimley, ACS Chem. Biol. 2010, 5, 905–917;
- 66cK. A. Brogden, Nat. Rev. Microbiol. 2005, 3, 238–250;
- 66dR. E. Hancock, H. G. Sahl, Nat. Biotechnol. 2006, 24, 1551–1557;
- 66eN. B. Nicolau, B. da Cunha, N. B. Cobacho, J. F. Viana, L. A. Lima, K. B. Sampaio, S. S. Dohms, A. C. Ferreira, C. la Fuente-Núñez, F. F. Costa, O. L. Franco, S. C. Dias, Drug Discovery Today 2017, 22, 234–248.
- 67C. D. Fjell, J. A. Hiss, R. E. Hancock, G. Schneider, Nat. Rev. Drug Discovery 2012, 11, 37–51.
- 68
- 68aY. Hamuro, J. P. Schneider, W. F. DeGrado, J. Am. Chem. Soc. 1999, 121, 12200–12201;
- 68bD. Liu, W. F. DeGrado, J. Am. Chem. Soc. 2001, 123, 7553–7559;
- 68cE. A. Porter, X. Wang, H. S. Lee, B. Weisblum, S. H. Gellman, Nature 2000, 404, 565;
- 68dT. L. Raguse, E. A. Porter, B. Weisblum, S. H. Gellman, J. Am. Chem. Soc. 2002, 124, 12774–12785;
- 68eP. I. Arvidsson, N. S. Ryder, H. M. Weiss, D. F. Hook, J. Escalante, D. Seebach, Chem. Biodiversity 2005, 2, 401–420;
- 68fA. Violette, S. Fournel, K. Lamour, O. Chaloin, B. Frisch, J. P. Briand, H. Monteil, G. Guichard, Chem. Biol. 2006, 13, 531–538;
- 68gP. Claudon, A. Violette, K. Lamour, M. Decossas, S. Fournel, B. Heurtault, J. Godet, Y. Mely, B. Jamart-Gregoire, M. C. Averlant-Petit, J. P. Briand, G. Duportail, H. Monteil, G. Guichard, Angew. Chem. Int. Ed. 2010, 49, 333–336;
- 68hG. N. Tew, D. Liu, B. Chen, R. J. Doerksen, J. Kaplan, P. J. Carroll, M. L. Klein, W. F. DeGrado, Proc. Natl. Acad. Sci. USA 2002, 99, 5110–5114;
- 68iD. Liu, S. Choi, B. Chen, R. J. Doerksen, D. J. Clements, J. D. Winkler, M. L. Klein, W. F. DeGrado, Angew. Chem. Int. Ed. 2004, 43, 1158–1162;
- 68jS. Choi, A. Isaacs, D. Clements, D. Liu, H. Kim, R. W. Scott, J. D. Winkler, W. F. DeGrado, Proc. Natl. Acad. Sci. USA 2009, 106, 6968–6973;
- 68kJ. Hua, R. Yamarthy, S. Felsenstein, R. W. Scott, K. Markowitz, G. Diamond, Mol. Oral Microbiol. 2010, 25, 418–425;
- 68lJ. Hua, R. W. Scott, G. Diamond, Mol. Oral Microbiol. 2010, 25, 426–432;
- 68mH. Tang, R. J. Doerksen, G. N. Tew, Chem. Commun. 2005, 1537–1539;
- 68nL. Arnt, K. Nüsslein, G. N. Tew, J. Polym. Sci. Part A 2004, 42, 3860–3864;
- 68oM. Laurencin, M. Simon, Y. Fleury, M. Baudy-Floc′h, A. Bondon, B. Legrand, Chem. Eur. J. 2018, 24, 6191–6201;
- 68pM. Laurencin, B. Legrand, E. Duval, J. Henry, M. Baudy-Floc′h, C. Zatylny-Gaudin, A. Bondon, J. Med. Chem. 2012, 55, 2025–2034.
- 69C. Bonnel, B. Legrand, M. Simon, M. Clavié, A. Masnou, E. Jumas-Bilak, Y. K. Kang, P. Licznar-Fajardo, L. T. Maillard, N. Masurier, J. Med. Chem. 2020, 63, 9168–9180.
- 70S. S. Shankar, S. N. Benke, N. Nagendra, P. L. Srivastava, H. V. Thulasiram, H. N. Gopi, J. Med. Chem. 2013, 56, 8468–8474.
- 71Q. Guan, S. Huang, Y. Jin, R. Campagne, V. Alezra, Y. Wan, J. Med. Chem. 2019, 62, 7603–7617.
- 72L. H. Kondejewski, S. W. Farmer, D. S. Wishart, R. E. W. Hancock, R. S. Hodges, Int. J. Pept. Protein Res. 1996, 47, 460–466.
- 73E. J. Prenner, R. N. Lewis, R. N. McElhaney, Biochim. Biophys. Acta 1999, 1462, 201–221.
- 74
- 74aM. Fernández-Vidal, S. Jayasinghe, A. S. Ladokhin, S. H. White, J. Mol. Biol. 2007, 370, 459–470;
- 74bI. A. Edwards, A. G. Elliott, A. M. Kavanagh, J. Zuegg, M. A. T. Blaskovich, M. A. Cooper, ACS Infect. Dis. 2016, 2, 442–450.
- 75M. L. Juba, D. K. Porter, E. H. Williams, C. A. Rodriguez, S. M. Barksdale, B. M. Bishop, Biochim. Biophys. Acta 2015, 1848, 1081–1091.
- 76
- 76aA. Makovitzki, D. Avrahami, Y. Shai, Proc. Natl. Acad. Sci. USA 2006, 103, 15997–16002;
- 76bA. Makovitzki, J. Baram, Y. Shai, Biochemistry 2008, 47, 10630–10636;
- 76cD. Avrahami, Y. Shai, J. Biol. Chem. 2004, 279, 12277–12285.
- 77
- 77aE. Sikorska, M. Dawgul, K. Greber, E. Iłowska, A. Pogorzelska, W. Kamysz, Biochim. Biophys. Acta. 2014, 1838, 2625–2634;
- 77bJ. N. Horn, T. D. Romo, A. Grossfield, Biochemistry 2013, 52, 5604–5610.
- 78
- 78aE. Muchtar, A. Dispenzieri, H. Magen, M. Grogan, M. Mauermann, E. D. McPhail, P. J. Kurtin, N. Leung, F. K. Buadi, D. Dingli, S. K. Kumar, M. A. Gertz, J. Intern. Med. 2020;
- 78bM. M. Picken, Acta Haematol. 2020, 143, 322–334.
- 79J. Kaffy, C. Berardet, L. Mathieu, B. Legrand, M. Taverna, F. Halgand, G. V. D. Rest, L. T. Maillard, S. Ongeri, Chem. Eur. J. 2020, 26, 14612–14622.
- 80
- 80aE. Andreetto, L. M. Yan, M. Tatarek-Nossol, A. Velkova, A. K. R. Frank, J. Ibarzo, Angew. Chem. Int. Ed. Engl. 2010, 49, 3081–3085;
- 80bY. Zhang, W. Song, Prog. Neurobiol. 2017, 153, 100–120.
- 81
- 81aS. Vivekanandan, J. R. Brender, S. Y. Lee, A. Ramamoorthy, Biochem. Biophys. Res. Commun. 2011, 411, 312–316;
- 81bR. P. R. Nanga, J. R. Brender, S. Vivekanandan, A. Ramamoorthy, Biochim. Biophys. Acta Biomembr. 2011, 1808, 2337–2342.
- 82
- 82aS. Kumar, A. Henning-Knechtel, I. Chehade, M. Magzoub, A. D. Hamilton, J. Am. Chem. Soc. 2017, 139, 17098–17108;
- 82bS. Kumar, A. D. Hamilton, J. Am. Chem. Soc. 2017, 139, 5744–5755;
- 82cS. Kumar, M. A. Brown, A. Nath, A. D. Miranker, Chem. Biol. 2014, 21, 775–781;
- 82dS. Kumar, A. D. Miranker, Chem. Commun. 2013, 49, 4749–4751;
- 82eS. Kumar, M. Birol, D. E. Schlamadinger, S. P. Wojcik, E. Rhoades, A. D. Miranker, Nat. Commun. 2016, 11412.
- 83L. M. A. Ali, M. Simon, K. El Cheikh, J. Aguesseau-Kondrotas, A. Godefroy, C. Nguyen, M. Garcia, A. Morere, M. Gary-Bobo, L. Maillard, Bioconjugate Chem. 2019, 30, 2533–2538.
- 84
- 84aJ. Prakash, L. Beljaars, A. K. Harapanahalli, M. Zeinstra-Smith, A. de Jager-Krikken, M. Hessing, H. Steen, K. Poelstra, Int. J. Cancer 2010, 126, 1966–1981;
- 84bE. D. Vedove, G. Costabile, O. M. Merkel, Adv. Healthcare Mater. 2018, 7, 1701398.
- 85
- 85aP. Tiels, E. Baranova, K. Piens, C. De Visscher, G. Pynaert, W. Nerinckx, J. Stout, F. Fudalej, P. Hulpiau, S. Tannler, S. Geysens, A. Van Hecke, A. Valevska, W. Vervecken, H. Remaut, N. Callewaert, Nat. Biotechnol. 2012, 30, 1225–1231;
- 85bK. El Cheikh, I. Basile, A. Da Silva, C. Bernon, P. Cerutti, F. Salgues, M. Perez, M. Maynadier, M. Gary-Bobo, C. Caillaud, M. Cerutti, M. Garcia, A. Morere, Angew. Chem. Int. Ed. Engl. 2016, 55, 14774–14777.
- 86
- 86aS. M. Banik, K. Pedram, S. Wisnovsky, G. Ahn, N. M. Riley, C. R. Bertozzi, Nature 2020, 584;
- 86bY. Ding, Y. Fei, B. Lu, Trends Pharmacol. Sci. 2020, 41, 464–474.
- 87
- 87aS. J. York, L. S. Arneson, W. T. Gregory, N. M. Dahms, S. Kornfeld, J. Biol. Chem. 1999, 274, 1164–1171;
- 87bJ. L. Kreiling, J. C. Byrd, R. G. MacDonald, J. Biol. Chem. 2005, 280, 21067–21077;
- 87cJ. C. Byrd, J. H. Park, B. S. Schaffer, F. Garmroudi, R. G. MacDonald, J. Biol. Chem. 2000, 275, 18647–18656.
- 88M. Simon, L. M. A. Ali, K. E. Cheikh, J. Aguesseau, M. Gary-Bobo, M. Garcia, A. Morère, L. T. Maillard, Chem. Eur. J. 2018, 24, 11426–11432.
- 89
- 89aB. Legrand, J. Aguesseau-Kondrotas, M. Simon, L. T. Maillard, Catalysts 2020, 10, 700;
- 89bZ. C. Girvin, S. H. Gellman, J. Am. Chem. Soc. 2020, 142, 17211–17223.
- 90
- 90aM. Wiesner, J. D. Revell, S. Tonazzi, H. Wennemers, J. Am. Chem. Soc. 2008, 130, 5610–5611;
- 90bM. Wiesner, J. D. Revell, H. Wennemers, Angew. Chem. Int. Ed. Engl. 2008, 47, 1871–1874;
- 90cM. Wiesner, M. Neuburger, H. Wennemers, Chem. Eur. J. 2009, 15, 10103–10109;
- 90dM. Wiesner, G. Upert, G. Angelici, H. Wennemers, J. Am. Chem. Soc. 2010, 132, 6–7.