{ "labelLang" : "hun", "responseDate" : "2024-03-28 14:41", "content" : { "otype" : "JournalArticle", "mtid" : 31385284, "status" : "VALIDATED", "published" : true, "comment" : "Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, United States \n Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology, PO Box 513, Eindhoven, MB 5600, Netherlands \n Department of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan \n The Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, 500 Main Street, Cambridge, MA 02142, United States \n Center for Environmental Health Sciences, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, United States \n Broad Institute of MIT and Harvard, 415 Main Street, Cambridge, MA 02142, United States \n Cited By :26 \n Export Date: 21 February 2022 \n Correspondence Address: Pentelute, B.L.; Department of Chemistry, United States; email: blp@mit.edu \n Chemicals/CAS: 4 fluorophenylalanine, 51-65-0, 60-17-3; amino acid, 65072-01-7; diaminobutyric acid, 27252-32-0; hydroxyproline, 51-35-4, 6912-67-0; norvaline, 6600-40-4; ornithine, 70-26-8, 7006-33-9; phosphoserine, 407-41-0; carrier protein, 80700-39-6; Amino Acids; Antibodies, Monoclonal; Carrier Proteins; Peptide Library; Peptides; Proto-Oncogene Proteins c-mdm2; Small Molecule Libraries \n Funding details: T32 GM008334 \n Funding details: National Institute of General Medical Sciences, NIGMS, GM008334 \n Funding details: Defense Advanced Research Projects Agency, DARPA, 023504-001 \n Funding text 1: This work was supported by the NIH/NIGMS Interdepartmental Biotechnology Training Program (T32 GM008334 to A.J.Q.), the Defense Advanced Research Projects Agency (DARPA; Award 023504-001 to B.L.P.), and Calico (to B.L.P.). We gratefully acknowledge Anne Fischer and Tyler Stukenbroeker (DARPA) for their support and guidance; Earl Moore, Mark Paul, Louis Abruzzese, and David Sarracino for their technical assistance with nanoLC and Orbitrap mass spectrometry; and Eric Spooner, Marko Jovanovic, and Dan Maloney for their discussions regarding MS-based analysis and sequencing. 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Why and how have drug discovery strategies in pharma changed? What are the new mindsets? Drug Discov. Today 21, 239–249 (2016).DOI:10.1016/j.drudis.2015.09.007; Erlanson, D. A., McDowell, R. S. & O’Brien, T. Fragment-based drug discovery. J. Med. Chem. 47, 3463–3482 (2004).DOI:10.1021/jm040031v; Gebauer, M. & Skerra, A. Engineered protein scaffolds as next-generation antibody therapeutics. Curr. Opin. Chem. Biol. 13, 245–255 (2009).DOI:10.1016/j.cbpa.2009.04.627; Tsomaia, N. Peptide therapeutics: targeting the undruggable space. Eur. J. Medicinal Chem. 94, 459–470 (2015).DOI:10.1016/j.ejmech.2015.01.014; Vinogradov, A. A., Yin, Y. & Suga, H. Macrocyclic peptides as drug candidates: recent progress and remaining challenges. J. Am. Chem. Soc. 141, 4167–4181 (2019).DOI:10.1021/jacs.8b13178; Grossmann, T. N. et al. Inhibition of oncogenic Wnt signaling through direct targeting of β-catenin. Proc Natl Acad. Sci. USA 109, 17942–17947 (2012).DOI:10.1073/pnas.1208396109; Chang, Y. S. et al. Stapled α−helical peptide drug development: a potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy. PRoc. Natl Acd. Sci USA 110, E3445–E3454 (2013).DOI:10.1073/pnas.1303002110; Leshchiner, E. S. et al. Direct inhibition of oncogenic KRAS by hydrocarbon-stapled SOS1 helices. Proc. Natl Acad. Sci. USA 112, 1761–1766 (2015).DOI:10.1073/pnas.1413185112; Rezai, T., Yu, B., Millhauser, G. L., Jacobson, M. P. & Lokey, R. S. Testing the conformational hypothesis of passive membrane permeability using synthetic cyclic peptide diastereomers. J. Am. Chem. Soc. 128, 2510–2511 (2006).DOI:10.1021/ja0563455; Walensky, L. D. & Bird, G. H. Hydrocarbon-stapled peptides: principles, practice, and progress. J. Med. Chem. 57, 6275–6288 (2014).DOI:10.1021/jm4011675; Bird, G. H. et al. Biophysical determinants for cellular uptake of hydrocarbon-stapled peptide helices. Nat. Chem. Biol. 12, 845–852 (2016).DOI:10.1038/nchembio.2153; Touti, F., Gates, Z. P., Bandyopadhyay, A., Lautrette, G. & Pentelute, B. L. In-solution enrichment identifies peptide inhibitors of protein–protein interactions. Nat. Chem. Biol. 15, 410–418 (2019).DOI:10.1038/s41589-019-0245-2; Rogers, J. M., Passioura, T. & Suga, H. Nonproteinogenic deep mutational scanning of linear and cyclic peptides. Proc. Natl Acad. Sci USA. 115, 10959–10964 (2018).DOI:10.1073/pnas.1809901115; Clackson, T. & Wells, J. A. In vitro selection from protein and peptide libraries. Trends Biotechnol. 12, 173–184 (1994).DOI:10.1016/0167-7799(94)90079-5; Kay, B. K., Kurakin, A. V. & Hyde-DeRuyscher, R. From peptides to drugs via phage display. Drug Discov. Today 3, 370–378 (1998).DOI:10.1016/S1359-6446(98)01220-3; Wilson, D. S., Keefe, A. D. & Szostak, J. W. The use of mRNA display to select high-affinity protein-binding peptides. Proc. Natl Acad. Sci. USA 98, 3750–3755 (2001).DOI:10.1073/pnas.061028198; Obexer, R., Walport, L. J. & Suga, H. Exploring sequence space: harnessing chemical and biological diversity towards new peptide leads. Curr. Opin. Chem. Biol. 38, 52–61 (2017).DOI:10.1016/j.cbpa.2017.02.020; Katoh, T., Tajima, K. & Suga, H. Consecutive elongation of D-Amino acids in translation. Cell Chem. Biol. 24, 46–54 (2017).DOI:10.1016/j.chembiol.2016.11.012; Katoh, T. & Suga, H. Ribosomal incorporation of consecutive β-amino acids. J. Am. Chem. Soc. 140, 12159–12167 (2018).DOI:10.1021/jacs.8b07247; Eidam, O. & L. Satz, A. Analysis of the productivity of DNA encoded libraries. MedChemComm 7, 1323–1331 (2016).DOI:10.1039/C6MD00221H; Zhao, G., Huang, Y., Zhou, Y., Li, Y. & Li, X. Future challenges with DNA-encoded chemical libraries in the drug discovery domain. Expert Opin. Drug Discov. 14, 735–753 (2019).DOI:10.1080/17460441.2019.1614559; Lam, K. S. et al. A new type of synthetic peptide library for identifying ligand-binding activity. Nature 354, 82–84 (1991).DOI:10.1038/354082a0; Lam, K. S., Lebl, M. & Krchňák, V. The “One-Bead-One-Compound” Combinatorial Library Method. Chem. Rev. 97, 411–448 (1997).DOI:10.1021/cr9600114; Gates, Z. P. et al. Xenoprotein engineering via synthetic libraries. Proc. Natl Acad. Sci. USA 115, E5298–E5306 (2018).DOI:10.1073/pnas.1722633115; Zuckermann, R. N., Kerr, J. M., Siani, M. A., Banville, S. C. & Santi, D. V. Identification of highest-affinity ligands by affinity selection from equimolar peptide mixtures generated by robotic synthesis. Proc. Natl Acad. Sci. USA 89, 4505–4509 (1992).DOI:10.1073/pnas.89.10.4505; Dunayevskiy, Y. M., Lai, J.-J., Quinn, C., Talley, F. & Vouros, P. Mass spectrometric identification of ligands selected from combinatorial libraries using gel filtration. Rapid Commun. Mass Spectrom. 11, 1178–1184 (1997).DOI:10.1002/(SICI)1097-0231(199707)11:11<1178::AID-RCM991>3.0.CO;2-H; Kaur, S., McGuire, L., Tang, D., Dollinger, G. & Huebner, V. Affinity selection and mass spectrometry-based strategies to identify lead compounds in combinatorial libraries. J. Protein Chem. 16, 505–511 (1997).DOI:10.1023/A:1026369729393; van Breemen, R. B. et al. Pulsed ultrafiltration mass spectrometry: a new method for screening combinatorial libraries. Anal. Chem. 69, 2159–2164 (1997).DOI:10.1021/ac970132j; Maaty, W. S. & Weis, D. D. Label-free, in-solution screening of peptide libraries for binding to protein targets using hydrogen exchange mass spectrometry. J. Am. Chem. Soc. 138, 1335–1343 (2016).DOI:10.1021/jacs.5b11742; Vinogradov, A. A. et al. Library design-facilitated high-throughput sequencing of synthetic peptide libraries. ACS Comb. Sci. 19, 694–701 (2017).DOI:10.1021/acscombsci.7b00109; Jiang, J. et al. Development of an immuno tandem mass spectrometry (iMALDI) assay for EGFR diagnosis. Proteom. Clin. Appl. 1, 1651–1659 (2007).DOI:10.1002/prca.200700009; Li, H., Popp, R. & Borchers, C. H. Affinity-mass spectrometric technologies for quantitative proteomics in biological fluids. TrAC Trends Anal. Chem. 90, 80–88 (2017).DOI:10.1016/j.trac.2017.02.011; Choi, Y. & van Breemen, R. B. Development of a screening assay for ligands to the estrogen receptor based on magnetic microparticles and LC-MS. Comb. Chem. High. Throughput Screen. 11, 1–6 (2008).DOI:10.2174/138620708783398340; Rush, M. D., Walker, E. M., Prehna, G., Burton, T. & van Breemen, R. B. Development of a magnetic microbead affinity selection screen (MagMASS) using mass spectrometry for ligands to the retinoid X receptor-α. J. Am. Soc. Mass Spectrom. 28, 479–485 (2017).DOI:10.1007/s13361-016-1564-0; Sannino, A. et al. Quantitative assessment of affinity selection performance by using DNA-encoded chemical libraries. ChemBioChem 20, 955–962 (2019).DOI:10.1002/cbic.201800766; Furka, A., Sebestyén, F., Asgedom, M. & Dibó, G. General method for rapid synthesis of multicomponent peptide mixtures. Int. J. Pept. Protein Res. 37, 487–493 (1991).DOI:10.1111/j.1399-3011.1991.tb00765.x; Ma, B. et al. PEAKS: powerful software for peptidede novo sequencing by tandem mass spectrometry. Rapid Commun. Mass Spectrom. 17, 2337–2342 (2003).DOI:10.1002/rcm.1196; Churchill, M. E. et al. Crystal structure of a peptide complex of anti-influenza peptide antibody Fab 26/9. Comparison of two different antibodies bound to the same peptide antigen. J. Mol. Biol. 241, 534–556 (1994).DOI:10.1006/jmbi.1994.1530; Olson, C. A. et al. Single-round, multiplexed antibody mimetic design through mRNA display. Angew. Chem. Int. Ed. Engl. 51, 12449–12453 (2012).DOI:10.1002/anie.201207005; Georgiou, G. et al. Display of heterologous proteins on the surface of microorganisms: From the screening of combinatorial libraries to live recombinant vaccines. Nat. Biotechnol. 15, 29–34 (1997).DOI:10.1038/nbt0197-29; Feldhaus, M. J. et al. Flow-cytometric isolation of human antibodies from a nonimmune Saccharomyces cerevisiae surface display library. Nat. Biotechnol. 21, 163–170 (2003).DOI:10.1038/nbt785; Alluri, P. G., Reddy, M. M., Bachhawat-Sikder, K., Olivos, H. J. & Kodadek, T. Isolation of protein ligands from large peptoid libraries. J. Am. Chem. Soc. 125, 13995–14004 (2003).DOI:10.1021/ja036417x; Böttger, V. et al. Identification of novel mdm2 binding peptides by phage display. Oncogene 13, 2141–2147 (1996).; Hu, B., Gilkes, D. M. & Chen, J. Efficient p53 activation and apoptosis by simultaneous disruption of binding to MDM2 and MDMX. Cancer Res. 67, 8810–8817 (2007).DOI:10.1158/0008-5472.CAN-07-1140; Pazgier, M. et al. Structural basis for high-affinity peptide inhibition of p53 interactions with MDM2 and MDMX. Proc. Natl Acad. Sci. USA 106, 4665–4670 (2009).DOI:10.1073/pnas.0900947106; Li, C. et al. Systematic mutational analysis of peptide inhibition of the p53–MDM2/MDMX interactions. J. Mol. Biol. 398, 200–213 (2010).DOI:10.1016/j.jmb.2010.03.005; Kritzer, J. A., Luedtke, N. W., Harker, E. A. & Schepartz, A. A rapid library screen for tailoring β-peptide structure and function. J. Am. Chem. Soc. 127, 14584–14585 (2005).DOI:10.1021/ja055050o; Stevers, L. M. et al. Modulators of 14-3-3 protein–protein interactions. J. Med. Chem. 61, 3755–3778 (2018).DOI:10.1021/acs.jmedchem.7b00574; Yaffe, M. B. et al. The structural basis for 14-3-3:phosphopeptide binding specificity. Cell 91, 961–971 (1997).DOI:10.1016/S0092-8674(00)80487-0; de Vink, P. J. et al. A binary bivalent supramolecular assembly platform based on Cucurbit[8]uril and dimeric adapter protein 14-3-3. Angew. Chem. Int Ed. Engl. 56, 8998–9002 (2017).DOI:10.1002/anie.201701807; Efimov, A. V. Standard structures in proteins. Prog. Biophysics Mol. Biol. 60, 201–239 (1993).DOI:10.1016/0079-6107(93)90015-C; Griffiths, A. D. & Duncan, A. R. Strategies for selection of antibodies by phage display. Curr. Opin. Biotechnol. 9, 102–108 (1998).DOI:10.1016/S0958-1669(98)80092-X; Zhang, Y., Fonslow, B. R., Shan, B., Baek, M.-C. & Yates, J. R. Protein analysis by shotgun/bottom-up proteomics. Chem. Rev. 113, 2343–2394 (2013).DOI:10.1021/cr3003533; Mándity, I. M. & Fülöp, F. An overview of peptide and peptoid foldamers in medicinal chemistry. Expert Opin. Drug Discov. 10, 1163–1177 (2015).DOI:10.1517/17460441.2015.1076790; Nizami, B. et al. FoldamerDB: a database of peptidic foldamers. Nucleic Acids Res 48, D1122–D1128 (2020).; Heinis, C., Rutherford, T., Freund, S. & Winter, G. Phage-encoded combinatorial chemical libraries based on bicyclic peptides. Nat. Chem. Biol. 5, 502–507 (2009).DOI:10.1038/nchembio.184; Goto, Y. et al. Reprogramming the translation initiation for the synthesis of physiologically stable cyclic peptides. ACS Chem. Biol. 3, 120–129 (2008).DOI:10.1021/cb700233t; Lee, J. H., Meyer, A. M. & Lim, H.-S. A simple strategy for the construction of combinatorial cyclic peptoid libraries. Chem. Commun. 46, 8615–8617 (2010).DOI:10.1039/c0cc03272g; Liang, X., Vézina-Dawod, S., Bédard, F., Porte, K. & Biron, E. One-pot photochemical ring-opening/cleavage approach for the synthesis and decoding of cyclic peptide libraries. Org. Lett. 18, 1174–1177 (2016).DOI:10.1021/acs.orglett.6b00296; Simon, M. D. et al. Rapid flow-based peptide synthesis. ChemBioChem 15, 713–720 (2014).DOI:10.1002/cbic.201300796; Mijalis, A. J. et al. A fully automated flow-based approach for accelerated peptide synthesis. Nat. Chem. 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