Skip to main content



39. J. M. Pelton,* J. E. Hochuli,* P. W. Sadecki, T. Katoh, H. Suga, L. M. Hicks, E. N. Muratov, A. Tropsha,* A. A. Bowers* Cheminformatics-Guided Cell-Free Exploration of Peptide Natural Products, J. Am. Chem. Soc. articles ASAP


38. S. E. Iskandar, L. F. Chiou, T. M. Leisner, D. J. Shell, J. L. Norris-Drouin, C. Vaziri, K. H. Pearce, A. A. Bowers, Identification of Covalent Cyclic Peptide Inhibitors in mRNA Display, J. Am. Chem. Soc., 145, 15065-70, 2023.

37. M. C. Fleming, M. M. Bowler, R. Park, K. I. Popov, A. A. Bowers, Tyrosinase-Catalyzed Peptide Macrocyclization for mRNA DisplayJ. Am. Chem. Soc., 145, 10445-50, 2023.

36. S. E. Iskandar, J. M. Pelton, E. T. Wick, D. L. Bolhuis, A. S. Baldwin, M. J. Emanuele, N. G. Brown, A. A. Bowers, Enabling Genetic Code Expansion and Peptide Macrocyclization in mRNA Display via a Promiscuous Orthogonal Aminoacyl-tRNA Synthetase, J. Am. Chem. Soc., 145, 1512-1517, 2023.

35. R. Park, C. Ongpipattanakul, S. K. Nair, A. A. Bowers,* B. Kuhlman,* Designer installation of a substrate recruitment domain to tailor enzyme specificity, Nat. Chem. Bio., 19, 460-467, 2023.


34. M. M. Bowler, M. Glavatskikh, C. V. Pecot, D. Kireev, A. A. Bowers, Enzymatic Macrolactamization of mRNA Display Libraries for Inhibitor Selection, ACS Chem. Bio., 18, 166-175, 2022.

33. A. J. Rice,* J. M. Pelton,* N. J. Kramer, D. S. Catlin, S. K. Nair, T. V. Pogorelov, D. A. Mitchell,* A. A. Bowers,* Enzymatic Pyridine Aromatization during Thiopeptide Biosynthesis, J. Am. Chem. Soc., 144, 21116-21124, 2022.

32. S. E. Iskandar, A. A. Bowers, mRNA Display Reaches for the Clinic with New PCSK9 Inhibitor, ACS Med. Chem. Lett., 13, 1379-1383, 2022.

31. M. C. Fleming, L. F. Chiou, P. P. Tumbale, G. N. Droby, J. Lim, J. L. Norris-Drouin, J. G. Williams, K. H. Pearce, R. S. Williams, C. Vaziri, A. A. Bowers, Discovery and Structural-Basis of Selectivity of Potent Cyclic Peptide Inhibitors of MAGE-A4, J. Med. Chem., 65, 7231-7245, 2022.


30. V. A. Haberman, S. R. Fleming, T. M. Leisner, A. C. Puhl, E. Feng, L. Xie, X. Chen, Y. Goto, H. Suga, L. V. Parise, D. Kireev, K. H. Pearce, and A. A. Bowers, Discovery and Development of Cyclic Peptide Inhibitors of CIB1, ACS Med. Chem. Lett., 12, 1832-1839, 2021.


29. S. E. Iskandar,* V. A. Haberman,* A. A. Bowers, Expanding the Chemical Diversity of Genetically Encoded Libraries. ACS Comb. Sci., 22, 712–733, 2020.

28. K. E. Bird, C. Xander, S. Murcia, A. A. Schmalstig, X. Wang, M. J. Emanuele, M. Braunstein, A. A. Bowers, Thiopeptides Induce Proteasome-Independent Activation of Cellular Mitophagy. ACS Chem. Bio., 15(8), 2164–2174, 2020.

27. J. W. Bogart,* N. J. Kramer,* A. Turlik, R. M. Bleich, D. S. Catlin, F. C. Schroeder, S. K. Nair, R. T. Williamson, K. N. Houk, A. A. Bowers Interception of the Bycroft-Gowland Intermediate in the Enzymatic Macrocyclization of Thiopeptides. J. Am. Chem. Soc., 142(30), 13170–13179, 2020.

26. A. C. Puhl, J. W. Bogart, V. A. Haberman, J. E. Larson, A. S. Godoy, J. L. Norris-Drouin, S. H. Cholensky, T. M. Leisner, S. V. Frye, L. V. Parise, A.A. Bowers, K. H. Pearce, Discovery and Characterization of Peptide Inhibitors for Calcium and Integrin Binding Protein 1. ACS Chem. Bio., 15(6), 1505–1516, 2020.

25. S. R. Fleming, P. M. Himes, S. V. Ghodge, Y. Goto, H. Suga, A. A. Bowers, Exploring the Post-translational Enzymology of PaaA by mRNA Display. J. Am. Chem. Soc., 142(11), 5024–5028, 2020.


24. J. W. Bogart, A. A, Bowers, Dehydroamino acids: Chemical multi-tools for late-stage diversification Org. Biomol. Chem., 17, 3653-69, 2019.

23. A. R. Gutgsell, S. V. Ghodge, A. A, Bowers, S. B. Neher, Mapping the sites of the lipoprotein lipase (LPL)-angiopoietin-like protein 4 (ANGPTL4) interaction provides mechanistic insight into LPL inhibition, J. Bio. Chem., 294, 2678-89, 2019.

22. S. Farag, R. M. Bleich, E. A. Shank, O. Isayev, A. A, Bowers, A. Tropsha, Inter-Modular Linkers play a crucial role in governing the biosynthesis of non-ribosomal peptides, Bioinformatics, 35, 3584-91, 2019.

21. J. W. Bogart, A. A. Bowers, Thiopeptide Pyridine Synthase TbtD Catalyzes an Intermolecular Formal Aza-Diels-Alder Reaction, J. Am. Chem. Soc., 141, 1842-46, 2019.

20. S. R. Fleming, T. E. Bartges, A. A. Vinogradov, C. L. Kirkpatrick, Y. Goto, H. Suga, L. M. Hicks, A. A. Bowers, Flexizyme-Enabled Benchtop Biosynthesis of Thiopeptides, J. Am. Chem. Soc., 141 (2), 758-762, 2019.


19. A. A. Bowers, The substrate lends a hand, Nat. Chem. Bio., 14 (10), 907–908, 2018.


18. K. J. Grubbs, R. M. Bleich, K. C. Santa Maria, S. E. Allen, S. Farag, E. A. Shank, A. A. Bowers, Large-Scale Bioinformatics Analysis of Bacillus Genomes Uncovers Conserved Roles of Natural Products in Bacterial PhysiologymSystems, 2(6), e00040–17, 2017.

17. A. A. Bowers, Methylating mushrooms, Nat. Chem. Bio., 13 (8), 821-2, 2017.

16.  T. L. Grove, P. M. Himes, S. Hwang, J. Bonnani, H. Yumerefendi, B. Kuhlman, S. Almo, A. A, Bowers, Structural Insights into Thioether Bond Formation of a Sactionine Synthase, J. Am. Chem. Soc., 139 (34), 11734-44, 2017.

15.  J.G. Gober, S.V. Ghodge, J. W. Bogart, W. J. Wever, R. R. Watkins, E. M. Brustad, A. A. Bowers, P450-Mediated Non-natural Cyclopropanation of Dehydroalanine-containing Thiopeptides, ACS Chem. Biol. 12, 1726-31, 2017.

14.  L. Lauinger, J. Li, A. Shostak, I. A. Cemel, N. Ha, Y. Zhang, P. E. Merkl, S. Obermeyer, N. Stankovic-Valentin, T. Schafmeier, W. J. Wever, A. A. Bowers, K. P. Carter, A. E. Palmer, H. Tschochner, F. Melchior, R. J. Deshaies, M. Brunner, A. Diernfellner, Thiolutin is a zinc chelator that inhibits the Rpn11 and other JAMM metalloproteases, Nat. Chem. Biol. 13, 709-14, 2017.

13.  X. Wang, A. Arceci, K. Bird, C. A. Mills, R. Choudhury, J. L. Kernan, C. Zhou, V. Bae-Jump, A. A. Bowers, and M. Emanuele, VprBP/DCAF1 regulates the degradation and non-proteolytic activation of the cell cycle transcription factor FoxM1, Mol. Cell Biol., 37, 1-15, 2017


12.  W. J. Wever, J. W. Bogart, and A. A. Bowers, Identification of Pyridine Synthase Recognition Sequences Allows Modular Solid-Phase Route to Thiopeptide Variants, J. Am. Chem. Soc., 138 (41), 13461–13464, 2016.

11.   S. V. Ghodge, K. A. Biernat, S. J. Bassett, M. R. Redinbo, and A. A. Bowers, Post-translational Claisen Condensation and Decarboxylation en Route to the Bicyclic Core of Pantocin A, J. Am. Chem. Soc., 138 (17), 5487–5490, 2016.

10.   P.M. Himes, S. E. Allen, S. Hwang, and A. A. Bowers, Production of Sactipeptides in Escherichia coli: Probing the Substrate Promiscuity of Subtilosin A Biosynthesis, ACS Chem. Biol., 11(6), 1737-1744, 2016.


9.   S. E. Allen, N. V. Dokholyan, A. A. Bowers, Dynamic Docking of Conformationally Constrained Macrocycles: Methods and Applications, ACS Chem. Biol., 11(1), 10-24, 2015.

8.   W. J. Wever, J. W. Bogart, J. A. Bacile, A. N. Chan, F. C. Schroeder, and A. A. Bowers, Chemoenzymatic Synthesis of Thiazolyl Peptide Natural Products Featuring an Enzyme-Catalyzed Formal [4+2] Cycloaddition, J. Am. Chem. Soc., 137(10), 3494-7, 2015.

7.   Z. D. Dunn, W. J. Wever, N. J. Economou, A. A. Bowers, and B. Li, Enzymatic Basis of ‘Hybridity’ in Thiomarinol Biosynthesis, Angew. Chem. Int. Ed., 54(17), 5137-41, 2015.

6.   R. M. Bleich, J. D. Watrous, P. C. Dorrestein, A. A. Bowers, E. A. Shank, Thiopeptide antibiotics stimulate biofilm formation in Bacillus subtilis, Proc. Nat. Acad. Sci. USA,  112, 3086-91, 2015.

5.   M. J. Powers, E. Sanabria-Valentin, A. A. Bowers, E. A. Shank, Inhibition of Cell Differentiation in Bacillus Subtilis by Pseudomonas protegens, J. Bacteriol., 197(13), 2129, 2015.


4.  X. Du, D. Wojtowicz, A. A. Bowers, D. Levens, C. Benham, and T. M. Przytycka, Genome-wide distribution of non-B DNA motifs is shaped by operon structure and suggests transcriptional importance of non-B DNA structures in Escherichia coli, Nuc. Acid. Res., 41(12), 5965, 2013.

3.  W. Wever, M. A. Cinelli, A. A. Bowers, Visible Light Mediated Activation and O-Glycosylation of Thioglycosides, Org. Lett.,15(1), 30-33, 2013.

2.  Arnison, P. et al., Ribosomally Synthesized and Post-Translationally Modified Peptide Natural Products: Overview and Recommendations for a Universal Nomenclature, Nat. Prod. Rep., 30, 108-160, 2013.


1.  A. A. Bowers, Preparation of natural product-like cyclic peptide libraries, MedChemComm, 3, 905-915, 2012.


Publications Prior to UNC

20.   B. Li, W. Wever, C. T. Walsh, and A. A. Bowers, Dithiolopyrrolones: Biosynthesis, Synthesis, and Activity of a Unique Class of Disulfide-Containing Natural ProductsNat. Prod. Rep., 31, 905, 2014.

19.  B. Li, R. R. Forseth, A. A. Bowers, F. C. Schroeder, C. T. Walsh, A Backup Plan for Self-protection: S-Methylation of Holomycin Biosynthetic Intermediates in Streptomyces clavuligerusChemBioChem, 13(17) 2521-2526, 2012.

18.  A. A. Bowers, M. G. Acker, T. S. Young, and C. T. Walsh, Generation of Thiocillin Ring Size Variants by Prepeptide Gene Replacement and In Vivo Processing by Bacillus cereus, J. Am. Chem. Soc., 134(25) 10313-10316, 2012.

17.  A. A. Bowers, C. T. Walsh, and M. G. Acker, Genetic Interception and Structural Characterization of Thiopeptide Cyclization Precursors from Bacillus cereus, J. Am. Chem. Soc., 132(35) 12182-12184, 2010.

16. C. T. Walsh, M. G. Acker, A. A. Bowers, Thiazolyl peptide antibiotic biosynthesis:  a cascade of posttranslational modifications on ribosomal nascent proteins, J. Bio. Chem.285, 27525-27531, 2010.

15. T. L. Newkirk, A. A. Bowers, R. M. Williams, Discovery, biological activity, synthesis and potential therapeutic utility of naturally occurring histone deacetylase inhibitors, Nat. Prod. Rep., 26(10), 1293-1320, 2009.

14.  A. A. Bowers, M. G. Acker, and C. T. Walsh, In vivo Manipulation of Thiocillin: Structure, Conformation, and Activity of Heterocycle Substitution Mutants, J. Am. Chem. Soc., 132(21) 7319-7327, 2010.

13.  M. G. Acker, A. A. Bowers, and C. T. Walsh, Generation of Thiocillin Variants by Prepeptide Gene Replacement and In Vivo Processing by B. cereus, J. Am. Chem. Soc., 131(48) 17563-17565, 2009.

12.  A. A. Bowers, N. West, T. Newkirk, A. Troutman-Youngman, S. L. Schreiber, O. Wiest, J. E. Bradner, and R. M. Williams, Synthesis and HDAC Inhibitory Activity of Largazole Analogs: Alteration of the Zinc-Binding Domain and Macrocyclic Scaffold. Org. Lett., 11(6) 1301-1304, 2009.

11.  A. A. Bowers, T. J. Greshock, N. West, G. Estiu, S. L. Schreiber, O. Wiest, R. M. Williams, J. E. Bradner, Synthesis and Conformation-Activity Relationships of the Peptide Isosteres of FK228 and Largazole. J. Am. Chem. Soc., 131(8) 2900-2905, 2009.

10.  A. A. Bowers, N. West, J. Taunton, S. L. Schreiber, J. E. Bradner, and R. M. Williams, The Total Synthesis and Biological Mode of Action of Largazole: A Potent Class I Histone Deacetylase (HDAC) Inhibitor. J. Am. Chem. Soc., 130(33) 11219-11222, 2008.

9.  D. Crich, K. Sasaki, M. Sardar, and A. A. Bowers, One-Pot Syntheses of Dissymmetric Diamides Based on the Chemistry of Cyclic Monothioanhydrides.  Scope, Limitations, and Application to the Synthesis of Glycopeptides, J. Org. Chem., 74(10) 3886-3893, 2009.

8.  D. Crich, A. A. Bowers, “Sulfoxides, Sulfimides, and Sulfones” in Handbook of Chemical Glycosylation, ed. A. Demchenko, Wiley-VCH, Weinheim, Germany, 2008, 303-328.

7.  D. Crich and A. A. Bowers, Cyclic Thioanhydrides: Linchpins for Multicomponent Coupling Reactions Based on the Reaction of Thioacids with Electron-Deficient Sulfonamides and Azides, Org. Lett., 9(25) 5323-5325, 2007.

6.  D. Crich, D. Grant, and A. A. Bowers, Heterobivalent Library Expansion by “Living Radical” Processes.  Thiocarbonyl Addition Elimination, and Nitroxide-Based Reactions with Fluorous Deconvolution, J. Am. Chem. Soc., 129(40) 12106-12107, 2007.

5.  T. Nokami, A. Shibuya, H. Tsuyama, A. A. Bowers, D. Crich, S. Suga, and J-I. Yoshida, Electrochemical Generation of Glycosyl Triflates. J. Am. Chem. Soc. 129(35) 10922-10928, 2007.

4.  D. Crich, C. M. Pedersen, A. A. Bowers, and D. J. Wink, Does Conformational Restriction Influence Stereoselectivity in the Formation of Arabinofuranosides?  The 3,5-Di-O-benzylidene and 3,5-Di-O(di-tert-butylsilylene)-2-O-benzylarabinofuranosides as Glycosyl Donors, J. Org. Chem., 72(5) 1553-1565, 2007.

3.  D. Crich and A. A. Bowers, Total Synthesis of a β-(1→3)-D-Rhamnotetraose by a One-Pot, Multiple Radical Fragmentation, Org. Lett., 8(19) 4327-4330, 2006.

2.  D. Crich and A. A Bowers, 4,6-O-[1-Cyano-2-(2-iodophenyl)ethylidene] Acetals.  Improved Second Generation Acetals for the Stereoselective Formation of β-D-Mannopyranosides and Regioselective Reductive Radical Fragmentation to β-D-Rhamnopyranosides.  Scope and Limitations. J. Org. Chem. 71(9) 3452-3463, 2006.

1.  D. Crich, Q. Yao, A. A. Bowers, On the regioselectivity of the Hanessian-Hullar reaction in 4,6-O-benzylidene protected galactopyranosides. Carbohydrate Res., 341(10) 1748-1752, 2006.


2. R. M. Williams, J. E. Bradner, A. A. Bowers, T. L. Newkirk, A. E. Troutman-Youngman Method for Preparing Largazole Analogs and Uses Thereof, PCT Int. Appl., 2010, WO 2010009334.

1. D. Crich, A. A. Bowers, Multicomponent coupling and glycopeptides synthesis with cyclic thioanhydrides, US. Pat. Appl. Publ., 2009, US 20090163697.