Original drugs approved by the Food and Drug Administration (Center for Drug Evaluation and Research) in 2024

The U.S. Food and Drug Administration (FDA), in particular the Center for Drug Evaluation and Research (CDER), plays a key role in ensuring the safety, efficacy, and innovation of medicines entering the U.S. market, and then the world. The annual review of new medicines approved by the FDA is an important tool for analyzing current trends in pharmacology and medicine, reflecting progress in the treatment of complex diseases, including cancers, orphan diseases, and infections. The review is compiled to familiarize medical specialists and pharmacologists with current trends in the registration of original medicines and in the therapy of malignant neoplasms, orphan diseases.

The aim. To summarize and systematize data on the newest medicines that entered the market in 2024, as well as to analyze the mechanisms of their action. The article aims to inform medical specialists and pharmacologists about current trends in the development and registration of innovative medicines in 2024.

Materials and methods. The presented data are taken from open sources and supplemented with the results of individual studies on new mechanisms and approaches in therapy. The main list of new drugs and introductory information about them are taken from the FDA report “Novel Drug Approvals for 2024”. Data on medicine prescriptions, as well as information on the mechanism of action, are taken from published summary of product characteristics (SmPC) published on this resource, as well as from the Drugs.com website. To describe previously registered medicines for which a new indication is presented, Drugs.com reports were also used. Structural formulas of drugs are taken from the PubChem resource. In case of the absence of structural formula, data from their SmPC or third-party resources, such as Drugbank, were used. The search for literature data on fundamental studies relating to the mechanisms of action of the presented medicines was carried out in the PubMed, ResearchGate, Google Scholar and elibrary.ru databases.

Results. A statistical analysis of registrations, the dynamics of changes in the shares of various types of medicines and basic data on new original drugs registered by CDER are presented. In 2024, the FDA registered 50 original medicines, among which 48% contain a “first-in-class” molecule as an active substance. Small molecules include active substances — 60%, and biopharmaceuticals — 34% (the remaining 6% are imaging agents). At the same time, monoclonal antibodies (mAb) of antitumor and anti-inflammatory action occupy a larger share among biopharmaceuticals.

Conclusion. The large proportion of biopharmaceuticals among those newly registered in 2024 emphasizes the dynamic development of the pharmaceutical industry and its focus on personalized medicine and biotechnology. Therapy based on mAbs interacting with receptors, as well as immunotherapy based on newly discovered mechanisms of antitumor immunity, occupies a separate part in the structure of registered original medicines. The search for new rational combinations of antibiotics remains relevant. Most of the original drug market is still made up of small molecules, among which there are medicines — ligands of new targets and oligonucleotide sequences.

1. Taberna M, Gil Moncayo F, Jané-Salas E, Antonio M, Arribas L, Vilajosana E, Peralvez Torres E, Mesía R. The Multidisciplinary Team (MDT) Approach and Quality of Care. Front Oncol. 2020;10:85. DOI: 10.3389/fonc.2020.00085

2. Lichtenberg FR. The effect of pharmaceutical innovation on longevity: Evidence from the U.S. and 26 high-income countries. Econ Hum Biol. 2022;46:101124. DOI: 10.1016/j.ehb.2022.101124

3. Duarte JG, Duarte MG, Piedade AP, Mascarenhas-Melo F. Rethinking Pharmaceutical Industry with Quality by Design: Application in Research, Development, Manufacturing, and Quality Assurance. AAPS J. 2025;27(4):96. DOI: 10.1208/s12248-025-01079-w

4. Schutz S. Mergers, Prices, and Innovation: Lessons from the Pharmaceutical Industry. SSRN. 2023. DOI: 10.2139/ssrn.4631188

5. Lionberger RA. FDA critical path initiatives: opportunities for generic drug development. AAPS J. 2008;10(1):103–109. DOI: 10.1208/s12248-008-9010-2

6. Mengel E, Patterson MC, Da Riol RM, Del Toro M, Deodato F, Gautschi M, Grunewald S, Grønborg S, Harmatz P, Héron B, Maier EM, Roubertie A, Santra S, Tylki-Szymanska A, Day S, Andreasen AK, Geist MA, Havnsøe Torp Petersen N, Ingemann L, Hansen T, Blaettler T, Kirkegaard T, Í Dali C. Efficacy and safety of arimoclomol in Niemann-Pick disease type C: Results from a double-blind, randomised, placebo-controlled, multinational phase 2/3 trial of a novel treatment. J Inherit Metab Dis. 2021;44(6):1463–1480. DOI: 10.1002/jimd.12428

7. Arneth B. Tumor Microenvironment. Medicina (Kaunas). 2019;56(1):15. DOI: 10.3390/medicina56010015

8. Weber CE, Kuo PC. The tumor microenvironment. Surg Oncol. 2012;21(3):172–177. DOI: 10.1016/j.suronc.2011.09.001

9. Bożyk A, Wojas-Krawczyk K, Krawczyk P, Milanowski J. Tumor Microenvironment-A Short Review of Cellular and Interaction Diversity. Biology (Basel). 2022;11(6):929. DOI: 10.3390/biology11060929

10. Wang Q, Shao X, Zhang Y, Zhu M, Wang FXC, Mu J, Li J, Yao H, Chen K. Role of tumor microenvironment in cancer progression and therapeutic strategy. Cancer Med. 2023;12(10):11149–11165. DOI: 10.1002/cam4.5698

11. Neophytou CM, Panagi M, Stylianopoulos T, Papageorgis P. The Role of Tumor Microenvironment in Cancer Metastasis: Molecular Mechanisms and Therapeutic Opportunities. Cancers (Basel). 2021;13(9):2053. DOI: 10.3390/cancers13092053

12. Thenuwara G, Javed B, Singh B, Tian F. Biosensor-Enhanced Organ-on-a-Chip Models for Investigating Glioblastoma Tumor Microenvironment Dynamics. Sensors (Basel). 2024;24(9):2865. DOI: 10.3390/s24092865

13. Toor SM, Sasidharan Nair V, Decock J, Elkord E. Immune checkpoints in the tumor microenvironment. Semin Cancer Biol. 2020;65:1–12. DOI: 10.1016/j.semcancer.2019.06.021

14. Ni L, Dong C. New checkpoints in cancer immunotherapy. Immunol Rev. 2017;276(1):52–65. DOI: 10.1111/imr.12524

15. Getu AA, Tigabu A, Zhou M, Lu J, Fodstad Ø, Tan M. New frontiers in immune checkpoint B7-H3 (CD276) research and drug development. Mol Cancer. 2023;22(1):43. DOI: 10.1186/s12943-023-01751-9

16. Zhao B, Li H, Xia Y, Wang Y, Wang Y, Shi Y, Xing H, Qu T, Wang Y, Ma W. Immune checkpoint of B7-H3 in cancer: from immunology to clinical immunotherapy. J Hematol Oncol. 2022;15(1):153. DOI: 10.1186/s13045-022-01364-7

17. Jeon H, Vigdorovich V, Garrett-Thomson SC, Janakiram M, Ramagopal UA, Abadi YM, Lee JS, Scandiuzzi L, Ohaegbulam KC, Chinai JM, Zhao R, Yao Y, Mao Y, Sparano JA, Almo SC, Zang X. Structure and cancer immunotherapy of the B7 family member B7x. Cell Rep. 2014;9(3):1089–1098. DOI: 10.1016/j.celrep.2014.09.053

18. Dangaj D, Lanitis E, Zhao A, Joshi S, Cheng Y, Sandaltzopoulos R, Ra HJ, Danet-Desnoyers G, Powell DJ Jr, Scholler N. Novel recombinant human b7-h4 antibodies overcome tumoral immune escape to potentiate T-cell antitumor responses. Cancer Res. 2013;73(15):4820–4829. DOI: 10.1158/0008-5472.CAN-12-3457

19. Wang L, Rubinstein R, Lines JL, Wasiuk A, Ahonen C, Guo Y, Lu LF, Gondek D, Wang Y, Fava RA, Fiser A, Almo S, Noelle RJ. VISTA, a novel mouse Ig superfamily ligand that negatively regulates T cell responses. J Exp Med. 2011;208(3):577–592. DOI: 10.1084/jem.20100619

20. Le Mercier I, Chen W, Lines JL, Day M, Li J, Sergent P, Noelle RJ, Wang L. VISTA Regulates the Development of Protective Antitumor Immunity. Cancer Res. 2014;74(7):1933–1944. DOI: 10.1158/0008-5472.CAN-13-1506

21. Zang X, Thompson RH, Al-Ahmadie HA, Serio AM, Reuter VE, Eastham JA, Scardino PT, Sharma P, Allison JP. B7-H3 and B7x are highly expressed in human prostate cancer and associated with disease spread and poor outcome. Proc Natl Acad Sci U S A. 2007;104(49):19458–19463. DOI: 10.1073/pnas.0709802104

22. Roth TJ, Sheinin Y, Lohse CM, Kuntz SM, Frigola X, Inman BA, Krambeck AE, McKenney ME, Karnes RJ, Blute ML, Cheville JC, Sebo TJ, Kwon ED. B7-H3 ligand expression by prostate cancer: a novel marker of prognosis and potential target for therapy. Cancer Res. 2007;67(16):7893–7900. DOI: 10.1158/0008-5472.CAN-07-1068

23. Cobbold SP, Adams E, Howie D, Waldmann H. CD4+ T Cell Fate Decisions Are Stochastic, Precede Cell Division, Depend on GITR Co-Stimulation, and Are Associated With Uropodium Development. Front Immunol. 2018;9:1381. DOI: 10.3389/fimmu.2018.01381

24. Herr F, Brunel M, Roders N, Durrbach A. Co-stimulation Blockade Plus T-Cell Depletion in Transplant Patients: Towards a Steroid- and Calcineurin Inhibitor-Free Future? Drugs. 2016;76(17):1589–1600. DOI: 10.1007/s40265-016-0656-2

25. Bao Z, Chai R, Liu X, Wang J. Fusion genes as diagnostic and predictive biomarkers for tumor. Global Translational Medicine. 2022;1(1):54. DOI: 10.36922/gtm.v1i1.54

26. Dai X, Theobard R, Cheng H, Xing M, Zhang J. Fusion genes: A promising tool combating against cancer. Biochim Biophys Acta Rev Cancer. 2018;1869(2):149–160. DOI: 10.1016/j.bbcan.2017.12.003

27. Dai Y, Liu P, He W, Yang L, Ni Y, Ma X, Du F, Song C, Liu Y, Sun Y. Genomic Features of Solid Tumor Patients Harboring ALK/ROS1/NTRK Gene Fusions. Front Oncol. 2022;12:813158. DOI: 10.3389/fonc.2022.813158

28. Nadal E, Olavarria E. Imatinib mesylate (Gleevec/Glivec) a molecular-targeted therapy for chronic myeloid leukaemia and other malignancies. Int J Clin Pract. 2004;58(5):511–516. DOI: 10.1111/j.1368-5031.2004.00173.x

29. Zhang H, Ma H, Yang X, Fan L, Tian S, Niu R, Yan M, Zheng M, Zhang S. Cell Fusion-Related Proteins and Signaling Pathways, and Their Roles in the Development and Progression of Cancer. Front Cell Dev Biol. 2022;9:809668. DOI: 10.3389/fcell.2021.809668

30. Roskoski R Jr. ROS1 protein-tyrosine kinase inhibitors in the treatment of ROS1 fusion protein-driven non-small cell lung cancers. Pharmacol Res. 2017;121:202–212. DOI: 10.1016/j.phrs.2017.04.022

31. Pophali PA, Patnaik MM. The Role of New Tyrosine Kinase Inhibitors in Chronic Myeloid Leukemia. Cancer J. 2016;22(1):40–50. DOI: 10.1097/PPO.0000000000000165

32. Weiner LM, Surana R, Wang S. Monoclonal antibodies: versatile platforms for cancer immunotherapy. Nat Rev Immunol. 2010;10(5):317–327. DOI: 10.1038/nri2744

33. Teillaud J. Antibody‐dependent Cellular Cytotoxicity (ADCC). В: Encyclopedia of Life Sciences. 2012. DOI: 10.1002/9780470015902.a0000498.pub2

34. Lutterbuese R, Raum T, Kischel R, Hoffmann P, Mangold S, Rattel B, Friedrich M, Thomas O, Lorenczewski G, Rau D, Schaller E, Herrmann I, Wolf A, Urbig T, Baeuerle PA, Kufer P. T cell-engaging BiTE antibodies specific for EGFR potently eliminate KRAS- and BRAF-mutated colorectal cancer cells. Proc Natl Acad Sci U S A. 2010;107(28):12605–12610. DOI: 10.1073/pnas.1000976107

35. Patel D, Bassi R, Hooper A, Prewett M, Hicklin DJ, Kang X. Anti-epidermal growth factor receptor monoclonal antibody cetuximab inhibits EGFR/HER-2 heterodimerization and activation. Int J Oncol. 2009;34(1):25–32.

36. Li S, Schmitz KR, Jeffrey PD, Wiltzius JJ, Kussie P, Ferguson KM. Structural basis for inhibition of the epidermal growth factor receptor by cetuximab. Cancer Cell. 2005;7(4):301–311. DOI: 10.1016/j.ccr.2005.03.003

37. Zahavi D, Weiner L. Monoclonal Antibodies in Cancer Therapy. Antibodies (Basel). 2020;9(3):34. DOI: 10.3390/antib9030034

38. Di Gaetano N, Cittera E, Nota R, Vecchi A, Grieco V, Scanziani E, Botto M, Introna M, Golay J. Complement activation determines the therapeutic activity of rituximab in vivo. J Immunol. 2003;171(3):1581–1587. DOI: 10.4049/jimmunol.171.3.1581

39. Racila E, Link BK, Weng WK, Witzig TE, Ansell S, Maurer MJ, Huang J, Dahle C, Halwani A, Levy R, Weiner GJ. A polymorphism in the complement component C1qA correlates with prolonged response following rituximab therapy of follicular lymphoma. Clin Cancer Res. 2008;14(20):6697–6703. DOI: 10.1158/1078-0432.CCR-08-0745

40. Gül N, Babes L, Siegmund K, Korthouwer R, Bögels M, Braster R, Vidarsson G, ten Hagen TL, Kubes P, van Egmond M. Macrophages eliminate circulating tumor cells after monoclonal antibody therapy. J Clin Invest. 2014;124(2):812–823. DOI: 10.1172/JCI66776

41. Wallace PK, Howell AL, Fanger MW. Role of Fc gamma receptors in cancer and infectious disease. J Leukoc Biol. 1994;55(6):816–826. DOI: 10.1002/jlb.55.6.816

42. Minard-Colin V, Xiu Y, Poe JC, Horikawa M, Magro CM, Hamaguchi Y, Haas KM, Tedder TF. Lymphoma depletion during CD20 immunotherapy in mice is mediated by macrophage FcgammaRI, FcgammaRIII, and FcgammaRIV. Blood. 2008;112(4):1205–1213. DOI: 10.1182/blood-2008-01-135160

43. Nimmerjahn F, Ravetch JV. Fcgamma receptors as regulators of immune responses. Nat Rev Immunol. 2008;8(1):34–47. DOI: 10.1038/nri2206

44. Clynes RA, Towers TL, Presta LG, Ravetch JV. Inhibitory Fc receptors modulate in vivo cytotoxicity against tumor targets. Nat Med. 2000;6(4):443–446. DOI: 10.1038/74704

45. de Weers M, Tai YT, van der Veer MS, Bakker JM, Vink T, Jacobs DC, Oomen LA, Peipp M, Valerius T, Slootstra JW, Mutis T, Bleeker WK, Anderson KC, Lokhorst HM, van de Winkel JG, Parren PW. Daratumumab, a novel therapeutic human CD38 monoclonal antibody, induces killing of multiple myeloma and other hematological tumors. J Immunol. 2011;186(3):1840–1848. DOI: 10.4049/jimmunol.1003032

46. Vermi W, Micheletti A, Finotti G, Tecchio C, Calzetti F, Costa S, Bugatti M, Calza S, Agostinelli C, Pileri S, Balzarini P, Tucci A, Rossi G, Furlani L, Todeschini G, Zamò A, Facchetti F, Lorenzi L, Lonardi S, Cassatella MA. slan+ Monocytes and Macrophages Mediate CD20-Dependent B-cell Lymphoma Elimination via ADCC and ADCP. Cancer Res. 2018;78(13):3544–3559. DOI: 10.1158/0008-5472.CAN-17-2344

47. Umaña P, Jean-Mairet J, Moudry R, Amstutz H, Bailey JE. Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity. Nat Biotechnol. 1999;17(2):176–180. DOI: 10.1038/6179

48. Davies J, Jiang L, Pan LZ, LaBarre MJ, Anderson D, Reff M. Expression of GnTIII in a recombinant anti-CD20 CHO production cell line: Expression of antibodies with altered glycoforms leads to an increase in ADCC through higher affinity for FC gamma RIII. Biotechnol Bioeng. 2001;74(4):288–894.

49. Shields RL, Lai J, Keck R, O'Connell LY, Hong K, Meng YG, Weikert SH, Presta LG. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J Biol Chem. 2002;277(30):26733–26740. DOI: 10.1074/jbc.M202069200

50. Liu Z, Gunasekaran K, Wang W, Razinkov V, Sekirov L, Leng E, Sweet H, Foltz I, Howard M, Rousseau AM, Kozlosky C, Fanslow W, Yan W. Asymmetrical Fc engineering greatly enhances antibody-dependent cellular cytotoxicity (ADCC) effector function and stability of the modified antibodies. J Biol Chem. 2014;289(6):3571–3590. DOI: 10.1074/jbc.M113.513366

51. Maloney DG, Grillo-López AJ, White CA, Bodkin D, Schilder RJ, Neidhart JA, Janakiraman N, Foon KA, Liles TM, Dallaire BK, Wey K, Royston I, Davis T, Levy R. IDEC-C2B8 (Rituximab) anti-CD20 monoclonal antibody therapy in patients with relapsed low-grade non-Hodgkin's lymphoma. Blood. 1997;90(6):2188–2195.

52. Mendelsohn J. The epidermal growth factor receptor as a target for therapy with antireceptor monoclonal antibodies. Semin Cancer Biol. 1990;1(5):339–344.

53. Rimawi MF, Schiff R, Osborne CK. Targeting HER2 for the treatment of breast cancer. Annu Rev Med. 2015;66:111–128. DOI: 10.1146/annurev-med-042513-015127

54. Ellis LM, Hicklin DJ. VEGF-targeted therapy: mechanisms of anti-tumour activity. Nat Rev Cancer. 2008;8(8):579–591. DOI: 10.1038/nrc2403

55. Pardoll DM. The blockade of immune checkpoints in cancer immunotherapy. Nat Rev Cancer. 2012;12(4):252–264. DOI: 10.1038/nrc3239

56. Anderson AC, Joller N, Kuchroo VK. Lag-3, Tim-3, and TIGIT: Co-inhibitory Receptors with Specialized Functions in Immune Regulation. Immunity. 2016;44(5):989–1004. DOI: 10.1016/j.immuni.2016.05.001