Abstract
Three types of chemical entities, namely, small organic molecules (organics), peptides, and biologics, are mainly used as drug candidates for the treatment of various diseases. Even though the peptide drugs are known since 1920 in association with the clinical use of insulin, only a limited number of peptides are currently used for therapeutics due to various disadvantages associated with them such as limited serum and blood stability, oral bioavailability, and permeability. Since, through chemical modifications and structure tuning, many of these limitations can be overcome, peptide-based drugs are gaining attention in pharmaceutical research. As of today, there are more than 60 peptide-based drugs approved by FDA, and over 150 peptides are in the advanced clinical studies. In this book chapter, the peptide-based lead compounds and drugs available for treating various viral diseases and their advantages and disadvantages when compared to small molecules drugs are discussed.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Abbreviations
- 3LPro:
-
3 L main protease
- ACE-2:
-
Angiotensin-converting enzyme-2
- ARDS:
-
Acute respiratory distress syndrome
- BKV:
-
BK virus
- CLPro:
-
Chymotrypsin-like protease
- CMV:
-
Cytomegalovirus
- CoV:
-
Coronavirus
- DCC:
-
N,N′-Dicyclohexylcarbodiimide
- FDA:
-
Food and Drug Administration
- FMDV:
-
Foot-and-mouth disease virus
- Fmoc:
-
9-Fluorenylmethoxycarbonyl
- HAdV:
-
Human adenovirus
- HATU:
-
Hexafluorophosphate Azabenzotriazole Tetramethyl Uronium
- HBTU:
-
Hexafluorophosphate Benzotriazole Tetramethyl Uronium
- HD:
-
Human defensin
- HIV:
-
Human immunodeficiency virus
- HPIV:
-
Human parainfluenza virus
- HPV:
-
Human papillomavirus
- HSV:
-
Herpes simplex virus
- IAV:
-
Influenza A virus
- MERS:
-
Middle East respiratory syndrome
- PIV:
-
Parainfluenza virus
- PyBOP:
-
Benzotriazol-1-yl-oxytripyrrolidinophosphonium hexafluorophosphate
- RSV:
-
Respiratory syncytial virus
- SARS:
-
Severe acute respiratory syndrome
- SPPS:
-
Solid-phase peptide synthesis
- VSV:
-
Vesicular stomatitis virus
- WHO:
-
World Health Organization
References
Zumla A, Hui DS (2019) Emerging and reemerging infectious diseases global overview. Infect Dis Clin North Am 33:xiii–xix
Chan WC, White P (eds) (1999) Fmoc solid phase peptide synthesis: a practical approach. OUP Oxford, Oxford, UK
Matsubara T, Onishi A, Saito T, Shimada A, Inoue H, Taki T, Nagata K, Okahata Y, Sato T (2010) Sialic acid-mimic peptides as hemagglutinin inhibitors for anti-influenza therapy. J Med Chem 53:4441–4449
Russell RJ, Haire LF, Stevens DJ, Collins PJ, Lin YP, Blackburn GM, Hay AJ, Gamblin SJ, Skehel JJ (2006) The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design. Nature 443:45–49
Wang TT, Tan GS, Hai R, Pica N, Ngai L, Ekiert DC, Wilson IA, García-Sastre A, Moran TM, Palese P (2010) Vaccination with a synthetic peptide from the influenza virus hemagglutinin provides protection against distinct viral subtypes. Proc Natl Acad Sci U S A 107:18979–18984
Geretti AM (2006) HIV-1 subtypes: epidemiology and significance for HIV management. Curr Opin Infect Dis 19:1–7
Buck CB, Day PM, Thompson CD, Lubkowski J, Lu W, Lowy DR, Schiller JT (2006) Human alpha-defensins block papillomavirus infection. Proc Natl Acad Sci U S A 103:1516–1521
Harrison SC (2008) Viral membrane fusion. Nat Struct Mol Biol 15:690–698
Ingallinella P, Bianchi E, Ladwa NA, Wang YJ, Hrin R, Veneziano M, Bonelli F, Ketas TJ, Moore JP, Miller MD, Pessi A (2009) Addition of a cholesterol group to an HIV-1 peptide fusion inhibitor dramatically increases its antiviral potency. Proc Natl Acad Sci U S A 106:5801–5806
Kim JJ, Culley CM, Mohammad RA (2012) Telaprevir: an oral protease inhibitor for hepatitis C virus infection. American journal of health-system pharmacy. Am J Health Syst Pharm 69:19–33
Mulder K, Lima LA, Miranda V, Dias SC, Franco OL (2013) Current scenario of peptide-based drugs: the key roles of cationic antitumor and antiviral peptides. Front Microbiol 4:321
Otvos L Jr, Wade JD (2014) Current challenges in peptide-based drug discovery. Front Chem 2:62
Mathur D, Prakash S, Anand P, Kaur H, Agrawal P, Mehta A, Kumar R, Singh S, Raghava GP (2016) PEPlife:a repository of the half-life of peptides. Sci Rep 6:1–7
Werle M, Bernkop-Schnürch A (2006) Strategies to improve plasma half life time of peptide and protein drugs. Amino Acids 30:351–367
Fairlie DP, Dantas de Araujo A (2016) Stapling peptides using cysteine crosslinking. Pept Sci 106:843–852
Meng G, Pu J, Li Y, Han A, Tian Y, Xu W, Zhang T, Li X, Lu L, Wang C, Jiang S (2019) Design and biological evaluation of m-xylene Thioether-stapled short helical peptides targeting the HIV-1 gp41 Hexameric coiled–coil fusion complex. J Med Chem 62:8773–8783
Wang C, Xia S, Zhang P, Zhang T, Wang W, Tian Y, Meng G, Jiang S, Liu K (2018) Discovery of hydrocarbon-stapled short α-helical peptides as promising middle east respiratory syndrome coronavirus (MERS-CoV) fusion inhibitors. J Med Chem 61:2018–2026
Cheng S, Chang X, Wang Y, Gao GF, Shao Y, Ma L, Li X (2015) Glycosylated enfuvirtide: a long-lasting glycopeptide with potent anti-HIV activity. J Med Chem 58:1372–1379
Fu M, Zhuang X, Zhang T, Guan Y, Meng Q, Zhang Y (2020) PEGylated leuprolide with improved pharmacokinetic properties. Bioorg Med Chem 28:115306
Veronese FM, Pasut G (2005) PEGylation, successful approach to drug delivery. Drug Discov Today 10:1451–1458
Avan I, Hall CD, Katritzky AR (2014) Peptidomimetics via modifications of amino acids and peptide bonds. Chem Soc Rev 43:3575–3594
Kazmaier U, Deska J (2008) Peptide backbone modifications. Curr Org Chem 12:355–385
Müller MM (2018) Post-translational modifications of protein backbones: unique functions, mechanisms, and challenges. Biochemistry 57:177–185
Tugyi R, Uray K, Iván D, Fellinger E, Perkins A, Hudecz F (2005) Partial D-amino acid substitution: improved enzymatic stability and preserved Ab recognition of a MUC2 epitope peptide. Proc Natl Acad Sci U S A 102:413–418
Wu J, Tang J, Chen H, He Y, Wang H, Yao H (2018) Recent developments in peptide macrocyclization. Tetrahedron Lett 59:325–333
Gante J (1994) Peptidomimetics—tailored enzyme inhibitors. Angew Chem Int Ed Engl 33:1699–1720
Orellana C (2002) Immune system stimulator shows promise against tuberculosis. Lancet Infect Dis 2:711
Reymond JL, Van Deursen R, Blum LC, Ruddigkeit L (2010) Chemical space as a source for new drugs. MedChemComm 1:30–38
Takahashi H, Fukuhara T, Kitazawa H, Kormelink R (2019) Virus latency and the impact on plants. Front Microbiol 10:2764
Scholthof KB, Adkins S, Czosnek H, Palukaitis P, Jacquot E, Hohn T, Hohn B, Saunders K, Candresse T, Ahlquist P, Hemenway C (2011) Top 10 plant viruses in molecular plant pathology. Mol Plant Pathol 12:938–954
Ohmann HB, Babiuk LA (1986) Viral infections in domestic animals as models for studies of viral immunology and pathogenesis. J Gen Virol 67:1–25
Woolhouse M, Scott F, Hudson Z, Howey R, Chase-Topping M (2012) Human viruses: discovery and emergence. Philos Trans R Soc Lond Ser B Biol Sci 367:2864–2871
Lau JL, Dunn MK (2018) Therapeutic peptides: historical perspectives, current development trends, and future directions. Bioorg Med Chem 26:2700–2707
Agarwal G, Gabrani R (2020) Antiviral peptides: identification and validation. Int J Pept Res Ther 18:1–20
Demirkhanyan LH, Marin M, Padilla-Parra S, Zhan C, Miyauchi K, Jean-Baptiste M (2012) Multifaceted mechanisms of HIV-1 entry inhibition by human alpha-defensin. J Biol Chem 287:28821–28838
Root MJ, Steger HK (2004) HIV-1 gp41 as a target for viral entry inhibition. Curr Pharm Des 10:1805–1825
Paeshuyse J, Kaul A, De Clercq E, Rosenwirth B, Dumont JM, Scalfaro P, Bartenschlager R, Neyts J (2006) The non-immunosuppressive cyclosporin DEBIO-025 is a potent inhibitor of hepatitis C virus replication in vitro. Hepatology 43:761–770
Flexner C (2007) HIV drug development: the next 25 years. Nat Rev Drug Discov 6:959–966
Cai L, Jiang S (2010) Development of peptide and small-molecule HIV-1 fusion inhibitors that target gp41. Chem Med Chem 5:1813–1824
Zhang D, Li W, Jiang S (2015) Peptide fusion inhibitors targeting the HIV-1 gp41: a patent review (2009–2014). Expert Opin Ther Pat 25:159–173
Chong H, Yao X, Zhang C, Cai L, Cui S, Wang Y, He Y (2012) Biophysical property and broad anti-HIV activity of albuvirtide, a 3-maleimimidopropionic acid-modified peptide fusion inhibitor. PLoS One 7:e32599
He Y, Xiao Y, Song H, Liang Q, Ju D, Chen X, Lu H, Jing W, Jiang S, Zhang L (2008) Design and evaluation of sifuvirtide, a novel HIV-1 fusion inhibitor. J Biol Chem 283:11126–11134
Wang RR, Yang LM, Wang YH, Pang W, Tam SC, Tien P, Zheng YT (2009) Sifuvirtide, a potent HIV fusion inhibitor peptide. Biochem Biophys Res Commun 382:540–544
Xie D, Yao C, Wang L, Min W, Xu J, Xiao J, Huang M, Chen B, Liu B, Li X, Jiang H (2010) An albumin-conjugated peptide exhibits potent anti-HIV activity and long in vivo half-life. Antimicrob Agents Chemother 54:191–196
Aneja R, Grigoletto A, Nangarlia A, Rashad AA, Wrenn S, Jacobson JM, Pasut G, Chaiken I (2019) Pharmacokinetic stability of macrocyclic peptide triazole HIV-1 inactivators alone and in liposomes. J Pept Sci 25:e3155
Gopi H, Umashankara M, Pirrone V, LaLonde J, Madani N, Tuzer F, Baxter S, Zentner I, Cocklin S, Jawanda N, Miller SR (2008) Structural determinants for affinity enhancement of a dual antagonist peptide entry inhibitor of human immunodeficiency virus type-1. J Med Chem 51:2638–2647
Hancock RE, Sahl HG (2006) Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat Biotechnol 24:1551–1557
National Center for Biotechnology Information (2020) PubChem Compound Summary for CID 100094, Oglufanide. https://pubchem.ncbi.nlm.nih.gov/compound/Oglufanide
Chen Q, Guo Y (2016) Influenza viral hemagglutinin peptide inhibits influenza viral entry by shielding the host receptor. ACS Infect Dis 2:187–193
Skalickova S, Heger Z, Krejcova L, Pekarik V, Bastl K, Janda J, Kostolansky F, Vareckova E, Zitka O, Adam V, Kizek R (2015) Perspective of use of antiviral peptides against influenza virus. Viruses 7:5428–5442
Lim SP, Shi PY (2013) West Nile virus drug discovery. Viruses 5:2977–3006
Hrobowski YM, Garry RF, Michael SF (2005) Peptide inhibitors of dengue virus and West Nile virus infectivity. Virol J 2:49
VanPatten S, He M, Altiti A, F Cheng K, Ghanem MH, Al-Abed Y (2020) Evidence supporting the use of peptides and peptidomimetics as potential SARS-CoV-2 (COVID-19) therapeutics. Future Med Chem 10:4155
Zorzi A, Middendorp SJ, Wilbs J, Deyle K, Heinis C (2017) Acylated heptapeptide binds albumin with high affinity and application as tag furnishes long-acting peptides. Nat Commun 8:1–9
Liang R, Wang L, Zhang N, Deng X, Su M, Su Y, Hu L, He C, Ying T, Jiang S, Yu F (2018) Development of small-molecule MERS-CoV inhibitors. Viruses 10:721
Tomar S, Johnston ML, John SES, Osswald HL, Nyalapatla PR, Paul LN, Ghosh AK, Denison MR, Mesecar AD (2015) Ligand-induced dimerization of middle east respiratory syndrome (MERS) coronavirus nsp5 protease (3CLpro) implications for nsp5 regulation and the development of antivirals. J Biol Chem 290:19403–19422
Gao J, Lu G, Qi J, Li Y, Wu Y, Deng Y, Geng H, Li H, Wang Q, Xiao H, Tan W (2013) Structure of the fusion core and inhibition of fusion by a heptad repeat peptide derived from the S protein of Middle East respiratory syndrome coronavirus. J Virol 87:13134–13140
Lu L, Liu Q, Zhu Y, Chan KH, Qin L, Li Y, Wang Q, Chan JF, Du L, Yu F, Ma C (2014) Structure-based discovery of Middle East respiratory syndrome coronavirus fusion inhibitor. Nat Commun 5:1–2
Bhattacharya M, Sharma AR, Patra P, Ghosh P, Sharma G, Patra BC, Lee SS, Chakraborty C (2020) Development of epitope-based peptide vaccine against novel coronavirus 2019 (SARS-COV-2): Immunoinformatics approach. J Med Virol 92:618–631
Panda PK, Murugan NA, Patel P, Verma SK, Luo W, Rubahn H-G, Mishra YK, Suar M, Ahuja R (2020) Structure-based drug designing and immunoinformatics approach for SARS-CoV-2. Sci Adv 6:eabb8097
Murugan NA, Pandian CJ, Jeyakanthan J (2020) Computational investigation on Andrographis paniculata phytochemicals to evaluate their potency against SARS-CoV-2 in comparison to known antiviral compounds in drug trials. J Biomol Struct Dyn 2020:1–12. https://doi.org/10.1080/07391102.2020.1777901
Badani H, Garry RF, Wimley WC (2014) Peptide entry inhibitors of enveloped viruses: the importance of interfacial hydrophobicity. Biochim Biophys Acta 1838:2180–2197
Jin Z, Du X, Xu Y, Deng Y, Liu M, Zhao Y, Zhang B, Li X, Zhang L, Peng C, Duan Y (2020) Structure of M pro from SARS-CoV-2 and discovery of its inhibitors. Nature 582:289–293
Majkowska-Pilip A, Halik PK, Gniazdowska E (2019) The significance of NK1 receptor ligands and their application in targeted radionuclide tumour therapy. Pharmaceutics 11:443
Han Y, Král P (2020) Computational design of ACE2-based peptide inhibitors of SARS-CoV-2. ACS Nano 14:5143–5147
Weissenhorn W, Hinz A, Gaudin Y (2007) Virus membrane fusion. FEBS Lett 15:690–698
Rao GS, Bhatnagar S, Ahuja V (2002) Structure-based design of a novel peptide inhibitor of HIV-1 integrase: a computer modeling approach. J Biomol Struct Dyn 20:31–38
Xia S, Liu Q, Wang Q, Sun ZW, Su S, Dub LY, Ying TL, Lu L, Jiang SB (2014) Middle east respiratory syndrome coronavirus (mers-cov) entry inhibitors targeting spike protein. Virus Res 194:200–210
Park S, Jackman JA, Cho NJ (2019) Comparing the membrane-interaction profiles of two antiviral peptides: insights into structure–function relationship. Langmuir 35:9934–9943
Elazar M, Cheong KH, Liu P, Greenberg HB, Rice CM, Glenn JS (2003) Amphipathic helix-dependent localization of NS5A mediates hepatitis C virus RNA replication. J Virol 77:6055–6061
Bodanszky M (2012) Principles of peptide synthesis. In: Reactivity and structure: concepts in organic chemistry, vol 16. Springer, New York
Bodanszky M, Bodanszky A (2013) The practice of peptide synthesis. In: Reactivity and structure: concepts in organic chemistry, vol 21. Springer, New York
Da’san MMJ (2018) Thirteen decades of peptide synthesis: key developments in solid phase peptide synthesis and amide bond formation utilized in peptide ligation. Amino Acids 50:39–68
Kimmerlin T, Seebach D (2005) ‘100 years of peptide synthesis’: ligation methods for peptide and protein synthesis with applications to β-peptide assemblies. J Pept Res 65:229–260
Merrifield RB (1963) Solid phase peptide synthesis I: the synthesis of a tetrapeptide. J Am Chem Soc 85:2149–2154
Conibear AC, Watson EE, Payne RJ, Becker CF (2018) Native chemical ligation in protein synthesis and semi-synthesis. Chem Soc Rev 47:9046–9068
Carpino LA, Han GY (1972) 9-Fluorenylmethoxycarbonyl amino-protecting group. J Org Chem 37:3404–3409
Mishra B, Reiling S, Zarena D, Wang G (2017) Host defense antimicrobial peptides as antibiotics: design and application strategies. Curr Opin Chem Biol 38:87–96
Gordon YJ, Huang LC, Romanowski EG, Yate KA, Proske RJ, McDermott AM (2005) Human cathelicidin (LL-37), a multifunctional peptide, is expressed by ocular surface epithelia and has potent antibacterial and antiviral activity. Curr Eye Res 30:385–394
Wilson SS, Wiens ME, Smith JG (2013) Antiviral mechanisms of human defensins. J Mol Biol 425:4965–4980
Ding J, Tasker C, Valere K, Sihvonen T, Descalzi-Montoya DB, Lu W, Chang TL (2013) Anti-HIV activity of human defensin 5 in primary CD4+T cells under serum-deprived conditions is a consequence of defensin-mediated cytotoxicity. PLoS One 8:e76038
Dugan AS, Maginnis MS, Jordan JA, Gasparovic ML, Manley K, Page R (2008) Human alpha-defensins inhibit BK virus infection by aggregating virions and blocking binding to host cells. J Biol Chem 283:31125–31132
Eade CR, Wood MP, Cole AM (2012) Mechanisms and modifications of naturally occurring host defense peptides for anti-HIV microbicide development. Curr HIV Res 10:61–72
Furci L, Tolazzi M, Sironi F, Vassena L, Lusso P (2012) Inhibition of HIV-1 infection by human alpha-defensin-5, a natural antimicrobial peptide expressed in the genital and intestinal mucosae. PLoS One 7:e45208
Hazrati E, Galen B, Lu W, Wang W, Ouyang Y, Keller MJ (2006) Human alpha- and beta-defensins block multiple steps in herpes simplex virus infection. J Immunol 177:8658–8666
Rapista A, Ding J, Benito B, Lo YT, Neiditch MB, Lu W (2011) Human defensins 5 and 6 enhance HIV-1 infectivity through promoting HIV attachment. Retrovirology 8:45
Smith JG, Nemerow GR (2008) Mechanism of adenovirus neutralization by human alpha-defensins. Cell Host Microbe 3:11–19
Verma C, Seebah S, Low SM, Zhou L, Liu SP, Li J (2007) Defensins: antimicrobial peptides for therapeutic development. Biotechnol J 2:1353–1359
Sun L (2013) Peptide-based drug development. Mod Chem appl 1:e103
Fosgerau K, Hoffmann T (2015) Peptide therapeutics: current status and future directions. Drug Discov Today 20:122–128
Muruga Poopathi Raja K (2016) Biopharmaceuticals – emerging peptide therapeutics. Cutting Edge 6:16–20
Di L (2015) Strategic approaches to optimizing peptide ADME properties. AAPS J 17:134–143
Ling R, Dai Y, Huang B, Huang W, Yu J, Lu X, Jiang Y (2020) In silico design of antiviral peptides targeting the spike protein of SARS-CoV-2. Peptides 130:170328
Pierce BG, Boucher EN, Piepenbrink KH, Ejemel M, Rapp CA, Thomas WD, Sundberg EJ, Weng Z, Wang Y (2017) Structure-based Design of Hepatitis C Virus Vaccines that Elicit Neutralizing Antibody Responses to a conserved epitope. J Virol 91:e01032–17
Zhang R, Wei DQ, Du S, Chou KC (2006) Molecular modeling studies of peptide drug candidates against SARS. Med Chem 2:309–314
Muhammed MT, Aki-Yalcin E (2019) Homology modeling in drug discovery: overview, current applications, and future perspectives. Chem Biol Drug Des 93:12–20
Yang Z, Yang G, Zu Y, Fu Y, Zhou L (2010) Computer-based de novo designs of tripeptides as novel neuraminidase inhibitors. Int J Mol Sci 11:4932–4951
Gallay PA, Lin K (2013) Profile of alisporivir and its potential in the treatment of hepatitis C. Drug Des Devel Ther 7:105–115
Coelmont L, Kaptein S, Paeshuyse J, Vliegen I, Dumont JM, Vuagniaux G, Neyts J (2009) Debio 025, a cyclophilin binding molecule, is highly efficient in clearing hepatitis C virus (HCV) replicon-containing cells when used alone or in combination with specifically targeted antiviral therapy for HCV (STAT-C) inhibitors. Antimicrob Agents Chemother 53:967–976
Aspinall RJ, Pockros PJ (2006) SCV-07 (SciClone pharmaceuticals/Verta). Curr Opin Investig Drugs 7:180–185
McHutchison JG, Manns MP, Muir AJ, Terrault NA, Jacobson IM, Afdhal NH, Heathcote EJ, Zeuzem S, Reesink HW, Garg J, Bsharat M, George S, Kauffman RS, Adda N, Di Bisceglie AM, PROVE3 Study Team (2010) Telaprevir for previously treated chronic HCV infection. N Engl J Med 362:1292–1303
Zeuzem S, Andreone P, Pol S, Lawitz E, Diago M, Roberts S, Focaccia R, Younossi Z, Foster GR, Horban A, Ferenci P (2011) Telaprevir for retreatment of HCV infection. N Engl J Med 364:2417–2428
Bold G, Fässler A, Capraro HG, Cozens R, Klimkait T, Lazdins J, Mestan J, Poncioni B, Rösel J, Stover D, Tintelnot-Blomley M, Acemoglu F, Beck W, Boss E, Eschbach M, Hürlimann T, Masso E, Roussel S, Ucci-Stoll K, Wyss D, Lang M (1998) New aza-dipeptide analogues as potent. J Med Chem 41:3387–3401
Croom KF, Dhillon S, Keam SJ (2009) Atazanavir: a review of its use in the management of HIV-1 infection. Drugs 69:1107–1140
Sjogren MH (2004) Thymalfasin: an immune system enhancer for the treatment of liver disease. J Gastroenterol Hepatol 19:S69–S72
Gramenzi A, Cursaro C, Andreone P, Bernardi M (1998) Thymalfasin: clinical pharmacology and antiviral applications. BioDrugs 9:477–486
Chien RN, Liaw YF (2004) Thymalfasin for the treatment of chronic hepatitis B. Expert Rev Anti-Infect Ther 2:9–16
Rustgi VK (2005) Thymalfasin for the treatment of hepatitis C infection. Expert Rev Anti-Infect Ther 3:885–892
Su SB, Gong WH, Gao JL, Shen WP, Grimm MC, Deng X, Murphy PM, Oppenheim JJ, Wang JM (1999) T20/DP178, an ectodomain peptide of human immunodeficiency virus type 1 gp41, is an activator of human phagocyte N-formyl peptide receptor. Blood 93:3885–3892
Lalezari JP, Eron JJ, Carlson M, Cohen C, DeJesus E, Arduino RC, Gallant JE, Volberding P, Murphy RL, Valentine F, Nelson EL, Sista PR, Dusek A, Kilby JM (2003) A phase II clinical study of the long-term safety and antiviral activity of enfuvirtide-based antiretroviral therapy. AIDS 17:691–698
Zhang H, Jin R, Yao C, Zhang T, Wang M, Xia W, Peng H, Wang X, Lu R, Wang C, Xie D (2016) Combination of long-acting HIV fusion inhibitor albuvirtide and LPV/r showed potent efficacy in HIV-1 patients. AIDS Res Ther 13:1–4
Acknowledgments
KMPR acknowledges the financial support through high priority COVID-19 research projects from Science and Engineering Research Board (SERB) [IPA/2020/000285], the Department of Biotechnology (DBT) [BT/PR-40921/COT/142/13/2020], and the Board of Research in Nuclear Sciences (BRNS) [54/14/10//2020-BRNS/37083] of the Government of India.
Author information
Authors and Affiliations
Corresponding authors
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2021 The Author(s), under exclusive license to Springer Nature Singapore Pte Ltd.
About this chapter
Cite this chapter
Murugan, N.A., Raja, K.M.P., Saraswathi, N.T. (2021). Peptide-Based Antiviral Drugs. In: Liu, X., Zhan, P., Menéndez-Arias, L., Poongavanam, V. (eds) Antiviral Drug Discovery and Development. Advances in Experimental Medicine and Biology, vol 1322. Springer, Singapore. https://doi.org/10.1007/978-981-16-0267-2_10
Download citation
DOI: https://doi.org/10.1007/978-981-16-0267-2_10
Published:
Publisher Name: Springer, Singapore
Print ISBN: 978-981-16-0266-5
Online ISBN: 978-981-16-0267-2
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)