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Antiviral Peptides Against Coronaviridae Family: A Review

Overview
Journal Peptides
Specialty Biochemistry
Date 2021 Mar 7
PMID 33676968
Citations 24
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Abstract

The Coronaviridae family comprises large enveloped single-stranded RNA viruses. The known human-infecting coronaviruses; severe acute respiratory syndrome coronavirus (SARS-CoV), Middle East respiratory syndrome coronavirus (MERS-CoV), novel SARS-CoV-2, human coronavirus (HCoV)-NL63, HCoV-229E, HCoV-OC43 and HKU1 cause mild to severe respiratory infections. The viral diseases induced by mammalian and avian viruses from Coronaviridae family pose significant economic and public health burdens. Due to increasing reports of viral resistance, co-infections and the emergence of viral epidemics such as COVID-19, available antiviral drugs show low or no efficacy, and the production of new treatments or vaccines are also challenging. Therefore, demand for the development of novel antivirals has considerably increased. In recent years, antiviral peptides have generated increasing interest as they are from natural and computational sources, are highly specific and effective, and possess the broad-spectrum activity with minimum side effects. Here, we have made an effort to compile and review the antiviral peptides with activity against Coronaviridae family viruses. They were divided into different categories according to their action mechanisms, including binding/attachment inhibitors, fusion and entry inhibitors, viral enzyme inhibitors, replication inhibitors and the peptides with direct and indirect effects on the viruses. Reported studies suggest optimism with regard to the design and production of therapeutically promising antiviral drugs. This review aims to summarize data relating to antiviral peptides particularly with respect to their applicability for development as novel treatments.

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References
1.
Wrapp D, Wang N, Corbett K, Goldsmith J, Hsieh C, Abiona O . Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science. 2020; 367(6483):1260-1263. PMC: 7164637. DOI: 10.1126/science.abb2507. View

2.
Wu J, Chi H, Fu Y, Cao A, Shi J, Zhu M . The antiviral protein viperin interacts with the viral N protein to inhibit proliferation of porcine epidemic diarrhea virus. Arch Virol. 2020; 165(10):2279-2289. PMC: 7382991. DOI: 10.1007/s00705-020-04747-8. View

3.
Ling R, Dai Y, Huang B, Huang W, Yu J, Lu X . In silico design of antiviral peptides targeting the spike protein of SARS-CoV-2. Peptides. 2020; 130:170328. PMC: 7198429. DOI: 10.1016/j.peptides.2020.170328. View

4.
Zhu Y, Yu D, Yan H, Chong H, He Y . Design of Potent Membrane Fusion Inhibitors against SARS-CoV-2, an Emerging Coronavirus with High Fusogenic Activity. J Virol. 2020; 94(14). PMC: 7343218. DOI: 10.1128/JVI.00635-20. View

5.
Meng F, Suo S, Zarlenga D, Cong Y, Ma X, Zhao Q . A phage-displayed peptide recognizing porcine aminopeptidase N is a potent small molecule inhibitor of PEDV entry. Virology. 2014; 456-457:20-7. PMC: 7112085. DOI: 10.1016/j.virol.2014.01.010. View