Model Membrane Platforms for Biomedicine: Case Study on Antiviral Drug Development

Biointerphases

Journal for Biophysical Chemistry

Table 2 Virus susceptibility to AH peptide analogue treatment

Virus	Enveloped	Genome	IC₅₀, μM	Target range
HCV genotypes
HCV(JFH-I) genotype 2a	Yes	RNA+	0.6	Yes
HCV (H77 envelope) genotype 1a	Yes	RNA+	3.9	Yes
HCV (Con1 envelope) genotype 1b	Yes	RNA+	1.6	Yes
HCV (J6CF envelope) genotype 2a	Yes	RNA+	1.1	Yes
Other viruses
Dengue virus	Yes	RNA+	2.0	Yes
West Nile virus	Yes	RNA+	4.5	Yes
Measles virus	Yes	RNA−	2.7	No
Respiratory syncytial virus	Yes	RNA−	4.5	No
Human immunodeficiency virus	Yes	RNA+	1.3	No
Adenovirus	No	DNA	>18	No
Borna disease virus	Yes	RNA−	>18	No
Coronavirus 229E	Yes	RNA+	>18	No
Coxsackie virus	No	RNA+	>18	No
Hepatitis B virus	Yes	DNA	>18	No
Influenza virus	Yes	RNA−	>18	No
Lymphocytic choriomeningitis virus	Yes	RNA−	>18	No
Rhinovirus	No	RNA+	>18	No
Rotavirus WISC2	No	dsRNA	>18	No
Vaccinia virus	Yes	DNA	>18	No
Vesicular stomatitis virus	Yes	RNA−	>18	No

To determine whether the antiviral activity of the AH peptide analogue is specific to HCV, Cheng et al. investigated whether the peptide also inhibited the infectivity of other viruses. Treatment with peptide had no significant effect on the infectivity of adenovirus, Borna disease virus, coronavirus, coxsackie virus, influenza A virus, lymphocytic choriomeningitis virus, rhinovirus, rotavirus, vaccinia virus, or vesicular stomatitis virus, or on the antigenicity and DNA content of hepatitis B virus. In contrast, peptide treatment strongly inhibited the infectivity of chimeric viruses containing the envelope proteins of HCV1a and 1b genotypes, and of other human Flaviviridae members, including West Nile virus and dengue 2 virus. Further, infectivity of the paramyxoviruses, measles and respiratory syncytial virus, and HIV-1 were inhibited by the AH peptide analogue. For each virus type, we report (i) presence of lipid envelope, (ii) type of genetic material, (iii) IC₅₀ value of AH peptide analogue, and (iv) whether or not the particle size distribution falls within the range of 100% rupture efficiency by AH peptide. Table is adapted and modified from Ref. [45]