Fig. 7

Biophysical characterization of AH peptide-mediated vesicle rupturing. The antiviral mode of action of the AH peptide was studied with the intact vesicle platform on the QCM-D sensor. a Resonance frequency response for different vesicle size distributions up to 100 nm upon AH peptide addition. Vesicles were added at 1.0 ks (arrow 1), and AH peptide was added at 4.2 ks (arrow 2). b Resonance frequency response for different vesicle size distributions greater than 100 nm upon AH peptide addition. Again, vesicles were added at 1.0 ks (arrow 1), and AH peptide was added at 4.2 ks (arrow 2). Note that the average vesicle effective diameters were measured by dynamic light scattering. c Calculation of rupturing efficiency from the resonance frequency response as a function of lipid vesicle size. One hundred percent rupturing is defined as the complete transformation of the intact vesicle layer into a planar lipid bilayer with the characteristic final frequency change of −26 Hz. d Interaction of AH peptide with large vesicles beyond the rupturing range. The absolute change in bound mass is determined from the data presented in Fig. 7b. e Broad-spectrum virocidal potential of AH peptide. The graph represents data replotted from Ref. [45], wherein the size distribution of virus particles is indicated by the black bars. Susceptibility to AH peptide-mediated inhibition of infectivity is indicated for a variety of viruses, as determined in Ref. [45]. Viruses reported to be susceptible and refractory to AH peptide-mediated treatment are indicated in blue and red, respectively. The vertical green dotted line indicates the size cutoff below which 100% lipid vesicle rupture occurs. Figure is adapted and modified from Ref. [41]