Specific protein-protein interactions limit the cutaneous iontophoretic transport of interferon beta-1B and a poly-ARG interferon beta-1B analogue.

ABSTRACT: The first objective was to investigate the transdermal iontophoresis of interferon beta 1b (IFN); the second was to determine whether the addition of 10 Arg residues at the N-terminus, creating a highly charged poly-Arg analogue (Arg₁₀-IFN), increased delivery. Cumulative permeation of IFN and Arg₁₀-IFN after iontophoresis at 0.5 mA/cm² for 8 h was 6.97 ± 4.82 and 9.55 ± 1.63 ng/cm², respectively - i.e. >1000-fold less than that of ribonuclease A, cytochrome c and human basic fibroblast growth factor. Co-iontophoresis of acetaminophen showed that, in contrast to lysozyme, neither IFN nor Arg₁₀-IFN interacted with skin to decrease convective solvent flow. Furthermore, there was no statistically significant difference between (i)

SUBMITTER: Dubey S 

PROVIDER: S-EPMC7358383 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature