Needless to say, more sophisticated approaches could be devised, which would exploit the
presence on DCs of specific receptors, such as Fcγ or C-type lectin receptors (see Vartak and Sucheck
2016 and references therein), or resort to DC-specific peptides or antibodies (see Moyle and Toth 2013
and references therein), to target to DCs the APol and, thereby, the APol-trapped MP used at an
immunogen.
As shown below (§ 15.4), choosing the route of injection of MP/APol complexes can be used to
favor the formation of long-lasting depots providing a sustained release of the immunogen, an
important feature of long-term protection (Bobbala and Hook 2016).
Biomedical applications of amphipols are still in their infancy
(# 2018 by Francis Haraux).
15.3 Uptake of A8-35 and a Passenger Peptide by Cells in Culture
Upon injection of MP/A8-35 complexes in mice, no toxicity is observed. Antibodies are produced
against MPs, but not against APols (Popot et al. 2003). In cell cultures, A8-35 is not cytolytic, at least
at the concentrations needed to deliver MPs to the plasma membrane (Popot et al. 2003). This has led
to the examination of APols as vectors for immunization, as discussed in § 15.2, or for the delivery of
MPs or other hydrophobic or amphipathic molecules for therapeutic purposes, as described here.
The transmembrane (TM) domain of bitopic MPs, which is made up of a single hydrophobic αhelix, often plays a key role in their oligomerization (see e.g. MacKenzie 2006, Matthews et al. 2006,
Hubert et al. 2010, Stangl et al. 2014, and references therein). Peptides mimicking the TM domain of
neuropilin-1 (NRP1), a receptor controlling various biological effects ranging from cell migration to
cell proliferation and cell death (Roth et al. 2009), have been shown to be able to block its biological
functions (Roth et al. 2008). In addition to helping to dissect signaling mechanisms, these peptides may
also offer novel opportunities in cancer therapy. Preclinical studies have demonstrated that interfering
with the function of NRP1 in tumor cells or in the endothelial cells establishing the neovascular
672
15 Biomedical Applications
presence on DCs of specific receptors, such as Fcγ or C-type lectin receptors (see Vartak and Sucheck
2016 and references therein), or resort to DC-specific peptides or antibodies (see Moyle and Toth 2013
and references therein), to target to DCs the APol and, thereby, the APol-trapped MP used at an
immunogen.
As shown below (§ 15.4), choosing the route of injection of MP/APol complexes can be used to
favor the formation of long-lasting depots providing a sustained release of the immunogen, an
important feature of long-term protection (Bobbala and Hook 2016).
Biomedical applications of amphipols are still in their infancy
(# 2018 by Francis Haraux).
15.3 Uptake of A8-35 and a Passenger Peptide by Cells in Culture
Upon injection of MP/A8-35 complexes in mice, no toxicity is observed. Antibodies are produced
against MPs, but not against APols (Popot et al. 2003). In cell cultures, A8-35 is not cytolytic, at least
at the concentrations needed to deliver MPs to the plasma membrane (Popot et al. 2003). This has led
to the examination of APols as vectors for immunization, as discussed in § 15.2, or for the delivery of
MPs or other hydrophobic or amphipathic molecules for therapeutic purposes, as described here.
The transmembrane (TM) domain of bitopic MPs, which is made up of a single hydrophobic αhelix, often plays a key role in their oligomerization (see e.g. MacKenzie 2006, Matthews et al. 2006,
Hubert et al. 2010, Stangl et al. 2014, and references therein). Peptides mimicking the TM domain of
neuropilin-1 (NRP1), a receptor controlling various biological effects ranging from cell migration to
cell proliferation and cell death (Roth et al. 2009), have been shown to be able to block its biological
functions (Roth et al. 2008). In addition to helping to dissect signaling mechanisms, these peptides may
also offer novel opportunities in cancer therapy. Preclinical studies have demonstrated that interfering
with the function of NRP1 in tumor cells or in the endothelial cells establishing the neovascular
672
15 Biomedical Applications