Thermally-Responsive Loading and Release of Elastin-Like Polypeptides from Contact Lenses

• Main Authors: Wan Wang, Changrim Lee, Martha Pastuszka, Gordon W. Laurie, J. Andrew MacKay
• Format: Article
• Language: English
• Published: MDPI AG 2019-05-01
• Series: Pharmaceutics
• Subjects: elastin-like polypeptide (ELPs); contact lens; lacritin; protein therapeutics; drug delivery
• Online Access: https://www.mdpi.com/1999-4923/11/5/221

Contact lenses are widely prescribed for vision correction, and as such they are an attractive platform for drug delivery to the anterior segment of the eye. This manuscript explores a novel strategy to drive the reversible adsorption of peptide-based therapeutics using commercially available contact lenses. To accomplish this, thermo-sensitive elastin-like polypeptides (ELPs) alone or tagged with a candidate ocular therapeutic were characterized. For the first time, this manuscript demonstrates that Proclear Compatibles^TM contact lenses are a suitable platform for ELP adsorption. Two rhodamine-labelled ELPs, V96 (thermo-sensitive) and S96 (thermo-insensitive), were employed to test temperature-dependent association to the contact lenses. During long-term release into solution, ELP coacervation significantly modulated the release profile whereby more than 80% of loaded V96 retained with a terminal half-life of ~4 months, which was only 1−4 days under solubilizing conditions. A selected ocular therapeutic candidate lacritin-V96 fusion (LV96), either free or lens-bound LV96, was successfully transferred to HCE-T cells. These data suggest that ELPs may be useful to control loading or release from certain formulations of contact lenses and present a potential for this platform to deliver a biologically active peptide to the ocular surface via contact lenses.