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

Pharmaceutics

卷:11

GordonW. Laurie¹  Changrim Lee²  J.Andrew MacKay²  Wan Wang²  Martha Pastuszka² 

[1] Department of Cell Biology, School of Medicine, University of Virginia, Charlottesville, VA 22908, USA;

[2] Department of Pharmacology and Pharmaceutical Sciences, School of Pharmacy, University of Southern California, Los Angeles, CA 90033, USA;

关键词: elastin-like polypeptide (ELPs);    contact lens;    lacritin;    protein therapeutics;    drug delivery;   

DOI  :  10.3390/pharmaceutics11050221

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown