Related Experiment Video
Updated: May 20, 2025

Wet Chemistry and Peptide Immobilization on Polytetrafluoroethylene for Improved Cell-adhesion
Published on: August 15, 2016
Enhancing the biocompatibility of phakic intraocular lens via selective fibronectin trapping
Yueze Hong1, Jianyu Xin2, Peng Wang2
1National Engineering Research Center for Biomaterials, Sichuan University, Chengdu 610065, China.
Abstract:
Myopia has become a significant public health problem in recent decades, resulting in a profound public health and financial burden. The phakic intraocular lens (PIOL) utilized in myopia intraocular refractive surgery is constantly facing challenges in terms of uveal biocompatibility. Inspired by the "sandwich theory", this study proposes the hypothesis that fibronectin (FN) can improve biocompatibility, and then creatively constructs a selective in-situ trap FN strategy. Specifically, PIOL surfaces with amide bonds covalently linking collagen were prepared, where selectivity was achieved by specific binding of collagen to FN. The obtained collagen modified material reduces immune response by reducing M1 polarization of macrophages, and its functionality and safety have been verified in vitro and in vivo. The grafting of collagen on the PIOL surface was able to occupy adsorption sites and inhibit the non-specific adsorption of other proteins while mimicking the extracellular matrix (ECM) microenvironment, further reducing the foreign body rejection. Overall, this strategy helps to address the issue of uveal biocompatibility in PIOL from a material design perspective, providing more economical and diversified options for patients with surgical needs. STATEMENT OF SIGNIFICANCE: 1. A phakic intraocular lens material with high ocular biocompatibility has been prepared. 2. By introducing acrylic anhydride and activating it, collagen is covalently grafted onto the surface of HEMA without altering its structure. 3. By utilizing the collagen binding domain in the structure of fibronectin, selective adsorption of fibronectin is enhanced, forming extracellular matrix analogs that reduce macrophage M1 polarization and lower inflammation.

