Taurine grafting and collagen adsorption on PLLA films improve human primary chondrocyte adhesion and growth

01 Pubblicazione su rivista
Pellegrino Luca, Cocchiola Rossana, Francolini Iolanda, Lopreiato Mariangela, Piozzi Antonella, Zanoni Robertino, SCOTTO D'ABUSCO Anna, Martinelli Andrea
ISSN: 0927-7765

Biocompatible and degradable poly(?-hydroxy acids) are one of the most widely used materials in scaffolds for tissue engineering. Nevertheless, they often need surface modification to improve interaction with cells. Aminolysis is a common method to increase the polymer hydrophilicity and to introduce surface functional groups, able to covalently link or absorb, through electrostatic interaction, bioactive molecules or macromolecules. For this purpose, multi-functional amines, such as diethylenediamine or hexamethylenediamine are used. However, common drawbacks are their toxicity and the introduction of positive charges on the surface. Thus, these kind of modified surfaces are unable to link directly proteins, such as collagens, a promising substrate for many cell types, in particular chondrocytes and osteoblasts. In this work, poly(L-lactide) (PLLA) film surface was labelled with negatively charged sulfonate groups by grafting taurine (TAU) through an aminolysis reaction. The novel modified PLLA film (PLLA-TAU) was able to interact directly with collagen. The reaction was carried out in mild conditions by using a solution of tetrabutylammonium salt of TAU in methanol. ATR-FTIR, XPS and contact angle measurements were used to verify the outcome of the reaction. After the exchange of tetrabutylamonium cation with Na+, collagen was absorbed on the TAU grafted PLLA film (PLLA-TAU-COLL). In vitro biological tests with human primary chondrocytes showed that PLLA-TAU and PLLA-TAU-COLL improved cell viability and adhesion, compared to the unmodified polymer, suggesting that these modifications make PLLA substrate suitable for cartilage repair.

© Università degli Studi di Roma "La Sapienza" - Piazzale Aldo Moro 5, 00185 Roma