Campus Units

Materials Science and Engineering, Chemical and Biological Engineering, Ames Laboratory

Document Type

Article

Publication Version

Accepted Manuscript

Publication Date

1-2020

Journal or Book Title

Materials Science and Engineering: C

Volume

106

First Page

110143

DOI

10.1016/j.msec.2019.110143

Abstract

Functionalized biomaterials interface with tissue upon implantation. There is a growing need to understand how materials properties influence this interaction so that efficient tissue engineering systems can be developed. In this study, we characterize collagen organization in response to functionalized glass beads implanted in SKH1-E mice. Poly-l-arginine (PLR) was modified with arginine derivatives to create a functionalized surface and was coated on glass beads. Tissue sections were removed 28 days post-implantation and were imaged using second harmonic generation (SHG) microscopy. These chemical modifications were able to alter the collagen distribution from highly aligned to disordered (17 ± 6 to 78 ± 1° full width at half-maximum (FWHM)) and the collagen III/I ratio (0.02 to 0.42). Principal component analysis (PCA) comparing the physical properties of the modifiers (e.g. hydrophobicity, molar volume, freely rotating bonds, polarizability) with the SHG analytically derived parameters (e.g. collagen III/I ratio, collagen orientation) was performed. Chemical properties of the PLR-like modifications including lipophilicity, along with the number of freely rotating bonds and the polarizability had significant effects on the collagen surrounding the implant, both in terms of collagen orientation as well as the production of collagen III. These findings demonstrate the possibility of tuning the foreign body response, in terms of collagen deposition and organization, to positively influence the acceptance of implanted biomaterials.

Comments

This is a manuscript of an article published as Boddupalli, Anuraag, Dana Akilbekova, and Kaitlin M. Bratlie. "Poly-l-arginine modifications alter the organization and secretion of collagen in SKH1-E mice." Materials Science and Engineering: C (2019): 110143. DOI: 10.1016/j.msec.2019.110143. Posted with permission.

Creative Commons License

Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.

Copyright Owner

Elsevier B.V.

Language

en

File Format

application/pdf

Available for download on Thursday, September 02, 2021

Published Version

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