Quantifying the interactions between biomimetic biomaterials - collagen I, collagen IV, laminin 521 and cellulose nanofibrils - by colloidal probe microscopy.

Robertus Wahyu N Nugroho,Monika Österberg,Xue Zhang,Juan José Valle-Delgado,Riina Harjumäki,Yan-Ru Lou,Marjo Yliperttula

doi:10.1016/j.colsurfb.2018.09.073

Robertus Wahyu N Nugroho, Monika Österberg + Show 5 more

Open Access

https://doi.org/10.1016/j.colsurfb.2018.09.073

Copy DOI

Abstract

Biomaterials of different nature have been and are widely studied for various biomedical applications. In many cases, biomaterial assemblies are designed to mimic biological systems. Although biomaterials have been thoroughly characterized in many aspects, not much quantitative information on the molecular level interactions between different biomaterials is available. That information is very important, on the one hand, to understand the properties of biological systems and, on the other hand, to develop new composite biomaterials for special applications. This work presents a systematic, quantitative analysis of self- and cross-interactions between films of collagen I (Col I), collagen IV (Col IV), laminin (LN-521), and cellulose nanofibrils (CNF), that is, biomaterials of different nature and structure that either exist in biological systems (e.g., extracellular matrices) or have shown potential for 3D cell culture and tissue engineering. Direct surface forces and adhesion between biomaterials-coated spherical microparticles and flat substrates were measured in phosphate-buffered saline using an atomic force microscope and the colloidal probe technique. Different methods (Langmuir-Schaefer deposition, spin-coating, or adsorption) were applied to completely coat the flat substrates and the spherical microparticles with homogeneous biomaterial films. The adhesion between biomaterials films increased with the time that the films were kept in contact. The strongest adhesion was observed between Col IV films, and between Col IV and LN-521 films after 30 s contact time. In contrast, low adhesion was measured between CNF films, as well as between CNF and LN-521 films. Nevertheless, a good adhesion between CNF and collagen films (especially Col I) was observed. These results increase our understanding of the structure of biological systems and can support the design of new matrices or scaffolds where different biomaterials are combined for diverse biological or medical applications.

Highlights

[33] Before deposition, the collagen I (Col I) and collagen IV (Col IV) films at the phosphate-buffered saline (PBS)-air interface were compressed to surface pressures of 12 mN/m and 30 mN/m, respectively, without provoking film collapse (Figure S2)
[65] Here we provide quantitative support to that observation: the adhesion energy of LN-521 to Col IV (1.9 ± 1.0 nJ/m) and protein films (Col I, Col IV, and LN-521)
It can be observed that the energies of the adhesion of Col I to either Col IV or LN-521 are quite similar. These results provide a quantitative explanation for the structural integrity of the Bruch’s membrane, formed by 5 layers alternating Col IV and Col I

Summary

Introduction

Materials for different biomedical applications have been extensively investigated for the last decades. [1,2,3,4,5,6,7,8,9,10,11] In many cases, the studies have been focused on the response of living cells to different materials, which has an impact on, for instance, the design of implants and scaffolds for tissue replacement or regeneration, and the development of materials for 2D and 3D cell cultures [12,13,14,15,16,17,18,19,20,21,22]. A deeper insight into biomaterial-biomaterial interactions could provide a better understanding of the behavior of biological systems and could support the development of materials to mimic them. Collagen-collagen and collagen-proteoglycans interactions determine the interfibrillar spacing and the structure of the ECM, which is important, for example, for corneal transparency [27]. The tensile stiffness and resilience of those tissues are mainly due to collagen-proteoglycans and collagen-collagen (interfibril and interfiber) interactions. Laminin is another protein present in the ECM that plays an important role in cell adhesion. Collagen-laminin interactions are expected to be essential for the cell support function of ECM, but not much is yet known about these forces

Objectives

Methods

Results

Conclusion