Atomic Force Microscopy for Collagen-Based Nanobiomaterials

Abstract

Novel nanobiomaterials are increasingly gaining ground in bioengineering research. Among the numerous biomaterials, collagen-nanobiomaterials, such as collagen thin films, are of great interest since they present a wide range of applications in the fields of biomaterials, tissue engineering, and biomedicine. Collagen type I is the most abundant protein within extracellular matrix and, due to its unique characteristics, is widely used as biomaterial. A thorough characterization of the structure and properties of nanomaterials can be achieved by Atomic Force Microscopy (AFM). AFM is a very powerful tool which can be used to obtain qualitative or quantitative information without destroying the collagen fibrillar structure. This mini review covers issues related to the use of AFM for studying the structure and mechanical properties of collagen-based nanobiomaterials, collagen-substrate interactions during the formation of collagen thin films, collagen-cells interactions, and the collagen-optical radiation interactions.

Type I collagen hydrogels as a delivery matrix for royal jelly derived extracellular vesicles

“…Further characterization of the 2 mg/ml collagen gels with RJ EVs in comparison to the control was done using AFM, a well-known method for nano-characterization of collagen-based biomaterials (Bozec & Horton, 2005 ; Aguayo et al., 2016 ; Stylianou, 2017 ). In the field of EVs, AFM is relatively new, but has significantly broadened the scope of characterization possibilities, i.e.…”

Atomic Force Microscopy on Biological Materials Related to Pathological Conditions

“…The fibrils of collagen type I are the elementary building blocks in many collagen-rich tissues [87, 88], while it presents different morphological functions (including tissue mechanical strength and scaffolding to cell migration) in different tissues [75, 77, 89]. Furthermore, collagen has been identified as a unique biomaterial for the formation of novel bioengineering interventions [75, 90–92]. AFM characterization (imaging and mechanical property measurements) has been extensively performed in pure collagen or collagen rich-tissues as AFM does not destroy the fibrillary structure of collagen and can offer information from collagen molecules to separated fibrils/fibers [81, 93].…”

“…The structural and the mechanical properties of collagen at the nanoscale under various conditions have been extensively studied using AFM [5, 22, 90, 94]. The major advantage of AFM in collagen investigation comparing to other techniques is its ability to provide information regarding nanotopographical features such as the D-band periodicity (the collagen fibril consists of an alternating gap and overlapping regions with a highly reproducible D-band periodicity of approximately 67 nm) [17].…”

“…In this panel, the amino acid sequence, the collagen molecule, the packing of collagen molecules, and the structure of a collagen fibril are presented. (b) A collagen fiber D-band periodicity from a collagen thin film imaged using atomic force microscope (CPII Veeco-Bruker Microscope) in the tapping mode (adapted from [90]).…”

A New Approach for Glyco-Functionalization of Collagen-Based Biomaterials

“…The fibrillary organization of collagen is a fundamental feature in cell culture and tissue engineering. Collagen molecules are packed in a quarter-staggered fashion which gives rise to a repeating banding pattern, the so-called D-periodicity or D-band, of about 67 nm [16,17]. It has been reported in the literature that the transverse D-banding periodic pattern is a key player with respect to fibril mechanical properties, which significantly impacts cell-collagen interactions and is correlated with pathological conditions.…”