The microstructure of collagen type I gel cross-linked with gold nanoparticles

Abstract

Scanning electron microscopy, transmission electron micrsocopy, rheomerty, and electrochemistry were used to provide insight into the microstructure of collagen type I gel (1% w/v) modified with the tiopronin-protected (N-(2-mercaptopropionyl)glycine) gold nanoparticles (TPAu), a multivalent crosslinker. The cross-linking reaction, performed via EDC (1-ethyl-3-(3-dimethyl aminopropyl) carbodiimide) coupling, results in compliant, mechanically stable and continuous gels. The gels contain unusual interconnected collagen-TPAu particles. Electrochemical measurements of 4-hydroxy-(2,2,6,6-tetramethylpiperidine-1-oxyl) (4HT) diffusion within the gel reveal that the gel hindrance is nearly independent of the TPAu concentration. The properties of the collagen-TPAu gel make it suitable for potential biomedical applications, such as delivery of small molecule drugs.

Comparative study on acid‐soluble and pepsin‐soluble collagens from skin and swim bladder of grass carp (Ctenopharyngodon idella)

“…All collagens were like a soft white sponge with a loose and porous structure observed by the naked eye. The SEM results indicated that the surfaces of ASC and PSC were partially wrinkled; it is likely that water was sublimed during lyophilization . However, there were some differences in the structures between ASC and PSC under SEM.…”

“…The SEM results indicated that the surfaces of ASC and PSC were partially wrinkled; it is likely that water was sublimed during lyophilization. 36 However, there were some differences in the structures between ASC and PSC under SEM. Figure 4A shows that ASC-s was rugose, similar to an irregular dense sheet-like film.…”

Cross-Linked Collagen Gels Using Gold Nanoparticles

“…To achieve a homogeneous matrix containing small pores suitable for drug delivery applications and a small size dispersion of the pores, the entire fibrillar component of the collagen has to be removed and only molecular collagen can be used for matrix preparation (9). …”

Characterization of three-spot seahorse (Hippocampus trimaculatus ) skin collagen and its fibrillar gel reinforced by EDC: A comparative study

“…Thus, the improvement of thermal stability and mechanical strength of the collagen gel is essential. From the previous studies, cross‐linking was a common method to enhance the thermal stability and mechanical strength of collagen during fibril formation (Schuetz et al, ). EDC (1‐ethyl‐3‐(3‐dimethylaminopropyl)‐carbodiimide), one of the zero‐length cross‐linkers which facilitates the direct conjugation of carboxyl to amine and does not become part of the final protein (Velmurugan, Jonnalagadda, & Nair, ), was used as the cross‐linking reagent for this study.…”

“…thermal stability and mechanical strength of collagen during fibril formation (Schuetz et al, 2012). EDC (1-ethyl-3-(3-dimethylaminopropyl)carbodiimide), one of the zero-length cross-linkers which facilitates the direct conjugation of carboxyl to amine and does not become part of the final protein (Velmurugan, Jonnalagadda, & Nair, 2013), was used as the cross-linking reagent for this study.…”