Related Papers
Scientific Reports
Effects of processing on structural, mechanical and biological properties of collagen-based substrates for regenerative medicine
2018 •
Elisa Storelli
Collagen Structure and Stability
Rafael de Jesus García Solís
Acta of bioengineering and biomechanics / Wrocław University of Technology
Structural alteration of collagen fibres--spectroscopic and mechanical studies
2010 •
Marlena Gąsior-głogowska, M. Kobielarz
Fourier Transform Near Infrared Raman Spectroscopy has been used to monitor the molecular changes of collagen in a tendon subjected to strain. In the Raman spectrum of the unstrained tendon, some protein bands, mainly assigned to collagen, can be observed: amide I (1666 cm-1) and III (1266 and 1248 cm-1) vibrational modes and skeletal (C-C) stretching vibrations (816 and 940 cm-1). The position of these bands is changing with the increasing strain values. It is concluded that elastin and non-helical domains of collagen are initially involved in the load transfer and triple helices of collagen are gradually joining this process.
The Characterization of Acid Soluble Collagen from Sheep Tail Tendon
Anujin Gantulga
Journal of Functional Biomaterials
An Overview of the Use of Equine Collagen as Emerging Material for Biomedical Applications
2020 •
Nunzia GALLO
Type I collagen has always aroused great interest in the field of life-science and bioengineering, thanks to its favorable structural properties and bioactivity. For this reason, in the last five decades it has been widely studied and employed as biomaterial for the manufacture of implantable medical devices. Commonly used sources of collagen are represented by bovine and swine but their applications are limited because of the zoonosis transmission risks, the immune response and the religious constrains. Thus, type-I collagen isolated from horse tendon has recently gained increasing interest as an attractive alternative, so that, although bovine and porcine derived collagens still remain the most common ones, more and more companies started to bring to market a various range of equine collagen-based products. In this context, this work aims to overview the properties of equine collagen making it particularly appealing in medicine, cosmetics and pharmaceuticals, as well as its main b...
Journal of Biomedical Materials Research Part A
Factors influencing the properties of reconstituted collagen fibers prior to self-assembly: Animal species and collagen extraction method
2008 •
Geoffrey Attenburrow
This research work allows a direct comparison between collagen solutions of equal concentration derived from the two widely used collagen sources: bovine Achilles tendon (BAT) and rat tail tendon (RTT), and extraction methods: acid (AS) and pepsin (PS) solubilization on the properties of extruded collagen fibers. Scanning electron microscopy revealed that the substructure of the collagen fibers was the same independent of the treatment. Transmission electron microscopy revealed that the AS collagen-derived fibers were comprised of thick quarter-staggered fibrils, while the coexistence of thin nonbanded and thick banded fibrils was apparent for the PS collagen-derived fibers. The BAT-derived fibers demonstrated higher denaturation temperature than the RTT-derived ones (p < 0.05). The extraction method had no influence on the thermal characteristics of the fibers produced (p > 0.05). ASBAT collagen was of higher viscosity than both ASRTT and PSBAT (p < 0.002), and therefore larger diameter fibers were obtained (p < 0.001). An inversely proportional relationship between dry-fiber diameter and stress at break was observed within the treatments. The PS yielded 10 times more soluble collagen from BAT and the derived fibers were of similar tensile strength, stiffness, and elongation (p > 0.05) as those derived from the AS collagen. No significant difference was observed for the stress at break for the ASBAT and the ASRTT, while significant difference was observed for the elongation and modulus values (p < 0.005). Overall, reconstituted collagen fibers were produced with properties similar to native or synthetic fibers to suit a wide range of tissue engineering applications. © 2007 Wiley Periodicals, Inc. J Biomed Mater Res 2008
Fibrillar Structure and Mechanical Properties of Collagen
Nicolas Grandin Perea
Collagen type I is among the most important stress-carrying protein structures in mammals. Despite their importance for the outstanding mechanical properties of this tissue, there is still a lack of understanding of the processes that lead to the specific shape of the stress–strain curve of collagen. Recent in situ synchrotron X-ray scattering experiments suggest that several different processes could dominate depending on the amount of strain. While at small strains there is a straightening of kinks in the collagen structure, first at the fibrillar then at the molecular level, higher strains lead to molecular gliding within the fibrils and ultimately to a disruption of the fibril structure. Moreover, it was observed that the strain within collagen fibrils is always considerably smaller than in the whole tendon. This phenomenon is still very poorly understood but points toward the existence of additional gliding processes occurring at the interfibrillar level. 1997 Academic Press
International Journal of Biological Macromolecules
An insight on type I collagen from horse tendon for the manufacture of implantable devices
2020 •
Nunzia GALLO
Biomaterials
Influence of different collagen species on physico-chemical properties of crosslinked collagen matrices
2004 •
Richard Kujat
Journal of the mechanical behavior of biomedical materials
The materials science of collagen
2015 •
Marc Meyers
Collagen is the principal biopolymer in the extracellular matrix of both vertebrates and invertebrates. It is produced in specialized cells (fibroblasts) and extracted into the body by a series of intra and extracellular steps. It is prevalent in connective tissues, and the arrangement of collagen determines the mechanical response. In biomineralized materials, its fraction and spatial distribution provide the necessary toughness and anisotropy. We review the structure of collagen, with emphasis on its hierarchical arrangement, and present constitutive equations that describe its mechanical response, classified into three groups: hyperelastic macroscopic models based on strain energy in which strain energy functions are developed; macroscopic mathematical fits with a nonlinear constitutive response; structurally and physically based models where a constitutive equation of a linear elastic material is modified by geometric characteristics. Viscoelasticity is incorporated into the exi...
