☆ 4.3 Article

Influence of telopeptides on the structural and physical properties of polymeric and monomeric acid-soluble type I collagen

MATERIALS SCIENCE & ENGINEERING C-MATERIALS FOR BIOLOGICAL APPLICATIONS (2017)

Journal

MATERIALS SCIENCE & ENGINEERING C-MATERIALS FOR BIOLOGICAL APPLICATIONS

Volume 77, Issue -, Pages 823-827

Publisher

ELSEVIER SCIENCE BV

DOI: 10.1016/j.msec.2017.03.267

Keywords

Polymeric collagen; Atelocollagen; Telopeptides

Funding

EPSRC Centre for Doctoral Training in Tissue Engineering and Regenerative Medicine at the University of Leeds
Southern Lights Biomaterials, New Zealand
Massey University, New Zealand
Collagen Solutions, UK
Engineering and Physical Sciences Research Council [EP/K029592/1, 1366827, EP/N00941X/1, EP/J017620/1] Funding Source: researchfish
EPSRC [EP/J017620/1, EP/K029592/1, EP/N00941X/1] Funding Source: UKRI

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Abstract

Currently two factors hinder the use of collagen as building block of regenerative devices: the limited mechanical strength in aqueous environment, and potential antigenicity. Polymeric collagen is naturally found in the cross linked state and is mechanically tougher than the monomeric, acid-soluble collagen ex vivo. The antigenicity of collagen, on the other hand, is mainly ascribed to inter-species variations in amino acid sequences of the non-helical terminal telopeptides. These telopeptides can be removed through enzymatic treatment to produce atelocollagen, although the effect of this cleavage on triple helix organization, amino acidic composition and thermal properties is often disregarded. Here, we compare the structural, chemical and physical properties of polymeric and monomeric type I collagen with and without telopeptides, in an effort to elucidate the influence of either mature covalent crosslinks or telopeptides. Circular dichroism (CD) was used to examine the triple helical conformation and quantify the denaturation temperature (T-d) of both monomeric collagen (36.5 degrees C) and monomeric atelocollagen (35.5 degrees C). CD measurements were combined with differential scanning calorimetry (DSC) in order to gain insight into the triple helix-to-coil thermal transition and shrinkage temperature (T-S) of polymeric atelo collagen (44.8 degrees C), polymeric collagen (62.7 degrees C), monomeric atelo collagen (51.4 degrees C) and monomeric collagen (66.5 degrees C). Structural and thermal analysis was combined with high pressure liquid chromatography (HPLC) to determine the content of specific collagen amino acidic residues used as markers for the presence of telopeptides and mature crosslinks. Hydroxylamine was used as the marker for polymeric collagen, and had a total content of 9.66% for both polymeric and polymeric atelo collagen; tyrosine was used as the marker for telopeptide cleavage, was expressed as 0.526% of the content of polymeric collagen and the partially-reduced content of 039% for atelocollagen. (C) 2017 The Authors. Published by Elsevier B.V.

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Mechanical performance of collagen gels is dependent on purity, α1/α2 ratio, and telopeptides

Leigh Slyker, Nicole Diamantides, Jongkil Kim, Lawrence J. Bonassar

Summary: This study investigates the compositional, mechanical, and structural differences between collagen gels sourced from different origins and processed using different methods. It was found that gel mechanics and gelation kinetics varied significantly depending on the collagen source and processing method, with differences correlating with variations in composition. Results showed that telopeptide-containing collagens had higher storage modulus and faster gelation compared to atelocollagens, despite lower purity levels.

JOURNAL OF BIOMEDICAL MATERIALS RESEARCH PART A (2022)