Related Experiment Video

Updated: Aug 6, 2026

A Novel Tenorrhaphy Suture Technique with Tissue Engineered Collagen Graft to Repair Large Tendon Defects
06:36

A Novel Tenorrhaphy Suture Technique with Tissue Engineered Collagen Graft to Repair Large Tendon Defects

Published on: December 10, 2021

Effect of HEMA adsorption on the stability of native and denatured type I tendon collagen

Tomohiro Morikawa1, Takashi Nezu, Kyosuke Fukuda

  • 1Section of Fixed Prosthodontics, Division of Oral Rehabilitation, Faculty of Dental Science, Kyushu University, 3-1-1, Maidashi, Higashi-ku, Fukuoka 812-8582, Japan. tomohiro@dent.kyushu-u.ac.jp

Dental Materials Journal
|August 19, 2006
PubMed

Adsorption behavior and stabilization/destabilization effects of 2-hydroxyethyl methacrylate (HEMA) on a bovine tendon collagen (BTC) (type I), either native (N) or thermally denatured (D), were studied by IR spectroscopy and differential scanning calorimetry (DSC). The amount of HEMA adsorbed was larger on BTC(D) than on BTC(N), because BTC(D) had a larger specific surface area (SSA) as revealed from SSA measurement. Denaturation temperature (Td) of BTC(N), measured by DSC in aqueous HEMA solution, decreased from 63 degrees C to 40 degrees C with increasing HEMA concentration (CHEMA) up to 20 wt%. This destabilization might be caused by the loss of hydrophobic stabilization of the helix structure as CHEMA was increased. At CHEMA > 20 wt%, the structure of collagen was restabilized presumably due to the dehydration effect conferred by HEMA at higher concentration. BTC(D) with little helix content, however, showed only a weak endothermic peak in the DSC measurement and the Td at 40 degrees C was independent of CHEMA.

Related Concept Videos

Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
Protein Denaturation01:28

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen  forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can exist in...