Refolding Behavior of Urea-Induced Denaturation Collagen

Controlling the Trimerization of the Collagen Triple-Helix by Solvent Switching

“…There have only been a limited number of investigations concerning the influence of the solvents on the natural collagen protein where the studies primarily focused on the solvation of the natural triple helices by nonaqueous solvents in swelling collagen fibers or stabilizing the natural triple helices against urea and GdnHCl using polyols (e.g., glycerol and erythritol). ,,, Meanwhile, all investigations into the solvent effects on the CHP trimers have focused on stabilizing the triple helix rather than dissociating it. Our study not only validated the effects of these solutions (including the polyols and denaturants) on the peptide triple helix but also extended the scope to multiple types of cosolvents, providing a reference for future investigations into the solvent effects on natural collagen.…”

“…Organic solvents, denaturants, acids, or detergents can often cause the unfolding of natural proteins, leading to activity loss, whereas removal of the denaturing solutions may partially or completely recover the native conformation of the denatured proteins. − While the structural effects of various solvents (or cosolvents) on many globular proteins have been investigated for decades, − their effects on the stability of the collagen triple-helix are underexplored . Particularly, no data comparing the solvent effects on the triple-helix formation by the collagen mimetic peptides have been reported.…”

“…26−30 While the structural effects of various solvents (or cosolvents) on many globular proteins have been investigated for decades, 31−33 their effects on the stability of the collagen triple-helix are underexplored. 34 Particularly, no data comparing the solvent effects on the triple-helix formation by the collagen mimetic peptides have been reported. Here, we evaluated the effects of 22 commonly available and watermiscible cosolvents on the triple-helix formation and stability of the collagen mimetic peptides to develop a simple and efficient solvent-switch technique (Figure 1b) to control the self-assembly and collagen hybridization of the peptide singlestrands for straightforward applications in histopathology and in vivo.…”

Effects of γ-ray irradiation on the molecular structure of collagen in different product forms

“…In particular, in the case of collagen stored in a fluid medium, exceeding the critical threshold (approximately 40 °C for bovine tendon collagen) results in the unwinding of the collagen, which results in a sharp drop in its biocompatibility and mechanical properties. 7 Ethylene oxide is the most commonly used reagent for chemical sterilization, gaining in popularity, and is used in collagen-based wound dressings and suture materials. A major advantage of ethylene oxide processing is that it can be performed at relatively low temperatures; however, ethylene oxide is a suspected carcinogen that may produce toxic residues and is unsuitable for materials stored in fluid media.…”

Low-Cost and High-Strength Soybean Meal Adhesives Modified by Tannin–Phenol–Formaldehyde Resin

“…Modifying methods, such as denaturants [16,17], cross-linking agents [18][19][20][21], graft modifications [22,23], and biomimetics [24], are commonly added to modify protein molecules to enhance the protein adhesive performance. As a denaturant [25], urea exposes the hydrophobic groups of protein molecules, significantly improving the water resistance of protein adhesives. However, urea denaturation alone may not meet the requirements for indoor plywood, necessitating further treatment to enhance the bonding strength.…”