Glutaraldehyde as a crosslinking agent for collagen-based biomaterials

Abstract

The formation of Schiff bases during crosslinking of dermal sheep collagen (DSC) with glutaraldehyde (GA), their stability and their reactivity towards GA was studied. All available free amine groups had reacted with GA to form a Schiff base within 5 rain after the start of the reaction under the conditions studied (0.5% (w/w) GA). Before crosslinks are formed the hydrolysable Schiff bases initially present were stabilized by further reaction with GA molecules. An increase in shrinkage temperature (Ts) from 56 °C for non-crosslinked DSC (N-DSC) to 78°C for GA crosslinked DSC (G-DSC) was achieved after crosslinking for 1 h. From the relationship between the free amine group content and the Ts during crosslinking it was concluded that higher GA concentrations and longer reaction times will result in the introduction of pendant-GA-related molecules rather than crosslinks. After 24 h crosslinking an average uptake of 3 GA molecules per reacted amine group was found. No increase in the tensile strength of the materials was observed after crosslinking, which may be a result of formation of crosslinks within the fibres rather than in between fibres. Aligning of the fibres by applying a pre-strain to the samples and subsequent crosslinking yielded materials with an increased tensile strength.

The Retention and Drainage Behavior of Cross-linked Gelatin with Glutaraldehyde in a Papermaking System

“…3. Cross-linked gelatin showed a new absorption band at 265 nm, which was ascribed to the formation of a Schiff base structure between the aldehyde group and the primary amine group (Bowes and Cater 1968;Damink et al 1995). This result is additional evidence of the crosslinking reaction between gelatin and glutaraldehyde.…”

Cytocompatibility studies of mouse pancreatic islets on gelatin - PVP semi IPN scaffolds in vitro: Potential implication towards pancreatic tissue engineering

“…Cross linking with GTA involves reacting the free amino groups of the polypeptide chains (lysine or hydroxylysine) with aldehyde groups of the GTA. 20 However during in vivo transplantation, GTA can be toxic due to the degradation of polymer. 20,21 Hence biocompatible water soluble carbodiimide class cross linker EDC has also been tried, which is widely used for cross linking collagen in dermal tissue engineering.…”

“…20 However during in vivo transplantation, GTA can be toxic due to the degradation of polymer. 20,21 Hence biocompatible water soluble carbodiimide class cross linker EDC has also been tried, which is widely used for cross linking collagen in dermal tissue engineering. 22 EDC crosslink the amino groups of one polypeptide chain with the carboxylic groups of the adjacent polypeptide chain by forming the extra amide bond without its incorporation.…”

Electrospinning of Gelatin Functionalized with Silver Na-noparticles for Nanofiber Fabrication

“…They also shrunk slightly from their original dimensions. The change in color of the gelatin upon crosslinking with GTA is caused by the formation of aldimine linkages (-CH=N-) between the free amino groups of lysine or hydroxylysine amino acid residues of the protein and the aldehyde groups of GTA [25,30].…”