Often the application of collagen requires the production of a structure that is mechanically robust.
This can be achieved through a process of cross-linking functional groups on the collagen
molecules. When using acid soluble collagen, the collagen molecules become insoluble and
aggregates to form a gel when the pH is increased. However, this is a weak gel and often requires
chemical cross-linking to produce a stiffer gel that is better suited to the cell growth application.
There are a number of chemical cross-linking methods that can be used to strengthen collagen gels
which include glutaraldehyde, genipin, EDC (1-Ethyl-3-(3-dimethylaminopropyl) carbodiimide,
dialdehyde starch and chitosan. The cross-linker favoured by many working in regenerative
medicine laboratories is genipin. Genipin is a naturally occurring crosslinking agent, obtained from
Geniposide which is present in gardenia fruits (Gardenia jasminoides). This compound does not
suffer from toxicity issues as with other commonly used cross-linking agents and is reported to have
antimicrobial, antitumor and anti-inflammatory properties. When it interacts with the amino acids of
collagen it produces dark blue pigments, helpfully identifying when the cross linking has occurred.

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ProColl - Collagen Gelation Protocol

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