Genipin, a New Type of Protein Crosslinking Reagent from Gardenia Fruits

Fujikawa, Shigeaki; Nakamura, Shigeyuki; Koga, Kunimasa

doi:10.1080/00021369.1988.10868755

Cited by 22 publications

(27 citation statements)

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“…The reaction mechanism of genipin with biological tissue is still not understood. In the study of the structure of a blue pigment formed from glycine and genipin, Fujikawa et al 27,28 found multiple blue components. They reported that the simplest component in the blue pigment was a 1:1 adduct.…”

Section: Discussionmentioning

confidence: 99%

“…These crosslinking agents can be used to bridge amino groups of lysine, hydroxylysine, or arginine residues of different polypeptide chains by monomeric or oligomeric crosslinks. 5,10,[26][27][28] Glutaraldehyde has been used extensively as a crosslinking agent for fixing biological tissue. 5 Using its aldehyde functional groups, glutaraldehyde reacts primarily with the -amino groups of lysyl or hydroxylysyl residues within biological tissue.…”

Section: Discussionmentioning

confidence: 99%

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Crosslinking characteristics and mechanical properties of a bovine pericardium fixed with a naturally occurring crosslinking agent

Sung

Chang

Chiu

et al. 1999

J. Biomed. Mater. Res.

163

123

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Currently available crosslinking agents used in fixing bioprostheses are all highly (or relatively highly) cytotoxic, which may induce an adverse inflammatory reaction in vivo. It is therefore desirable to provide a crosslinking agent that is of low cytotoxicty and may form stable and biocompatible crosslinked products. To achieve this goal, a naturally occurring crosslinking agent-genipin-was used by our group to fix biological tissues. Genipin may be obtained from its parent compound, geniposide, which may be isolated from the fruits of Gardenia jasminoides Ellis. In our previous studies, it was found that the cytotoxicity of genipin is significantly lower than both glutaraldehyde and an epoxy compound. Also, it was shown that genipin can form stable and biocompatible crosslinked products. The present study further investigates the crosslinking characteristics and mechanical properties of a genipin-fixed bovine pericardium. Fresh and glutaraldehyde- and epoxy-fixed counterparts were used as controls. It was found that the denaturation temperatures of the glutaraldehyde- and genipin-fixed tissues were significantly greater than the epoxy-fixed tissue, although their fixation indices were comparable. The mechanical properties of fresh bovine pericardium are anisotropic. However, fixation tended to eliminate tissue anisotropy. The tendency in the elimination of tissue anisotropy for the genipin-fixed tissue was more remarkable than for the glutaraldehyde- and epoxy-fixed tissues. In addition, the genipin-fixed tissue had the greatest ultimate tensile strength and toughness among all the fixed tissues. Distinct patterns in rupture were observed in the study: The torn collagen fibers of the genipin- and glutaraldehyde-fixed tissues appeared to be bound together, while those of fresh and the epoxy-fixed tissues stayed loose. The results obtained in the study suggests that tissue fixation in glutaraldehyde, epoxy compound, and genipin may produce distinct crosslinking structures. The differences in crosslinking structure may affect the crosslinking characteristics and mechanical properties of the fixed tissues.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Crosslinking characteristics and mechanical properties of a bovine pericardium fixed with a naturally occurring crosslinking agent

Sung

Chang

Chiu

et al. 1999

J. Biomed. Mater. Res.

163

123

View full text Add to dashboard Cite

show abstract

“…In the study of the structure of a blue pigment formed from glycine and genipin, Fujikawa's group found multiple blue components. 27,28 They reported that the simplest component in the blue pigment was a 1:1 adduct. From the structure of this simplest component, they proposed that genipin reacts spontaneously with an amino acid to form a nitrogen-iridoid, which undergoes dehydration to form an aromatic monomer.…”

Section: Crosslinking Structurementioning

confidence: 99%

Crosslinking of biological tissues using genipin and/or carbodiimide

Sung

Chang

et al. 2003

J Biomedical Materials Res

250

201

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The study was to investigate the crosslinking characteristics, mechanical properties, and resistance against enzymatic degradation of biological tissues after fixation with genipin (a naturally occurring crosslinking agent) and/or carbodiimide. Fresh tissue was used as a control. It was found that both genipin and carbodiimide are effective crosslinking agents for tissue fixation and genipin crosslinking is comparatively slower than carbodiimide crosslinking. Additionally, tissue fixation in genipin and/or carbodiimide may produce distinct crosslinking structures. Carbodiimide may form intrahelical and interhelical crosslinks within or between tropocollagen molecules, whereas genipin may further introduce intermicrofibrillar crosslinks between adjacent collagen microfibrils. The stability (denaturation temperature and resistance against enzymatic degradation) of the fixed tissue is mainly determined by its intrahelical and interhelical crosslinks. In contrast, intermicrofibrillar crosslinks significantly affect the mechanical properties (tissue shrinkage during fixation, tensile strength, strain at break, and ruptured pattern) of the fixed tissue. Moreover, the degree of enzymatic degradation of the fixed tissue may be influenced by three factors: the availability, to the enzyme, of recognizable cleavage sites, the degree of crosslinking, and the extent of helical integrity of tropocollagen molecules in tissue.

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“…Genipin reacts spontaneously with an amino acid to form a nitrogen-iridoid, which undergoes dehydration to form an aromatic monomer. Dimerrization occurs at the second stage, perhaps by radical reaction [16,17].…”

Section: Introductionmentioning

confidence: 99%