Temperature-Responsive Gelation of Type I Collagen Solutions Involving Fibril Formation and Genipin Crosslinking as a Potential Injectable Hydrogel
Author(s) -
Shunji Yunoki,
Yoshimi Ohyabu,
Hirosuke Hatayama
Publication year - 2013
Publication title -
international journal of biomaterials
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 28
eISSN - 1687-8795
pISSN - 1687-8787
DOI - 10.1155/2013/620765
Subject(s) - genipin , collagen fibril , fibril , chemistry , polymer chemistry , type i collagen , chemical engineering , self healing hydrogels , biophysics , materials science , organic chemistry , biochemistry , chitosan , pathology , medicine , engineering , biology
We investigated the temperature-responsive gelation of collagen/genipin solutions using pepsin-solubilized collagen (PSC) and acid-solubilized collagen (ASC) as substrates. Gelation occurred in the PSC/genipin solutions at genipin concentrations 0–2 mM under moderate change in temperature from 25 to 37°C. The PSC/genipin solutions exhibited fluidity at room temperature for at least 30 min, whereas the ASC/genipin solutions rapidly reached gel points. In specific cases PSC would be preferred over ASC as an injectable gel system. The temperature-responsive gelation of PSC/genipin solutions was due to temperature responses to genipin crosslinking and collagen fibril formation. The elastic modulus of the 0.5% PSC/genipin gel system could be adjusted in a range of 2.5 to 50 kPa by the PSC and genipin concentrations, suggesting that a PSC/genipin solution is a potential injectable gel system for drug and cell carriers, with mechanical properties matching those of living tissues.
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