bm0c00740_si_001.pdf (588.81 kB)
Catechol-Functionalized Elastin-like Polypeptides as Tissue Adhesives
journal contribution
posted on 2020-06-29, 12:04 authored by Malav
S. Desai, Min Chen, Farn Hing Julio Hong, Ju Hun Lee, Yaojiong Wu, Seung-Wuk LeeAdhesives
can potentially be used to achieve fast and efficient
wound closure; however, current products show poor bonding on wet
surfaces, undergo swelling, and lack adequate biocompatibility. We
designed a hydrogel adhesive with recombinant elastin-like polypeptides
(ELPs), which are flexible proteins that can be customized for biomedical
needs. The adhesive proteins are synthesized by chemically modifying
the ELPs with dopamine, which contain adhesive catechol moieties.
The resulting catechol-functional ELPs or Cat-ELPs can form flexible
hydrogels that show stable swelling in aqueous conditions at 37 °C.
We demonstrate their flexibility and viscoelastic properties through
rheology. We also show the advantage of using customizable recombinant
proteins to improve the material biological properties by demonstrating
improved fibroblast binding on Cat-ELP by adding ELP with “RGD”
peptides. We further confirmed in vivo biocompatibility
and biodegradation of Cat-ELP hydrogels by implanting them in mice
and monitoring for 10 weeks. Finally, we tested the bonding strength
of the adhesives on porcine skin through tensile pull-off and lap-shear
testing, in which we found strengths of 37 and 39 kPa, respectively.
We demonstrated the tensile bonding strength by suspending a 2 kg
mass on a one square inch (6.5 cm2) skin sample. As our
adhesives are developed further, our strategy combining recombinant
protein engineering and chemical modification will help yield an ideal
bioadhesive for wound closure.