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Pena-Francesch, A.

Publications and source records attributed to Pena-Francesch, A..

2 recordsLinked to original sources

Squid Ring Teeth Coated Mesh Improves Abdominal Wall Repair

BackgroundHernia repair is a common surgical procedure with mesh often used. Current mesh materials have a high incidence of repair failures, due to poor tissue integration, and complications such as seroma and pain. Polypropylene (PP) mesh is the standard material in hernia repair secondary to its material durability; however, failures still approach 15%. In this first time animal study, we hypothesized that squid ring teeth (SRT), a biologically-derived high strength protein, coated polypropylene (SRT-PP) mesh, would offer enhanced tissue integration and strength compared to standard PP mesh, while proving biocompatibility for in vivo use.\n\nMaterials and methodsPolypropylene mesh was coated with SRT. Mechanical properties and cell proliferation studies of the composite mesh were performed in vitro. Rats underwent inlay mesh implantation in an anterior abdominal wall defect model. Repair was assessed clinically and radiographically, with integration evaluated by histology and mechanical testing.\n\nResultsCell proliferation was enhanced on SRT-PP composite mesh. This was corroborated by abdominal wall histology, dramatically diminished cranio-caudal mesh contraction, improved strength testing, and higher tissue failure strain following in vivo implantation. There was no increase in complications with SRT, with regard to seroma or visceral adhesion. No foreign body reactions were noted on liver histology.\n\nConclusionSRT-PP mesh showed better tissue integration than PP mesh. SRT is a high strength protein that is applied as a coating to augment mesh-tissue integration leading to improvements in abdominal wall stability with potential to reduce re-intervention for failures.

bioengineering

ULTRAFAST LASER-PROBING SPECTROCOPY FOR STUDYING MOLECULAR STRUCTURE OF POLYMERIC PROTEINS

We report the development of a new technique to screen protein crystallinity quantitatively based on laser-probing spectroscopy with sub-picosecond resolution. First, we show theoretically that the temperature dependence of the refractive index of a polymeric protein is correlated to its crystallinity. Then, we performed time-domain thermo-transmission experiments on purified semi-crystalline proteins, both native and recombinant (i.e., silk and squid ring teeth), and also on intact E. coli cells bearing overexpressed recombinant protein. Our results demonstrate, for the first time, quantification of crystallinity in real time for polymeric proteins. Our approach can potentially be used for screening an ultra-large number of polymeric proteins in vivo.

biophysics