Introduction: For decades, radiofrequency (RF)-induced tissue fusion has garnered great attention due to its potential to replace sutures and staples for anastomosis of tissue reconstruction. However, the complexities of achieving high bonding strength and reducing excessive thermal damage present substantial limitations of existing fusion devices.
Materials And Methods: This study proposed a discrete linkage-type electrode to carry out RF-induced intestinal anastomosis experiments. The anastomotic strength was examined by burst pressure and shear strength test. The degree of thermal damage was monitored through an infrared thermal imager. And the anastomotic stoma fused by the electrode was further investigated through histopathological and ultrastructural observation.
Results: The burst pressure and shear strength of anastomotic tissue can reach 62.2 ± 3.08 mmHg and 8.73 ± 1.11N, respectively, when the pressure, power and duration are 995 kPa, 160 W and 13 s, and the thermal damage can be controlled within limits. Histopathological and ultrastructural observation indicate that an intact and fully fused stomas with collagenic crosslink can be formed.
Conclusion: The discrete linkage-type electrode presents favorable efficiency and security in RF-induced tissue fusion, and these results are informative to the design of electrosurgical medical devices with controllable pressure and energy delivery.
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http://dx.doi.org/10.1080/13645706.2023.2291439 | DOI Listing |
RSC Chem Biol
April 2024
Department of Biochemistry and Biophysics, Department of Cancer Biology and Epigenetics Institute, Perelman School of Medicine, University of Pennsylvania PA 19104 USA
Ubiquitination is a key post-translational modification on protein lysine sidechains known to impact protein stability, signal transduction cascades, protein-protein interactions, and beyond. Great strides have been made towards developing new methods to generate discrete chains of polyubiquitin and conjugate them onto proteins site-specifically, with methods ranging from chemical synthetic approaches, to enzymatic approaches and many in between. Previous work has demonstrated the utility of engineered variants of the bacterial transpeptidase enzyme sortase (SrtA) for conjugation of ubiquitin site-specifically onto target proteins.
View Article and Find Full Text PDFMinim Invasive Ther Allied Technol
April 2024
Shanghai Institute for Minimally Invasive Therapy, School of Health Science and Engineering, University of Shanghai for Science and Technology, Shanghai, China.
Introduction: For decades, radiofrequency (RF)-induced tissue fusion has garnered great attention due to its potential to replace sutures and staples for anastomosis of tissue reconstruction. However, the complexities of achieving high bonding strength and reducing excessive thermal damage present substantial limitations of existing fusion devices.
Materials And Methods: This study proposed a discrete linkage-type electrode to carry out RF-induced intestinal anastomosis experiments.
Chem Res Toxicol
April 2015
†Department of Chemistry and Biochemistry, University of Lethbridge, Lethbridge, Alberta, Canada T1K 3M4.
Computational (DFT, MD, and free energy) methods are used to systematically compare the structural and energetic properties of C(8)-bonded 2'-deoxyguanosine (dG) adducts derived from phenolic toxins, namely, the oxygen-linked (unsubstituted) adduct ((PhO)dG) and carbon-linked adducts ((ortho-PhOH)dG or (para-PhOH)dG) that contain a hydroxyl group in the bulky moiety. Despite restricted rotation at the C(8)-X bond due to the presence of the oxygen linker, the (PhO)dG adduct likely possesses the greatest glycosidic (anti/syn) conformational flexibility at the 5'-terminus of DNA. However, the anti/syn energy difference is the smallest for the (para-PhOH)dG nucleotide at other helical positions, which correlates with the greatest conformational heterogeneity for the corresponding (NarI) adducted DNA.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!