Characteristics of Collagen Changes in Small Intestine Anastomoses Induced by High-Frequency Electric Field Welding

Author:

Zhu Caihui,Yin LiORCID,Xu JianzhiORCID,Yang Xingjian,Wang HaoORCID,Xiang XiaoweiORCID,Liu Haotian,Liu KefuORCID

Abstract

High-frequency electric field welding-induced tissue fusion has been explored as an advanced surgical method for intestinal anastomoses; however, intrinsic mechanisms remain unclear. The aim of this study was to investigate microcosmic changes of collagen within the fusion area, with various parameters. Ex vivo small intestine was fused with mucosa–mucosa. Four levels of compressive pressure (100 kPa, 150 kPa, 200 kPa, 250 kPa) were applied for 10 s in order to fuse the colons under a power level of 140 W. Then, collagen fibers of the fusion area were examined by fibrillar collagen alignment and TEM. Three levels of power (90 W, 110 W, 140 W) and three levels of time (5 s, 10 s, 20 s) were applied in order to fuse colons at 250 kPa, and then collagen within the fusion area was examined by Raman spectroscopy. Fibrillar collagen alignment analysis showed that with the increase in compression pressure, alignment of the collagen in the fusion area gradually increased, and the arrangement of collagen fibers tended to be consistent, which was conducive to the adhesion of collagen fibers. TEM showed that pressure changed the distribution and morphology of collagen fibers. Raman spectroscopy showed that increased power and time within a certain range contributed to collagen cross linking. Peak positions of amide I band and amide III band changed. These results suggested that higher power and a longer amount of time resulted in a decrease in non-reducible cross links and an increase in reducible cross links. Compression pressure, power, and time can affect the state of collagen, but the mechanisms are different. Compressive pressure affected the state of collagen by changing its orientation; power and time denatured collagen by increasing temperature and improved the reducible cross linking of collagen to promote tissue fusion.

Funder

National Natural Science Foundation of China

Pioneering Project of the Academy for Engineering and Technology of Fudan University

Publisher

MDPI AG

Subject

Molecular Biology,Biochemistry

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