Effect of Heat Level and Expose Time on Denaturation of Collagen Tissues
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Cellular and Molecular Bioengineering ( 2020) https://doi.org/10.1007/s12195-020-00653-w
Original Article
Effect of Heat Level and Expose Time on Denaturation of Collagen Tissues I_ REM DENIZ DERMAN,1,2 ESAT CAN S¸ENEL,1,2 ONUR FERHANOG˘LU,1 I_ NCI C¸ILESIZ,1 and MURAT KAZANCI
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Electronics and Communication Engineering, Istanbul Technical University, 34469 Istanbul, Turkey; 2Biomedical Engineering Graduate Program, Istanbul Technical University, 34469 Istanbul, Turkey; and 3Biomedical Engineering Department, School of Engineering and Natural Sciences, Istanbul Medeniyet University, 34700 Istanbul, Turkey (Received 15 July 2020; accepted 16 September 2020) Associate Editor Stephanie Michelle Willerth oversaw the review of this article.
Abstract Introduction—The applied heat level and expose time are main issues in certain operations/applications, such as a laser assisted tissue welding, preparation of collagen-based biomaterials (films, implants). Therefore, the precise investigation of these parameters is crucial. The results can serve as a guideline to assess potential effects while maintaining the functionality of the collagen structures. Methods—Collagen tissues from rat-tail tendon, calfskin, and bones are soaked in buffer solutions, then examined by microscope at different temperature levels. Results—Increase in temperature reduced the microscopically observed collagen crimp contrast for calfskin and rattail tendons but not for bone tissues. The contrast level for rat tail tendon decreased down to 80% of its initial value at 37, 157, and 266 s for 70, 65, and 60 C, respectively. The decrease in the crimp contrast was about only 25% and 2% at 55 and 50 C after 2 h, respectively. 50% drop in contrast level was occurred for the skin samples at 16, 90, 110 and 1900 s for 70, 65, and 60 C, respectively. The bone samples, did not show any significant differences in contrast levels. Conclusion—The observed denaturation behaviours are in line with Arrhenius Law. This study could be expanded on to other types of tissues at wider temperature ranges to make a guideline for biological/medical processes that radiate heat in order to assess their side effects on collagen and other proteins. Keywords—Collagen, Denaturation, Arrhenius, Tissues, Expose time.
Address correspondence to Murat Kazanci, Biomedical Engineering Department, School of Engineering and Natural Sciences, Istanbul Medeniyet University, 34700 Istanbul, Turkey. Electronic mail: [email protected]
INTRODUCTION Collagen is the most abundant protein in mammals.19 It has a high tensile strength that ranges in between 1.4 and 24.6 MPa and can withstand to high forces without plastic deformation.9 Over 16 types of collagen present in the nature. However, types I, II, and III alone make up 80–90% of total collagen in the human body. Although all the collagen types constitute of polypeptide chains that form triple helix structure, they differ in small sections that can cause them to fold into different three-dimensional forms.19 These structures
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