Literature DB >> 33643470

Effect of Heat Level and Expose Time on Denaturation of Collagen Tissues.

İrem Deniz Derman1,2, Esat Can Şenel1,2, Onur Ferhanoğlu1, İnci Çilesiz1, Murat Kazanci3.   

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 rat-tail 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. © Biomedical Engineering Society 2020.

Entities:  

Keywords:  Arrhenius; Collagen; Denaturation; Expose time; Tissues

Year:  2020        PMID: 33643470      PMCID: PMC7878606          DOI: 10.1007/s12195-020-00653-w

Source DB:  PubMed          Journal:  Cell Mol Bioeng        ISSN: 1865-5025            Impact factor:   2.321


  20 in total

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Journal:  Opt Express       Date:  1998-09-14       Impact factor: 3.894

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Authors:  Dasong Liu; Mehdi Nikoo; Gökhan Boran; Peng Zhou; Joe M Regenstein
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Authors:  Ryosuke Tanaka; Shu-ichiro Fukushima; Kunihiko Sasaki; Yuji Tanaka; Hiroyuki Murota; Takeshi Matsumoto; Kenji Matsumoto; Tsutomu Araki; Takeshi Yasui
Journal:  J Biomed Opt       Date:  2013-06       Impact factor: 3.170

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Journal:  Biochim Biophys Acta       Date:  1984-12-07

6.  Collagen fibril size and crimp morphology in ruptured and intact Achilles tendons.

Authors:  S P Magnusson; K Qvortrup; J O Larsen; S Rosager; P Hanson; P Aagaard; M Krogsgaard; M Kjaer
Journal:  Matrix Biol       Date:  2002-06       Impact factor: 11.583

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Authors:  M Jackson; D S Johnston; D Chapman
Journal:  Biochim Biophys Acta       Date:  1988-10-20

8.  Characterization of temperature dependent mechanical behavior of cartilage.

Authors:  YongSeok Chae; Guillermo Aguilar; Enrique J Lavernia; Brian J F Wong
Journal:  Lasers Surg Med       Date:  2003       Impact factor: 4.025

9.  Correlated parameter fit of arrhenius model for thermal denaturation of proteins and cells.

Authors:  Zhenpeng Qin; Saravana Kumar Balasubramanian; Willem F Wolkers; John A Pearce; John C Bischof
Journal:  Ann Biomed Eng       Date:  2014-09-10       Impact factor: 3.934

10.  Effect of carboidiimide on thermal denaturation temperature of dentin collagen.

Authors:  Milena Cadenaro; Luca Fontanive; Chiara Ottavia Navarra; Pietro Gobbi; Annalisa Mazzoni; Roberto Di Lenarda; Franklin R Tay; David H Pashley; Lorenzo Breschi
Journal:  Dent Mater       Date:  2016-01-05       Impact factor: 5.304

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