Thermostability of rat sarcoma M1 procollagen solutions, procollagen fibers and whole tissues
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Thermostability of rat sarcoma M1 procollagen solutions, procollagen fibers and whole tissues Jamlet Monaselidze1 · Liana Kikalishvili2 · Manana Ramishvili2 · Maya Gorgoshidze1 · Maya Kiladze1 Received: 13 September 2019 / Accepted: 13 January 2020 © Akadémiai Kiadó, Budapest, Hungary 2020
Abstract In close to equilibrium conditions (1° per 400 min), the DSC measurements demonstrated that the melting parameters of white rat sarcoma M1 procollagen equaled to Tm = 34.4 °C and ΔTm = 2.7°, and the same parameters of fibers reconstructed from those solutions of procollagen were Tm = 38.5 °C and ΔT = 3.1°. These values were by 1.0° lower and 0.8° wider, and by 1.7° lower and 0.7° wider in comparison with the parameters of procollagen and fibers of healthy rat tissue, accordingly. The simultaneous increase in melting temperature and melting width, and a weak decrease in melting enthalpy demonstrated that sarcoma M1 procollagen had some defects. The considerable decrease by 7° in melting temperature and decrease in thermostability of procollagen fibrils in case of sarcoma M1 in comparison to the healthy norm gives a good prospective potential of using this approach as a quick DSC test to detect various sarcomas, including human sarcomas, by comparing the biopsy material or postsurgical tissues with the normal samples. Keywords Calorimeter · Calorimetry · DSC · Rat sarcoma M1 · Collagen · Thermostability
Introduction The trimetric super helix of the collagen fibril protein forms a structural basis for skin, tendons, cartilages and bones. The trimetric structure is stabilized with hydrogen bonds where hydrated water molecules make a successful contribution to the stabilization of collagen structure [1]. The environmental medium pH [2], ion strength [3, 4], water content [5, 6], specific chaperons and cross-linking formations between singe chains [7, 8] influence on the collagen thermodynamic stability and function. According to numerous published data, collagen isolated from vertebrate melts only at bit higher temperatures than the body temperature of the organism from which they are isolated [9–11]. In particular, in case of rats and mice, the melting process of acid-soluble procollagen at presence of 0.1 M NaCL cover the temperature range from 29 to 38 °C with two clear and intensive heat absorption peaks at 32 and 35.8 °C, but the melting process
* Jamlet Monaselidze [email protected] 1
E. Andronikashvili Institute of Physics, Iv. Javakhishvili Tbilisi State University, Tbilisi, Georgia
Tbilisi State Medical University, Tbilisi, Georgia
2
has one stage with Tm = 37 °C when Na ions absent [9–11]. The two-stage transition of collagen in 0.1 M NaCI directly demonstrates that collagen thermal stability is regulated by the electrostatic forces. At physiological conditions of the medium, collagen molecules aggregate and form the native-type fibrils, and this process is regulated by both electrostatic and hydrophobic (dominate) forces [12]. In this case, thermally unstable collagen melts significantly hig
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