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RISS 인기검색어
- 검색키워드
- 저자 : Corral G. M.S. (검색결과 2 건)
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Self-assembly study of type I collagen extracted from male Wistar Hannover rat tail tendons
Jeimmy González-Masís,Jorge M. Cubero-Sesin,Simón Guerrero,Sara González-Camacho,Yendry Regina Corrales-Ureña,Carlos Redondo-Gómez,José Roberto Vega-Baudrit,Rodolfo J. Gonzalez-Paz 한국생체재료학회 2020 생체재료학회지 Vol.24 No.4
Background: Collagen, the most abundant protein in the animal kingdom, represents a promising biomaterial for regenerative medicine applications due to its structural diversity and self-assembling complexity. Despite collagen’s widely known structural and functional features, the thermodynamics behind its fibrillogenic self-assembling process is still to be fully understood. In this work we report on a series of spectroscopic, mechanical, morphological and thermodynamic characterizations of high purity type I collagen (with a D-pattern of 65 nm) extracted from Wistar Hannover rat tail. Our herein reported results can be of help to elucidate differences in selfassembly states of proteins using ITC to improve the design of energy responsive and dynamic materials for applications in tissue engineering and regenerative medicine. Methods: Herein we report the systematic study on the self-assembling fibrillogenesis mechanism of type I collagen, we provide morphological and thermodynamic evidence associated to different self-assembly events using ITC titrations. We provide thorough characterization of the effect of pH, effect of salts and protein conformation on self-assembled collagen samples via several complementary biophysical techniques, including circular dichroism (CD), Fourier Transform infrared spectroscopy (FTIR), differential scanning calorimetry (DSC), atomic force microscopy (AFM), scanning electron microscopy (SEM), dynamic mechanical thermal analysis (DMTA) and thermogravimetric analysis (TGA). Results: Emphasis was made on the use of isothermal titration calorimetry (ITC) for the thermodynamic monitoring of fibrillogenesis stages of the protein. An overall self-assembly enthalpy value of 3.27 ± 0.85 J/mol was found. Different stages of the self-assembly mechanism were identified, initial stages take place at pH values lower than the protein isoelectric point (pI), however, higher energy release events were recorded at collagen’s pI. Denatured collagen employed as a control exhibited higher energy absorption at its pI, suggesting different energy exchange mechanisms as a consequence of different aggregation routes.
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Highly Economic and High Quality Zinc-flake Manufacturing by High Kinetic Processing
Ren H.,Benz H.U.,Chimal V. O.,Corral G. M.S.,Zhang Y.,Jaramillo V. D.,Zoz H. 한국분말야금학회 2006 한국분말야금학회 학술대회논문집 Vol.2006 No.1
The present paper is a parameter study of zinc flake production using a Simoloyer CM01 horizontal high energy rotary ball mill. The manufactured flakes have a dimension in thickness (t) < 1μm and diameters (d) 5-100 μm, consequently a ratio d/t up to 200. The flake geometry is mainly controlled by the variation of process parameters such as rotary speed of the rotor, ratio of powder/ball charge, load ratio of the system, process temperature, operating model and the quantity of process control agent (PCA). The Zn flakes were characterized by SEM, tap densitometry, laser diffraction and water coverage measurement.
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