International Transaction Journal of Engineering, Management, & Applied Sciences & Technologies

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:: International Transaction Journal of Engineering, Management, & Applied Sciences & Technologies

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ISSN 2228-9860
eISSN 1906-9642
CODEN: ITJEA8


FEATURE PEER-REVIEWED ARTICLE

Vol.13(13)(2022)

  • Stability of Proteins on the Surface of Ti-6Al-4V, 316L SS and Nitinol Alloys using 2D Correlation Analysis

    Ain Athirah Rozali (School of Mechanical Engineering, College of Engineering, Universiti Teknologi MARA, MALAYSIA),
    Nik Rozlin Nik Masdek (School of Mechanical Engineering, College of Engineering, Universiti Teknologi MARA, MALAYSIA),
    (Fracture Mechanic and Materials Integrity Research Group, Universiti Teknologi MARA, MALAYSIA),
    Mardziah Che Murad, Natasha Ahmad Nawawi (School of Mechanical Engineering, College of Engineering, Universiti Teknologi MARA, MALAYSIA).

    Discipline: Biomedical engineering, Biomaterials, Engineering materials, Mechanical Engineering.

    ➤ FullText

    doi: 10.14456/ITJEMAST.2022.268

    Keywords:Bio-implants; Proteins; 2D spectroscopy; BSA; HSA

    Abstract
    Ti-6Al-4V, 316L SS and Nitinol are often used as metallic bio-implants. However, their biocompatibility with the environment of a living organism implant surfaces needs to be enhanced by exposing them to proteins such as albumin in the human body. An analysis of the adsorption of bovine and human serum albumin on the surface of these bio-implants was investigated to confirm its biocompatibility. The adsorption of both albumins was done to obtain the time for the proteins to establish stable contact with the outermost surface of the metallic bio-implant. 2D application of correlation spectroscopy was displayed as a contour map from vibrational spectra of Amide III bands. This has allowed for the selection of an optimal time of conformational stability of protein adsorption on the surface of the biomaterials. The findings revealed that albumin was in contact with the surface of Ti-6Al- 4V after 30 minutes in BSA, while 316L SS and Nitinol took longer at 60 minutes. HSA achieved a stable configuration after 15 minutes for Ti-6Al-4V, while 316L SS and Nitinol took longer, with about 40 minutes. Dynamic changes were observed through conformation of absorption between BSA and HSA that showed a significant difference between both types of protein.

    Paper ID: 13A13P

    Cite this article:

    Ain Athirah, R., Nik Rozlin, N. M., Mardziah, C. M. and Natasha, A. N. (2022). Stability of Proteins on the Surface of Ti-6Al-4V, 316L SS and Nitinol Alloys using 2D Correlation Analysis. International Transaction Journal of Engineering, Management, & Applied Sciences & Technologies, 13(13), 13A13P, 1-11. http://TUENGR.COM/V13/13A13P.pdf DOI: 10.14456/ITJEMAST.2022.268

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Other issues:
Vol.13(12)(2022)
Vol.13(11)(2022)
Vol.13(10)(2022)
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