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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | El-Rashidy, Aiah A. Gad, Ahmed Abu-Hussein, Abd El-Hay G. Habib, Shaymaa I. Badr, Nadia A. Hashem, Azza A. |
| Description | Author Affiliation: El-Rashidy AA ( Department of Biomaterials, Faculty of Oral and Dental Medicine, Cairo University, 11562 Cairo, Egypt. Electronic address: aiah.abdelwahab@dentistry.cu.edu.eg.); Gad A ( Department of Animal Production, Faculty of Agriculture, Cairo University, 12613 Giza, Egypt); Abu-Hussein Ael-H ( Cairo University Research Park (CURP), Faculty of Agriculture, Cairo University, 12613 Giza, Egypt.); Habib SI ( Department of Biomaterials, Faculty of Oral and Dental Medicine, Cairo University, 11562 Cairo, Egypt.); Badr NA ( Department of Biomaterials, Faculty of Oral and Dental Medicine, Cairo University-Affiliated to Faculty of dentistry, Umm Al-Qura University, Saudi Arabia.); Hashem AA ( Department of Biomaterials, Faculty of Oral and Dental Medicine, Cairo University, 11562 Cairo, Egypt.) |
| Abstract | Collagen is considered to be one of the most useful biomaterials with different medical applications. However, collagen properties differ from one source to another. The aim of this study was to extract, purify, characterize and perform preliminary biological evaluation of type I collagen from scales of Egyptian Nile Tilapia. Pepsin-solubilized collagen (PSC) was successfully prepared from Nile Tilapia fish scale waste. Lyophilized collagen was dissolved in dilute HCl to form acidic collagen solutions (ACS) which was neutralized to form gel. To confirm the biocompatibility of the produced gel, baby hamster kidney (BHK-21) fibroblast cells were seeded onto a 3D collagen gel (0.3% and 0.5%, w/v). The results of an SDS-PAGE test showed that the extracted collagens were type I collagen, with chain composition of ( 1)2 2. Thermal analysis showed that the denaturation temperature was 32 °C. X-ray diffraction (XRD) analysis and Fourier-transform infrared spectra (FTIR) showed that the extracted collagen had a triple helix structure. Active proliferation of BHK-21 cells with no signs of toxicity was evident with both collagen gel concentrations tested. The results show that Nile Tilapia scales can be an effective source of collagen extraction that could be used as a potential biomaterial in biomedical applications. |
| File Format | HTM / HTML |
| ISSN | 01418130 |
| Volume Number | 79 |
| e-ISSN | 18790003 |
| Journal | International Journal of Biological Macromolecules |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-08-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biochemistry Cichlids Collagen Type I Chemistry Fish Proteins Animals Biocompatible Materials Cell Adhesion Cell Line Cell Shape Drug Effects Pharmacology Ultrastructure Cricetinae Culture Media Gels Materials Testing Protein Denaturation Spectroscopy, Fourier Transform Infrared X-ray Diffraction Journal Article |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology Biochemistry |
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