The adsorption of preferential binding peptides to apatite-based materials |
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| Authors: | Sharon J Segvich Hayes C Smith David H Kohn |
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| Institution: | 1. Biomedical Engineering, University of Michigan, 2218 Dental Building, 1011 N University Avenue, Ann Arbor, MI 48109, USA;2. Biologic and Materials Science, University of Michigan, 2213 Dental Building, 1011 N University Avenue, Ann Arbor, MI 48109, USA;1. Cancer Molecular Pathology Research Centre, Ghaem Medical Centre, Faculty of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran;2. Department of Microbiology, Faculty of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran;3. Cancer Molecular Pathology Research Centre, Faculty of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran;4. Faculty of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran;1. Department of Chemical Engineering, Worcester Polytechnic Institute, Worcester, MA 01609, United States;2. Molecular Sciences and Engineering Team, Natick Soldier Research, Development and Engineering Center, Natick, MA 01760, United States;1. Institute for Advancing Translational Medicine in Bone & Joint Diseases, School of Chinese Medicine, Hong Kong Baptist University, Hong Kong, China;2. Academician Chen Xinzi Workroom for Advancing Translational Medicine in Bone & Joint Diseases, Kunshan RNAi Institute, Kunshan Industrial Technology Research Institute, Kunshan, Jiangsu 215347, China;3. Institute of Integrated Bioinformatic Medicine and Translational Sciences, HKBU Shenzhen Research Institute and Continuing Education, Shenzhen 518057, China;4. Shum Yiu Foon Shum Bik Chuen Memorial Centre for Cancer and Inflammation Research, HKBU Shenzhen Research Institute and Continuing Education, Shenzhen 518057, China;5. Hong Kong Baptist University – Northwestern Polytechnical University Joint Research Centre for Translational Medicine on Musculoskeletal Health in Space, Shenzhen, 518057, China;6. Key Laboratory for Space Bioscience and Biotechnology, Institute of Special Environmental Biophysics, School of Life Science, Northwestern Polytechnical University, Xi''an, 721000, China;7. Institute of Basic Research in Clinical Medicine, China Academy of Chinese Medical Sciences, Beijing, 100700, China;8. Department of Biology and Chemistry, City University of Hong Kong, 999077, Hong Kong, China;9. School of Chinese Medicine, The Chinese University of Hong Kong, Hong Kong SAR, 999077, China;10. Department of Orthopaedics, Xijing Hospital, The Fourth Military Medical University, Xi''an, 710032, China;11. Department of Orthopaedics & Traumatology, Shenzhen People''s Hospital, Second Medical College of Ji''nan University, Shenzhen, 518020, China;12. Molecular Lab, School of Pathology and Laboratory Medicine, University of Western Australia, Nedlands, WA 6009, Australia;13. Department of Chemistry, University of Florida, Gainesville, FA 32611-7200, USA;14. Department of Physiology and Functional Genomics, University of Florida, Gainesville, FA 32611-7200, USA;15. Center for Research at Bio/Nano Interface, Shands Cancer Center, University of Florida, Gainesville, FA 32611-7200, USA;p. Institute of Molecular Medicine, Peking University, Beijing, 100871, China;1. Department of Biomedical Engineering, Tufts University, 4 Colby Street, Medford, MA 02155, United States;2. Biomolecular and Materials Interface Research Group, Interdisciplinary Biomedical Research Centre, School of Science and Technology, Nottingham Trent University, Clifton Lane, Nottingham NG11 8NS, UK;1. Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, Australia;2. Department of Molecular Medicine & Pathology, Medical School, University of Auckland, Auckland, New Zealand |
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| Abstract: | The objective of this work was to identify peptide sequences with high affinity to bone-like mineral (BLM) to provide alternative design methods for functional bone regeneration peptides. Adsorption of preferential binding peptide sequences on four apatite-based substrates BLM and three sintered apatite disks pressed from powders containing 0% CO32? (HA), 5.6% CO32? (CA5), 10.5% CO32? (CA10)] with varied compositions and morphologies was investigated. A combination of phage display, ELISA, and computational modeling was used to elucidate three 12-mer peptide sequences APWHLSSQYSRT (A), STLPIPHEFSRE (S), and VTKHLNQISQSY (V), from 243 candidates with preferential adsorption on BLM and HA. Overall, peptides S and V have a significantly higher adsorption to the apatite-based materials in comparison to peptide A (for S vs. A, BLM p = 0.001, CA5 p < 0.001, CA10 p < 0.001, HA p = 0.038; for V vs. A, BLM p = 0.006, CA5 p = 0.033, CA10 p = 0.029). FT-IR analysis displayed carbonate levels in CA5 and CA10 dropped to approximately 1.1–2.2% after sintering, whereas SEM imaging displayed CA5 and CA10 possess distinct morphologies. Adsorption results normalized to surface area indicate that small changes in carbonate percentage at a similar morphological scale did not provide enough carbonate incorporation to show statistical differences in peptide adsorption. Because the identified peptides (S and V) have preferential binding to apatite, their use can now be investigated in bone and dentin tissue engineering, tendon and ligament repair, and enamel formation. |
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