Back to Search
Start Over
Identification of Peptides with Targeted Adhesion to Bone-Like Mineral via Phage Display and Computational Modeling
- Source :
- Cells Tissues Organs. 189:245-251
- Publication Year :
- 2008
- Publisher :
- S. Karger AG, 2008.
-
Abstract
- The challenges in engineering bone scaffolds reflect the complexity of bone as an organ. The organic-inorganic hybrid system design aims to provide signals within a conductive apatite layer to promote cell adhesion, proliferation and ultimately differentiation into bone tissue. Dual functioning peptides designed to specifically adhere to the apatite layer, while promoting cell adhesion via cell recognition sequences, may increase cell adhesion, leading to increased osteogenesis. The aim of this study is to identify peptide sequences with preferential adsorption towards apatite-based materials. Bone-like mineral films and hydroxyapatite disks were panned with a phage library to elucidate peptide sequences with favorable adsorption. Peptide sequences were analyzed using the web-based biotechnology tool RELIC and validated with a modified ELISA, in addition to being investigated using a newly developed method of high-throughput computational modeling. Peptides having the highest affinity and greatest potential to be incorporated into a dual functioning peptide design are APWHLSSQYSRT, VTKHLNQISQSY and STLPIPHEFSRE. These experiments provide a method of rationally designing peptides that adhere to apatite and that may improve bone tissue regeneration. This work also provides structure for investigating peptide/protein adsorption on apatite substrates with varied carbonate, or other impurity, content.
- Subjects :
- Models, Molecular
Paper
Histology
Phage display
Molecular Sequence Data
Enzyme-Linked Immunosorbent Assay
Peptide
Bone tissue
Bone and Bones
Apatite
Peptide Library
medicine
Amino Acid Sequence
Cell adhesion
chemistry.chemical_classification
Minerals
Regeneration (biology)
Adhesiveness
Computational Biology
Adhesion
Clone Cells
Durapatite
medicine.anatomical_structure
Biochemistry
chemistry
visual_art
Biophysics
visual_art.visual_art_medium
Adsorption
Anatomy
Peptides
Protein adsorption
Subjects
Details
- ISSN :
- 14226421 and 14226405
- Volume :
- 189
- Database :
- OpenAIRE
- Journal :
- Cells Tissues Organs
- Accession number :
- edsair.doi.dedup.....9240f8f776214a9de282b64702470e56