Dual-functioning peptides discovered by phage display increase the magnitude and specificity of BMSC attachment to mineralized biomaterials

Abstract Design of biomaterials for cell-based therapies requires presentation of specific physical and chemical cues to cells, analogous to cues provided by native extracellular matrices (ECM). We previously identified a peptide sequence with high affinity towards apatite (VTKHLNQISQSY, VTK) using...

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Bibliographic Details
Published in:Biomaterials 2017-07, Vol.134, p.1-12
Main Authors: Ramaraju, Harsha, Miller, Sharon J, Kohn, David H., Ph.D
Format: Article
Language:English
Subjects:
Adhesion strength
Advanced Basic Science
Animals
Biocompatible Materials - chemistry
Biomimetic apatite
Biomimetic Materials - chemistry
Cell Adhesion - drug effects
Cell Adhesion - physiology
Cell Differentiation - drug effects
Cell Differentiation - physiology
Cells, Cultured
Dentistry
Fibroblasts - cytology
Fibroblasts - drug effects
Fibroblasts - physiology
Humans
Mesenchymal Stromal Cells - cytology
Mesenchymal Stromal Cells - drug effects
Mesenchymal Stromal Cells - physiology
MSCs
Osteoblasts - cytology
Osteoblasts - drug effects
Osteoblasts - physiology
Peptides
Peptides - chemistry
Peptides - pharmacology
Phage display
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Summary:Abstract Design of biomaterials for cell-based therapies requires presentation of specific physical and chemical cues to cells, analogous to cues provided by native extracellular matrices (ECM). We previously identified a peptide sequence with high affinity towards apatite (VTKHLNQISQSY, VTK) using phage display. The aims of this study were to identify a human MSC-specific peptide sequence through phage display, combine it with the apatite-specific sequence, and verify the specificity of the combined dual-functioning peptide to both apatite and human bone marrow stromal cells. In this study, a combinatorial phage display identified the cell binding sequence (DPIYALSWSGMA, DPI) which was combined with the mineral binding sequence to generate the dual peptide DPI-VTK. DPI-VTK demonstrated significantly greater binding affinity (1/KD ) to apatite surfaces compared to VTK, phosphorylated VTK (VTKphos ), DPI-VTKphos , RGD-VTK, and peptide-free apatite surfaces (p 
ISSN:0142-9612
1878-5905
DOI:10.1016/j.biomaterials.2017.04.034