Journal
POLYMERS
Volume 13, Issue 15, Pages -Publisher
MDPI
DOI: 10.3390/polym13152549
Keywords
bone morphogenetic protein (BMP-2); BMP-2 knuckle epitope; disulphide bridging; cyclic peptide
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Funding
- National Health Research Institutes [BN-109-PP-09]
- Kaohsiung Medical University [KMU-KI109004]
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In this study, novel cyclic peptide analogues were designed to investigate interactions involved in osteogenesis, demonstrating higher binding affinity of peptides with active regions inside the ring. In vitro experiments further confirmed the potential role of these cyclic peptide analogues in osteogenesis.
In the current study, we designed four cyclic peptide analogues by incorporating two cysteine residues in a BMP-2 linear knuckle epitope in such a way that the active region of the peptide could be either inside or outside the cyclic ring. Bone morphogenetic protein receptor BMPRII was immobilized on the chip surface, and the interaction of the linear and cyclic peptide analogues was studied using surface plasmon resonance (SPR). From the affinity data, the peptides with an active region inside the cyclic ring had a higher binding affinity in comparison to the other peptides. To confirm that our affinity data are in line in vitro, we studied the expression levels of RUNX2 (runt-related transcription factor) and conducted an osteogenic marker alkaline phosphatase (ALP) assay and staining. Based on the affinity data and the in vitro experiments, peptide P-05 could be a suitable candidate for osteogenesis, with higher binding affinity and increased RUNX2 and ALP expression in comparison to the linear peptides.
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