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April 30, 2026Materials Advances0 citationsOpen Access

Glycine-proline-hydroxyproline Modification Improves the Affinity of CEMP1 N-terminal 20-residue Peptide to Collagen

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YSYuxiang SunYangzhou UniversityYZYanqian ZhaoYangzhou UniversityLXLi XuYangzhou University

Key Points

  • To enhance the affinity of CEMP1 N-terminal 20-residue peptide for collagen through glycine-proline-hydroxyproline modification.
  • Glycine-proline-hydroxyproline modification applied to CEMP1 n-terminal peptide.
  • Affinity measurements for collagen compared before and after modification.
  • Glycine-proline-hydroxyproline modification significantly increased the affinity of the peptide for collagen.
  • Improved binding may enhance the application of CEMP1 in tissue engineering.

Abstract

N-terminal 20 peptide of cementum matrix protein 1 (CEMP1) shows the affinity for hydroxyapatite (HAP) and induces the nucleation of HAP. However, its poor affinity for collagen limits its application...

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Cite This Study

Sun et al. (2026) studied this question.

synapsesocial.com/papers/69f2a4b78c0f03fd67763c87https://doi.org/10.1039/d5ma01497b
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1A novel mineralization-inductive peptide derived from CEMP1functinal domains2025
  2. 2Incorporation of Azapeptoid Residues Into Collagen2025 · 1 citations
  3. 3Data‐Driven Engineering of Thermostable Collagen‐Mimetic Peptoid Triple Helices2026
  4. 4Investigating the Role of Amino Acids in Short Peptides for Hydroxyapatite Binding and Osteogenic Differentiation of Mesenchymal Stem Cells to Aid Bone Regeneration2024 · 26 citations
  5. 5From Collagen Mimetics to Collagen Hybridization and Back2024 · 22 citations