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Published on: January 31, 2014
Characterization of LL37 Binding to Collagen through Peptide Modification with a Collagen-Binding Domain
Ziqi Wei1, Marsha W Rolle2, Terri A Camesano1
1Department of Chemical Engineering, Worcester Polytechnic Institute, 100 Institute Road, Worcester, Massachusetts 01609, United States.
We investigated how modified antimicrobial peptides (AMPs) bind to collagen for better wound healing dressings. The collagen-binding domain (cCBD) enhances peptide stability and retention on collagen scaffolds, suggesting improved wound care applications.
Area of Science:
- Biomaterials Science
- Wound Healing
- Antimicrobial Peptides
Background:
- Collagen-based biomaterials with antimicrobial peptides (AMPs) are promising for wound healing and infection control.
- Previous work modified the AMP LL37 with a collagen-binding domain (cCBD) for improved retention on collagen dressings.
- The binding mechanism of cCBD-modified LL37 (cCBD-LL37) to collagen required further elucidation.
Purpose of the Study:
- To elucidate the binding mechanism of cCBD-LL37 to collagen.
- To investigate the role of the collagen-binding domain (cCBD) in peptide-collagen interactions.
- To assess the impact of cCBD on peptide structural stability and retention.
Main Methods:
- Affinity measurements comparing LL37 and cCBD-LL37 binding to collagen.
- Electrostatic interaction studies using varying ionic strengths and pH.
- Circular dichroism spectroscopy to analyze peptide structural stability.
- Assessment of peptide release from collagen scaffolds.
Main Results:
- cCBD-LL37 exhibited slightly higher affinity for collagen than LL37.
- cCBD partially inhibited, but did not eliminate, cCBD-LL37 binding, suggesting multi-site interactions.
- Both peptides interact with collagen via electrostatic forces, transitioning to close-range or hydrophobic interactions.
- cCBD-LL37 showed enhanced structural stability compared to LL37 under varying conditions.
- cCBD enhanced peptide retention on collagen scaffolds, despite release influenced by the electrostatic environment.
Conclusions:
- The binding of cCBD-LL37 to collagen involves both specific interactions via cCBD and non-specific forces.
- The cCBD moiety enhances the structural stability and retention of LL37 on collagen scaffolds.
- These findings provide insights into optimizing collagen-based wound dressings with modified AMPs for improved wound care.
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