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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
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LL37 and collagen-binding domain-mediated LL37 binding with type I collagen: Quantification via QCM-D.
Ziqi Wei1, Marsha W Rolle2, Terri A Camesano1
1Department of Chemical Engineering, Worcester Polytechnic Institute, 100 Institute Road, Worcester, MA 01609, United States.
Colloids and Surfaces. B, Biointerfaces
|September 30, 2022
Summary
Antimicrobial peptide delivery for wound healing was improved using a collagen-binding domain (cCBD) to anchor peptides to dressings. This study quantifies peptide-collagen binding, showing cCBD enhances peptide retention on collagen for better wound care.
Area of Science:
- Biomaterials Science
- Wound Healing Research
- Biophysics
Background:
- Antimicrobial peptide (AMP)-loaded biomaterials offer a dual approach for wound healing and infection prevention.
- The cathelicidin antimicrobial peptide LL37 was previously modified with a collagen-binding domain (cCBD) for improved binding to collagen-based wound dressings.
- Direct quantification of LL37 and cCBD-LL37 binding to collagen was lacking.
Purpose of the Study:
- To establish and characterize a collagen layer on sensors for quantifying peptide-collagen interactions.
- To compare the binding and retention of unmodified LL37 and cCBD-LL37 with collagen.
- To investigate the influence of surface hydrophobicity on collagen adsorption.
Main Methods:
- Quartz crystal microbalance with dissipation monitoring (QCM-D) for quantifying peptide-collagen binding and collagen deposition.
- Immunohistochemistry (IHC) and Atomic Force Microscopy (AFM) for observing collagen self-assembly and surface characterization.
- Comparative analysis of collagen adsorption on hydrophilic (SiO2) and hydrophobic (polystyrene) surfaces.
Main Results:
- A robust protocol for collagen deposition on QCM-D sensors was established, with self-assembly confirmed by IHC and AFM.
- Hydrophobic surfaces demonstrated significantly higher collagen adsorption compared to hydrophilic surfaces.
- While LL37 and cCBD-LL37 showed similar binding affinities to collagen, cCBD-LL37 exhibited superior retention after washing, highlighting the anchoring advantage.
Conclusions:
- Hydrophobic surfaces are advantageous for establishing collagen layers for peptide binding studies.
- The collagen-binding domain (cCBD) enhances the retention of antimicrobial peptides on collagenous wound dressings.
- This work provides a quantitative method for assessing peptide-collagen interactions and supports the use of cCBD-modified AMPs for advanced wound healing applications.
Keywords:
Antimicrobial peptideCathelicidin LL37CollagenCollagen-binding domainPeptide deliveryQuartz crystal microbalance with dissipation monitoringMore Related Videos
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