Journal
LANGMUIR
Volume 26, Issue 23, Pages 18083-18088Publisher
AMER CHEMICAL SOC
DOI: 10.1021/la1038766
Keywords
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Funding
- National Science Foundation [CHE-0418902]
- Center for Authentic Science Practice in Education (CASPiE)
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Fourier transform infrared (FT-IR) spectroscopy is utilized to observe adsorbate interactions with a tissue-derived collagen scaffold extracted from the Bruch's membrane of pig eyes. The characterization includes conformational changes in isoleucine, polyisoleucine, collagen-binding peptide, ROD-tagged collagen-binding peptide, and laminin after adsorption onto the substrate. Isotopically labeled isoleucine is further utilized to understand changes in the biomolecular structure upon binding to a tissue-derived surface. The adsorbates associated with the collagen scaffold predominately through hydrophobic interactions and hydrogen bonding. The results of this study can be used to improve our understanding of surface chemistry changes during the engineering of biomimetic scaffolds before and after biomolecule adsorption.
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