1. Characterization of conformational adsorbate changes on a tissue-derived substrate using Fourier transform infrared spectroscopy.
- Author
-
Kramer MA, Andrews B, Hugar DL, Jaitli A, Larsen SB, Kline BP, McEllen KN, Agrawal N, Su SM, Dammu SA, Kammeyer RM, and Ivanisevic A
- Subjects
- Adsorption, Amino Acids chemistry, Animals, Biomimetics, Bruch Membrane metabolism, Collagen chemistry, Hydrogen Bonding, Hydrophobic and Hydrophilic Interactions, Laminin chemistry, Molecular Conformation, Peptides chemistry, Surface Properties, Swine, Spectroscopy, Fourier Transform Infrared methods
- Abstract
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, RGD-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.
- Published
- 2010
- Full Text
- View/download PDF