Characterization of conformational adsorbate changes on a tissue-derived substrate using Fourier transform infrared spectroscopy.
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.
Weldon School of Biomedical Engineering, Purdue University, West Lafayette, Indiana, United States.
Marcus A
MA
Kramer
Benjamin
B
Andrews
Daniel L
DL
Hugar
Arjun
A
Jaitli
Seij B
SB
Larsen
Benjamin P
BP
Kline
Kristin N
KN
McEllen
Namita
N
Agrawal
Si Min
SM
Su
Sandhya A
SA
Dammu
Ryan M
RM
Kammeyer
Albena
A
Ivanisevic
D000327:Adsorption; D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D032701:Biomimetics; D016570:Bruch Membrane / Q000378:metabolism; D003094:Collagen / Q000737:chemistry; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D007797:Laminin / Q000737:chemistry; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*; D013499:Surface Properties; D013552:Swine
D000596:Amino Acids; D007797:Laminin; D010455:Peptides; D003094:Collagen