Proteins are important in bacterial adhesion, but interactions at molecular-scales between proteins and specific functional groups are not well understood. The adhesion forces between four proteins [bovine serum albumin (BSA), protein A, lysozyme, and poly-d-lysine] and COOH, NH2 and OH-functionalized (latex) colloids were examined using colloid probe atomic force microscopy (AFM) as the function of colloid residence time (T) and solution ionic strength (IS). For three of the proteins, OH-functionalized colloids produced higher adhesion forces to proteins (2.6-30.5 nN; IS = 1 mM, T = 10 s) than COOH- and NH2-functionalized colloids (1.6-6.8 nN). However, protein A produced the largest adhesion force (8.1 ± 1.0 nN, T = 10 s) with the COOH-functionalized colloid, demonstrating the importance of specific and unanticipated protein-functional group interactions. The NH 2-functionalized colloid typically produced the lowest adhesion forces with all proteins, likely due to repulsive electrostatic forces and weak bonds for NH2-NH2 interactions. The adhesion force (F) between functionalized colloids and proteins consistently increased with residence time (T), and data was well fitted by F = ATn. The constant value of n = 0.21 ± 0.07 for all combinations of proteins and functionalized colloids indicated that water exclusion and protein rearrangement were the primary factors affecting adhesion over time. Adhesion forces decreased inversely with IS for all functional groups interacting with surface proteins, consistent with previous findings. These results demonstrate the importance of specific molecular-scale interactions between functional groups and proteins that will help us to better understand factors colloidal adhesion to surfaces.
All Science Journal Classification (ASJC) codes
- Surfaces and Interfaces
- Physical and Theoretical Chemistry
- Colloid and Surface Chemistry