How do proteins interact with, and bind to nitrocellulose coated slides?
Protein binding to nitrocellulose is based on a variety of different forces, including hydrophobic interactions, electrostatic interactions and hydrogen bonding. However, the quantitative contribution of each force to the binding between proteins and nitrocellulose varies under different conditions (such as type of print buffer, protein type etc.), and is still not fully understood. Several models on how proteins are gradually attached and stably bound to the membrane structure are discussed in the literature. The most accepted model suggests that proteins are initially attracted to a membrane surface by electrostatic interaction. Long-term attachment is achieved by a combination of hydrogen bonding and hydrophobic interactions. Internal R&D tests have shown that a major part of protein fixation on nitrocellulose is mediated by hydrophobic interaction, since the use of 1% non-ionic detergent is able to wash away about 90% of the pre-bound protein. In addition, proteins can also be elut
