Biomedical Engineering Reference
In-Depth Information
In most general cases, the binding process may be represented as the follow reaction [77]:
Figure 6. Presentation of whole protein imprinting (traditional approach) and peptide imprinting
(epitope approach). On the left, the entire protein molecule creates large imprints with high surface
availability. On the right, a small polypeptide sequence from the protein creates small imprints that bind
the template molecule at only a specific location.
n
∑
∑
P
+
TPT
→−
+
T
i
k
i
i
=
1
i
≠
k
Here, the polymer P specifically recognizes the target T
k
from a mixture of molecules T
i
(i=1, n) and forms a polymer/target complex.
If the compact molecules are larger than the characteristic size of the polymers, the
targets are effectively two-dimensional surfaces, and the recognition becomes a process
where the polymers selectively bind to specific heterogeneous surfaces. The common
property of these targets is that they have a distribution of functional groups. It is the
difference in the distribution of these functional groups on the target surfaces or along the
linear chains that make the targets recognizable.
Concerning the interactions between the template molecule and the functional monomer,
molecular imprinting technology can be categorized into covalent approach and non-covalent
approach.
The covalent imprinting method was developed by Wulff [78]. In his studies, template
species with covalently attached polymerizable functionality were copolymerized with cross-
