Anchoring of Polymer Loops on Enzyme-Immobilized Mesoporous ZIF-8 Enhances the Recognition Selectivity of Angiotensin-Converting Enzyme Inhibitory Peptides.

Immobilized angiotensin-converting enzyme (ACE) is a promising material for the rapid screening of antihypertensive drugs, but the nonspecific adsorption is a serious problem in separation processes involving complex biological products. In this study, triblock copolymers with dopamine (DA) block as anchors and PEG block as the main body (DA-PEGx-DA) were attached to an immobilized ACE (ACE@mZIF-8/PDA, AmZP) surface via the "grafting to" strategy which endowed them with anti-nonspecific adsorption. The influence of DA-PEGx-DA chain length on nonspecific adsorption was confirmed. The excellent specificity and reusability of the obtained ACE@mZIF-8/PDA/DA-PEG5000-DA (AmZPP5000) was validated by screening two known ACE inhibitory peptides Val-Pro-Pro (VPP, competitive inhibitory peptides of ACE) and Gly-Met-Lys-Cys-Ala-Phe (GF-6, noncompetitive inhibitory peptides of ACE) from a mixture containing active and inactive compounds. These results demonstrate that anchored polymer loops are effective for high-recognition selectivity and AmZPP5000 is a promising compound for the efficient separation of ACE inhibitors in biological samples.