A　novel　imprinting　strategy　using　reversible　covalent　complexation　of　glycoprotein　is　described　for　creating　glycoprotein-specific　recognition　cavities　on　3-acrylamidophenylboronic　acid-immobilized　silica　nanoparticles　(SiO2@AAPBA).　Two　kinds　of　organic　silanes　(3-aminopropyltriethoxysilane　(APTES)　and　n-octyltrimethoxysilane　(OTMS))　were　then　polymerized　on　the　surface　of　SiO2@AAPBA　after　the　template　(horseradish　peroxidase　(HRP))　was　covalently　immobilized　by　forming　cyclic　boronate　complexes　and　their　influence　was　examined.　The　results　showed　that　not　only　the　silane　composition　but　also　the　relative　proportions　play　an　important　role　in　glycoprotein　imprinting.　The　template　recognition　properties　were　evaluated　by　single-protein　or　competitive　batch　rebinding　experiments,　and　the　results　showed　that　the　HRP-imprinted　silica　nanoparticles　(HRP-MIP　silica　NPs)　exhibited　higher　recognition　ability　and　selectivity　towards　the　template　than　the　nonimprinted　silica　NPs　and　their　corresponding　imprinted　factor　(a)　reached　2.71.　The　as-prepared　HRP-MIP　silica　NPs　could　not　only　differentiate　the　template　from　another　glycoprotein,　but　also　enrich　HRP　from　spiked　human　serum.　The　good　results　demonstrated　their　potential　in　glycoproteomic　analysis.