A　kind　of　surface　glycoprotein　imprinting　over　magnetic　Fe3O4@Au　multifunctional　nanofibers　(NFs)　was　developed　and　investigated.　Magnetic　Fe3O4@Au　nanoparticles　(NPs)　as　the　core　materials　were　modified　consecutively　with　aniline,　3-aminophenylboronic　acid　(APBA)　and　acrylic　acid　to　introduce　boronic　acids　and　polymerizable　double　bonds.　With　horseradish　peroxidase　(HRP)　as　a　glycoprotein　template,　thin　protein-imprinted　films　were　fabricated　via　radical　induced　graft　copolymerization　of　monomers　on　the　surface　of　the　multifunctional　NFs.　Experimental　results　show　that　the　magnetic　multifunctional　Fe3O4@Au　NFs　can　not　only　direct　the　selective　occurrence　of　imprinting　polymerization,　but　also　drive　glycoprotein　templates　into　the　polymer　through　reversible　covalent　complex　formation.　The　results　show　that　the　imprinted　NFs　reached　saturated　adsorption　at　0.3　mg　mL(-1)　within　90　min　and　exhibited　significant　specific　recognition　towards　the　template　protein.　Moreover,　the　molecularly　imprinted　polymers　(MIPs)　were　used　to　electrochemically　detect　HRP　with　good　linearity　in　the　range　of　low　concentrations　from　0.01　to　0.30　mg　mL(-1)　through　molecular　recognition　of　K-3[Fe(CN)(6)]　current　response.　The　detection　limit　of　this　method　was　found　to　be　0.005　mg　mL(-1)　(S/N　=　3).　The　synthetic　strategy　paves　the　way　for　preparation　of　functional　nanomaterials　by　molecular　imprinting　technique　and　direct　detection　of　proteins　in　a　more　convenient,　simpler　and　cheaper　way.