antibodies covalently immobilized on actin filaments for fast myosin driven analyte transport抗体共价固定化对肌动蛋白丝快肌凝蛋白驱动分析物运输.pdfVIP

antibodies covalently immobilized on actin filaments for fast myosin driven analyte transport抗体共价固定化对肌动蛋白丝快肌凝蛋白驱动分析物运输.pdf

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antibodies covalently immobilized on actin filaments for fast myosin driven analyte transport抗体共价固定化对肌动蛋白丝快肌凝蛋白驱动分析物运输

Antibodies Covalently Immobilized on Actin Filaments for Fast Myosin Driven Analyte Transport 1 1 1 2 3 2 Saroj Kumar , Lasse ten Siethoff , Malin Persson , Mercy Lard , Geertruy te Kronnie , Heiner Linke , ˚ 1* Alf Mansson 1 School of Natural Sciences, Linnaeus University, Kalmar, Sweden, 2 The Nanometer Structure Consortium and Division of Solid State Physics, Lund University, Lund, Sweden, 3 Department of Women’s and Children’s Health, University of Padua, Padova, Italy Abstract Biosensors would benefit from further miniaturization, increased detection rate and independence from external pumps and other bulky equipment. Whereas transportation systems built around molecular motors and cytoskeletal filaments hold significant promise in the latter regard, recent proof-of-principle devices based on the microtubule-kinesin motor system have not matched the speed of existing methods. An attractive solution to overcome this limitation would be the use of myosin driven propulsion of actin filaments which offers motility one order of magnitude faster than the kinesin- microtubule system. Here, we realized a necessary requirement for the use of the actomyosin system in biosensing devices, namely covalent attachment of antibodies to actin filaments using heterobifunctional cross-linkers. We also demonstrated consistent and rapid myosin II driven transport where velocity and the fraction of motile actin filaments was negligibly affected by the presence of antibody-antigen complexes at rather high density (.20 mm21). The results, however, also demonstrated that i

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