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Journal of Self-Assembly and Molecular Electronics (SAME)

Editors-in-Chief: Peter Fojan and Leonid Gurevich


ISSN: 2245-4551 (Print Version),

ISSN: 2245-8824 (Online Version)
Vol: 4   Issue: Continuos Article Publication

Published In:   2016

Publication Frequency: Continuous Article Publication

Search Available Volume and Issue for Journal of Self-Assembly and Molecular Electronics (SAME)


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Improved Anti-Fouling Performance of Sintered Alumina Membrane Filters Modified with Grafted-on PEG-Brush Polymer

doi: 10.13052/jsame2245-4551.2016.002
Dennis A. Nielsen1, Lasse Christiansen1, Allan H. Holm2, Karin Dooleweerdt2, Leonid Gurevich1, and Peter Fojan1

1Department of Physics and Nanotechnology, Aalborg University, 9220 Aalborg East, Denmark
2Grundfos Holding A/S, 8850 Bjerringbro, Denmark

Abstract: [+]    |    Download File [ 2410KB ]   |    Read Article Online

Abstract: Fouling of membrane filters is the key performance limiting factor in membrane filtration. Thus fouling and anti-fouling have received much attention in recent years, covering topics from fouling mechanisms and characteristics to anti-fouling surface modifications. This paper presents a method to achieve controlled grafting of an anti-fouling poly(ethylene glycol) (PEG) brush polymer layer onto a sintered alumina membrane filter surface without reduction of the filter permeability. The obtained PEG layers were characterized using a broad range of surface techniques including Fourier transformed infrared spectroscopy, ellipsometry, atomic force microscopy, and contact angle measurements. Dead-end filtration experiments with PEG-brush modified filters showed improved fouling reversibility for the filtration of a BSA solution and significantly slowed down the fouling rate during filtration of a lysozyme solution. The cross-flow filtration of model lake-water demonstrated improved foulant removal for the PEG modified filters during backflush cleaning and thereby increased the overall throughput during a filtration cycle as compared to the bare membrane filters.

Keywords:

Probing the Amyloid Peptide-Membrane Interaction Using a Liposome Model System

doi: 10.13052/jsame2245-4551.2016.001
Liguo Tao1, Yunpeng Cao2, Cuixia Ma1, Jie Wang2, Lin Lin1, Lei Liu2, and Mingdong Dong3

1School of Food and Biological Engineering, Jiangsu University, China
2Institute for Advanced Materials, Jiangsu University, China
3Interdisciplinary Nanoscience Center (iNANO), Aarhus University, 8000 Aarhus C, Denmark

Abstract: [+]    |    Download File [ 2288KB ]   |    Read Article Online

Abstract: The aggregation of amyloid peptides is closely related to the pathogenesis of degenerative diseases. More and more evidence implies that the proto fibrillar intermediates rather than the mature amyloid fibrils are the toxic species related to the membrane disruption. In this work we found that the self-assembling intermediates of Aβ33-42 during early aggregation are able to break down the liposome. During the process of amyloid peptide (Aβ33-42) intermediate binding to liposome, the Aβ-sheet secondary structure of peptide took change on the molecular level which was characterized by circular dichroism (CD) spectra. The small micelles were formed due to the disruption of amyloid peptide, and further to grow into big irregular complexes with further incubation, which is characterized by the assay of disrupting liposome membrane and atomic force microscopy (AFM). This founding paved the way to understand the interactions between the amyloid peptide and membranes, and support the amyloid peptide nanostructure formed in the early stage of aggregation has good affinity with membrane.

Keywords: Probing the Amyloid Peptide-Membrane Interaction Using a Liposome Model System

River Publishers: Journal of Self-Assembly and Molecular Electronics (SAME)