NDLI: SPRi determination of inter-peptide interaction by using 3D supramolecular co-assembly polyrotaxane film.

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SPRi determination of inter-peptide interaction by using 3D supramolecular co-assembly polyrotaxane film.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wang, Yanmei Wang, Zhiyou Zheng, Zheng Yang, Mo Wang, Chenxuan Cheng, Zhiqiang Yang, Yanlian Zhang, Dongdong Song, Lusheng Li, Shaopeng Han, Baohang Wang, Chen Zhou, Wenfei Zhu, Jinsong
Description	Author Affiliation: Wang Y ( National Center for Nanoscience and Technology, Beijing 100190, PR China.); Wang C ( National Center for Nanoscience and Technology, Beijing 100190, PR China); Cheng Z ( National Center for Nanoscience and Technology, Beijing 100190, PR China); Zhang D ( National Center for Nanoscience and Technology, Beijing 100190, PR China.); Li S ( National Center for Nanoscience and Technology, Beijing 100190, PR China.); Song L ( National Center for Nanoscience and Technology, Beijing 100190, PR China.); Zhou W ( National Center for Nanoscience and Technology, Beijing 100190, PR China.); Yang M ( National Center for Nanoscience and Technology, Beijing 100190, PR China.); Wang Z ( National Center for Nanoscience and Technology, Beijing 100190, PR China.); Zheng Z ( Beihang University, Beijing 100191, PR China.); Han B ( National Center for Nanoscience and Technology, Beijing 100190, PR China.); Wang C ( National Center for Nanoscience and Technology, Beijing 100190, PR China.); Yang Y ( National Center for Nanoscience and Technology, Beijing 100190, PR China.); Zhu J ( National Center for Nanoscience and Technology, Beijing 100190, PR China.)
Abstract	Accurate measurement of inter-peptide interactions is beneficial for in-depth understanding disease-related protein folding and peptide aggregation, and further for designing and selecting potential peptide drugs to the target antigen. Herein, we demonstrate a 3D polyrotaxane (PRX) surface for detecting peptides interactions by surface plasmon resonance imaging (SPRi). This surface is supramolecular self-assembly monolayer (SAM) structure fabricated by threading -cyclodextrans ( -CD) through a linear polyethylene glycol (PEG) chain fixed on gold chip surface to form pseudopolyrotaxane, and further capping the pseudopolyrotaxane with bulky terminated group to form PRX film. The hydroxyl groups of -CD can provide more active sites to increase molecules immobilization density, and PEG chain has unique protein non-fouling feature. We chose Alzheimer's disease marker ß-amyloid 40 (Aß40) as model peptide, and detected the interaction between it and its inhibitors KLVFFK6 by SPRi. As a striking result, the specific adsorption of KLVFFK6 solution at the concentration of 352µM on Aß40-PRX was 700RU, whereas PEG SAM surface gave no significant binding. Interaction between other lower molecular weight peptides was detected via PRX surface, and the relatively weak interactions (KD=1.73×10(-4)M) between LPFFD (Mw=0.6kDa) and amylin20-29 (Mw=1.0kDa) are successfully detected.
ISSN	09565663
Volume Number	66
e-ISSN	18734235
Journal	Biosensors and Bioelectronics
Language	English
Publisher	Elsevier
Publisher Date	2015-04-15
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Amyloid Beta-peptides Metabolism Cyclodextrins Chemistry Peptide Fragments Peptides Poloxamer Rotaxanes Surface Plasmon Resonance Instrumentation Amino Acid Sequence Analysis Equipment Design Molecular Sequence Data Surface Properties Journal Article Research Support, Non-u.s. Gov't Discipline Biotechnology
Content Type	Text
Resource Type	Article
Subject	Nanoscience and Nanotechnology Medicine Biophysics Biomedical Engineering Biotechnology Electrochemistry

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