NDLI: Molecular level studies on binding modes of labeling molecules with polyalanine peptides

Content Provider	Royal Society of Chemistry (RSC)
Author	Zeng, Qindao Ma, Xiaojing Yang, Yanlian Zhang, Lan Wang, Chen Wang, Chenxuan Liu, Lei Mao, Xiaobo Zhang, Min Niu, Lin
Copyright Year	2011
Abstract	In this work, the binding modes of typical labeling molecules (thioflavin T (ThT), Congo red (CR) and copper(II) phthalocyanine tetrasulfonic acid tetrasodium salt (PcCu(SO3Na)4)) on pentaalanine, which is a model peptide segment of amyloid peptides, have been resolved at the molecular level by using scanning tunneling microscopy (STM). In the STM images, ThT molecules are predominantly adsorbed parallel to the peptide strands and two binding modes could be identified. It was found that ThT molecules are preferentially binding on top of the peptide strand, and the mode of intercalated between neighboring peptides also exists. The parallel binding mode of CR molecules can be observed with pentaalanine peptides. Besides the binding modes of labeling molecules, the CR and PcCu(SO3Na)4 display different adsorption affinity with the pentaalanine peptides. The results could be beneficial for obtaining molecular level insight of the interactions between labeling molecules and peptides.
Starting Page	1592
Ending Page	1599
Page Count	8
File Format	HTM / HTML PDF
ISSN	20403364
Volume Number	3
Issue Number	4
Journal	Nanoscale
DOI	10.1039/c0nr00782j
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Phthalocyanine Congo red Adsorption Thioflavin Amyloid Copper Peptide Scanning tunneling microscope Congo
Content Type	Text
Resource Type	Article
Subject	Nanoscience and Nanotechnology

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