Synergistic Inhibitory Effect of Peptide-Organic Coassemblies on Amyloid Aggregation

Lin Niu; Lei Liu; Wenhui Xi; Qiusen Han; Qiang Li; Yue Yu; Qunxing Huang; Fuyang Qu; Meng Xu; Yibao Li; Huiwen Du; Rong Yang; Jacob Cramer; Kurt V. Gothelf; Mingdong Dong; Flemming Besenbacher; Qingdao Zeng; Chen Wang; Guanghong Wei; Yanlian Yang

doi:10.1021/acsnano.5b07396

Synergistic Inhibitory Effect of Peptide-Organic Coassemblies on Amyloid Aggregation

Lin Niu
, Lei Liu
, Wenhui Xi
, Qiusen Han
, Qiang Li
, Yue Yu
, Qunxing Huang
, Fuyang Qu
, Meng Xu
, Yibao Li
, Huiwen Du
, Rong Yang
, Jacob Cramer
, Kurt V. Gothelf
, Mingdong Dong
, Flemming Besenbacher
, Qingdao Zeng
, Chen Wang^*
, Guanghong Wei
, Yanlian Yang

^*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

48 Citations (Scopus)

Abstract

Inhibition of amyloid aggregation is important for developing potential therapeutic strategies of amyloid-related diseases. Herein, we report that the inhibition effect of a pristine peptide motif (KLVFF) can be significantly improved by introducing a terminal regulatory moiety (terpyridine). The molecular-level observations by using scanning tunneling microscopy reveal stoichiometry-dependent polymorphism of the coassembly structures, which originates from the terminal interactions of peptide with organic modulator moieties and can be attributed to the secondary structures of peptides and conformations of the organic molecules. Furthermore, the polymorphism of the peptide-organic coassemblies is shown to be correlated to distinctively different inhibition effects on amyloid-β 42 (Aβ42) aggregations and cytotoxicity.

Original language	English
Journal	A C S Nano
Volume	10
Issue	4
Pages (from-to)	4143-4153
Number of pages	11
ISSN	1936-0851
DOIs	https://doi.org/10.1021/acsnano.5b07396
Publication status	Published - 26 Apr 2016

Keywords

ALZHEIMERS-DISEASE
BETA
BINDING
CONSTRAINTS
DYNAMICS
FIBRIL FORMATION
PROTEIN
SEQUENCE
SPECTROSCOPY
TOXICITY
amyloid beta (A beta) peptide
amyloid cytotoxicity
inhibitory effect
peptide aggregation
peptide motif
polymorphism effect
scanning tunneling microscopy

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title = "Synergistic Inhibitory Effect of Peptide-Organic Coassemblies on Amyloid Aggregation",

abstract = "Inhibition of amyloid aggregation is important for developing potential therapeutic strategies of amyloid-related diseases. Herein, we report that the inhibition effect of a pristine peptide motif (KLVFF) can be significantly improved by introducing a terminal regulatory moiety (terpyridine). The molecular-level observations by using scanning tunneling microscopy reveal stoichiometry-dependent polymorphism of the coassembly structures, which originates from the terminal interactions of peptide with organic modulator moieties and can be attributed to the secondary structures of peptides and conformations of the organic molecules. Furthermore, the polymorphism of the peptide-organic coassemblies is shown to be correlated to distinctively different inhibition effects on amyloid-β 42 (Aβ42) aggregations and cytotoxicity.",

keywords = "ALZHEIMERS-DISEASE, BETA, BINDING, CONSTRAINTS, DYNAMICS, FIBRIL FORMATION, PROTEIN, SEQUENCE, SPECTROSCOPY, TOXICITY, amyloid beta (A beta) peptide, amyloid cytotoxicity, inhibitory effect, peptide aggregation, peptide motif, polymorphism effect, scanning tunneling microscopy",

author = "Lin Niu and Lei Liu and Wenhui Xi and Qiusen Han and Qiang Li and Yue Yu and Qunxing Huang and Fuyang Qu and Meng Xu and Yibao Li and Huiwen Du and Rong Yang and Jacob Cramer and Gothelf, \{Kurt V.\} and Mingdong Dong and Flemming Besenbacher and Qingdao Zeng and Chen Wang and Guanghong Wei and Yanlian Yang",

year = "2016",

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doi = "10.1021/acsnano.5b07396",

language = "English",

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pages = "4143--4153",

journal = "A C S Nano",

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T1 - Synergistic Inhibitory Effect of Peptide-Organic Coassemblies on Amyloid Aggregation

AU - Niu, Lin

AU - Liu, Lei

AU - Xi, Wenhui

AU - Han, Qiusen

AU - Li, Qiang

AU - Yu, Yue

AU - Huang, Qunxing

AU - Qu, Fuyang

AU - Xu, Meng

AU - Li, Yibao

AU - Du, Huiwen

AU - Yang, Rong

AU - Cramer, Jacob

AU - Gothelf, Kurt V.

AU - Dong, Mingdong

AU - Besenbacher, Flemming

AU - Zeng, Qingdao

AU - Wang, Chen

AU - Wei, Guanghong

AU - Yang, Yanlian

PY - 2016/4/26

Y1 - 2016/4/26

N2 - Inhibition of amyloid aggregation is important for developing potential therapeutic strategies of amyloid-related diseases. Herein, we report that the inhibition effect of a pristine peptide motif (KLVFF) can be significantly improved by introducing a terminal regulatory moiety (terpyridine). The molecular-level observations by using scanning tunneling microscopy reveal stoichiometry-dependent polymorphism of the coassembly structures, which originates from the terminal interactions of peptide with organic modulator moieties and can be attributed to the secondary structures of peptides and conformations of the organic molecules. Furthermore, the polymorphism of the peptide-organic coassemblies is shown to be correlated to distinctively different inhibition effects on amyloid-β 42 (Aβ42) aggregations and cytotoxicity.

AB - Inhibition of amyloid aggregation is important for developing potential therapeutic strategies of amyloid-related diseases. Herein, we report that the inhibition effect of a pristine peptide motif (KLVFF) can be significantly improved by introducing a terminal regulatory moiety (terpyridine). The molecular-level observations by using scanning tunneling microscopy reveal stoichiometry-dependent polymorphism of the coassembly structures, which originates from the terminal interactions of peptide with organic modulator moieties and can be attributed to the secondary structures of peptides and conformations of the organic molecules. Furthermore, the polymorphism of the peptide-organic coassemblies is shown to be correlated to distinctively different inhibition effects on amyloid-β 42 (Aβ42) aggregations and cytotoxicity.

KW - ALZHEIMERS-DISEASE

KW - BETA

KW - BINDING

KW - CONSTRAINTS

KW - DYNAMICS

KW - FIBRIL FORMATION

KW - PROTEIN

KW - SEQUENCE

KW - SPECTROSCOPY

KW - TOXICITY

KW - amyloid beta (A beta) peptide

KW - amyloid cytotoxicity

KW - inhibitory effect

KW - peptide aggregation

KW - peptide motif

KW - polymorphism effect

KW - scanning tunneling microscopy

UR - https://www.scopus.com/pages/publications/84968765250

U2 - 10.1021/acsnano.5b07396

DO - 10.1021/acsnano.5b07396

M3 - Journal article

C2 - 26982522

SN - 1936-0851

VL - 10

SP - 4143

EP - 4153

JO - A C S Nano

JF - A C S Nano

IS - 4

ER -

Synergistic Inhibitory Effect of Peptide-Organic Coassemblies on Amyloid Aggregation

Abstract

Keywords

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