Journal
ACS NANO
Volume 8, Issue 9, Pages 9503-9510Publisher
AMER CHEMICAL SOC
DOI: 10.1021/nn503737r
Keywords
amyloid peptide; molecular tethering effect; peptide aggregation; modulation; membrane disruption
Categories
Funding
- National Natural Science Foundation of China [91127043, 21261130090]
- National Basic Research Program of China [2011CB932800]
- Villum Fonden [00007194] Funding Source: researchfish
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Amyloid peptides are considered to be the main contributor for the membrane disruption related to the pathogenesis of degenerative diseases. The variation of amino acids at the carboxylic terminus of amyloid peptide has revealed significant effects on the modulation of abnormal assemblies of amyloid peptides. In this work, molecular binding agents were tethered to the C-terminus of beta-amyloid peptide 1-42 (A beta 42). The molecular interaction between A beta 42 and molecule tethers was identified at single molecule level by using scanning tunneling microscopy (STM). The mechanistic insight into the feature variation of the self-assembly of A beta 42 peptide caused by molecular tethering at C-terminus was clearly revealed, which could appreciably affect the nucleation of amyloid peptide, thus reducing the membrane disruptions.
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