1. Microglia-Mediated Neuroinflammation: A Potential Target for the Treatment of Cardiovascular Diseases
Hong Jiang, Yao Xu, Wei Pan, Menglong Wang, Jishou Zhang, Jun Wan J Inflamm Res . 2022 May 25;15:3083-3094. doi: 10.2147/JIR.S350109.
Microglia are tissue-resident macrophages of the central nervous system (CNS). In the CNS, microglia play an important role in the monitoring and intervention of synaptic and neuron-level activities. Interventions targeting microglia have been shown to improve the prognosis of various neurological diseases. Recently, studies have observed the activation of microglia in different cardiovascular diseases. In addition, different approaches that regulate the activity of microglia have been shown to modulate the incidence and progression of cardiovascular diseases. The change in autonomic nervous system activity after neuroinflammation may be a potential intermediate link between microglia and cardiovascular diseases. Here, in this review, we will discuss recent updates on the regulatory role of microglia in hypertension, myocardial infarction and ischemia/reperfusion injury. We propose that microglia serve as neuroimmune modulators and potential targets for cardiovascular diseases.
2. Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide
Xiaofeng Wang, Jingyuan Li, Lei Liu, Flemming Besenbacher, Mingdong Dong, Søren Vrønning Hoffmann, Qiang Li, Shuai Zhang, Zheng Liu Adv Sci (Weinh) . 2016 Apr 8;3(6):1500369. doi: 10.1002/advs.201500369.
The differentiation of protein properties and biological functions arises from the variation in the primary and secondary structure. Specifically, in abnormal assemblies of protein, such as amyloid peptide, the secondary structure is closely correlated with the stable ensemble and the cytotoxicity. In this work, the early Aβ33-42aggregates forming the molecular monolayer at hydrophobic interface are investigated. The molecular monolayer of amyloid peptide Aβ33-42consisting of novel parallel β-strand-like structure is further revealed by means of a quantitative nanomechanical spectroscopy technique with force controlled in pico-Newton range, combining with molecular dynamic simulation. The identified parallel β-strand-like structure of molecular monolayer is distinct from the antiparallel β-strand structure of Aβ33-42amyloid fibril. This finding enriches the molecular structures of amyloid peptide aggregation, which could be closely related to the pathogenesis of amyloid disease.
3. Size Effect of Graphene Oxide on Modulating Amyloid Peptide Assembly
Yunpeng Cao, Lei Liu, Mingdong Dong, Qiang Li, Jie Wang Chemistry . 2015 Jun 26;21(27):9632-7. doi: 10.1002/chem.201500577.
Protein misfolding and abnormal assembly could lead to aggregates such as oligomer, proto-fibril, mature fibril, and senior amyloid plaques, which are associated with the pathogenesis of many amyloid diseases. These irreversible amyloid aggregates typically form in vivo and researchers have been endeavoring to find new modulators to invert the aggregation propensity in vitro, which could increase understanding in the mechanism of the aggregation of amyloid protein and pave the way to potential clinical treatment. Graphene oxide (GO) was shown to be a good modulator, which could strongly control the amyloidosis of Aβ (33-42). In particular, quartz crystal microbalance (QCM), circular dichroism (CD) spectroscopy, and atomic force microscopy (AFM) measurements revealed the size-dependent manner of GO on modulating the assembly of amyloid peptides, which could be a possible way to regulate the self-assembled nanostructure of amyloid peptide in a predictable manner.
