Hydrogen peroxide-responsive platelet membrane-coated nanoparticles for thrombus therapy

2021 ◽  
Author(s):  
Yi Zhao ◽  
Ruosen Xie ◽  
Nisakorn Yodsanit ◽  
Mingzhou Ye ◽  
Yuyuan Wang ◽  
...  

A schematic diagram of the PNPArg as a thrombus-targeting antithrombotic agent.

2020 ◽  
Vol 41 (Supplement_2) ◽  
Author(s):  
H Yang ◽  
Y Song ◽  
Z Huang ◽  
J Qian ◽  
Z Pang ◽  
...  

Abstract Background Aortic valve disease is the most common valvular heart disease leading to valve replacement. The efficacy of pharmacological therapy for aortic valve disease is limited by the high mechanical stress at the aortic valves impairing the binding rate. We aimed to identify nanoparticle coating with entire platelet membranes to fully mimic their inherent multiple adhesion mechanisms and target the sclerotic aortic valve of apolipoprotein E-deficient (ApoE−/−) mice based on their multiple sites binding capacity under high shear stress. Methods Considering the potent interaction of platelet membrane glycoproteins with components present in sclerotic aortic valves, platelet membrane-coated nanoparticles (PNPs) were synthetized and the binding capacity under high shear stress was evaluated in vitro and in vivo. Results Compared with PNPs bound intensity in the static station, 161%, 59%, and 39% of attached PNPs remained adherent on VWF-, collagen-, and fibrin-coated surfaces under shear stress of 25dyn/cm2 respectively. PNPs demonstrated effectively adhering to von Willebrand factor, collagen and fibrin under shear stresses in vitro. In an aortic valve disease model established in ApoE−/− mice, PNPs group exhibited significant increase of accumulation in the aortic valves compared with PBS and control NP group. PNPs displayed high degrees of proximity or co-localization with vWF, collagen and fibrin, which exhibited good targeting to sclerotic aortic valves by mimicking platelet multiple adhesive mechanisms. Conclusion PNPs could provide a promising platform for the molecular diagnosis and targeting treatment of aortic valve disease. Targeting combination Funding Acknowledgement Type of funding source: Foundation. Main funding source(s): National Natural Science Foundation of China


2020 ◽  
Vol 1 (1) ◽  
pp. 2000018
Author(s):  
Shuyan Wang ◽  
Yaou Duan ◽  
Qiangzhe Zhang ◽  
Anvita Komarla ◽  
Hua Gong ◽  
...  

Engineering ◽  
2020 ◽  
Author(s):  
Jwa-Kyung Kim ◽  
Satoshi Uchiyama ◽  
Hua Gong ◽  
Alexandra Stream ◽  
Liangfang Zhang ◽  
...  

2020 ◽  
Vol 8 (21) ◽  
pp. 4648-4659 ◽  
Author(s):  
Long Wu ◽  
Wei Xie ◽  
Hui-Ming Zan ◽  
Zhongzhong Liu ◽  
Ganggang Wang ◽  
...  

Specific targeted drug delivery and controllable release of drugs at tumor regions are two of the main challenges for hepatocellular carcinoma (HCC) therapy, particularly post metastasis.


Nano Letters ◽  
2021 ◽  
Vol 21 (6) ◽  
pp. 2588-2595
Author(s):  
Bozhao Li ◽  
Tianjiao Chu ◽  
Jingyan Wei ◽  
Yinlong Zhang ◽  
Feilong Qi ◽  
...  

Nano Research ◽  
2018 ◽  
Vol 11 (11) ◽  
pp. 6086-6101 ◽  
Author(s):  
Yuwei He ◽  
Ruixiang Li ◽  
Jianming Liang ◽  
Ying Zhu ◽  
Shuya Zhang ◽  
...  

2020 ◽  
Vol Volume 15 ◽  
pp. 901-912 ◽  
Author(s):  
Hongbo Yang ◽  
Yanan Song ◽  
Jing Chen ◽  
Zhiqing Pang ◽  
Ning Zhang ◽  
...  

Author(s):  
D. C. Brindley ◽  
M. McGill

Morphological and cytochemical studies of platelets have reported a surface coat, or glycocalyx, external to the plasma membrane (1). Biochemical analyses have likewise confirmed the highly adsorptive properties of platelets as transporters of coagulation factors (2). However, visualization of the platelet membrane by conventional EM procedures does not reflect this special relationship between the platelet and its plasma environment. By the routine method of alcohol-propylene oxide dehydration for Epon embedding, the lipid bilayer nature of the platelet membrane appears similar to other blood cells (Fig. 1). A new rapid embedding technique using dimethoxypropane (DMP) as dehydrating agent (13) has permitted ultrastructural analyses of the surface features of the platelet-plasma interface.Aliquots of human or rabbit platelet-rich plasma (PRP) were added to equal volumes of 6% glutaraldehyde in Millonig's buffer at 37° for 45 minutes, rinsed in buffer and postfixed in 1% osmium in Millonig's buffer for 45 minutes.


Author(s):  
George E. Childs ◽  
Joseph H. Miller

Biochemical and differential centrifugation studies have demonstrated that the oxidative enzymes of Acanthamoeba sp. are localized in mitochondria and peroxisomes (microbodies). Although hartmanellid amoebae have been the subject of several electron microscopic studies, peroxisomes have not been described from these organisms or other protozoa. Cytochemical tests employing diaminobenzidine-tetra HCl (DAB) and hydrogen peroxide were used for the ultrastructural localization of peroxidases of trophozoites of Hartmanella sp. (A-l, Culbertson), a pathogenic strain grown in axenic cultures of trypticase soy broth.


2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.


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