(1) Background: Small Animal Fast Insert for MRI detector I (SAFIR-I) is a preclinical Positron Emission Tomography (PET) insert for the Bruker BioSpec 70/30 Ultra Shield Refrigerated (USR) preclinical 7T Magnetic Resonance Imaging (MRI) system. It is designed explicitly for high-rate kinetic studies in mice and rats with injected activities reaching 500MBq, enabling truly simultaneous quantitative PET and Magnetic Resonance (MR) imaging with time frames of a few seconds in length. (2) Methods: SAFIR-I has an axial field of view of 54.2mm and an inner diameter of 114mm. It employs Lutetium Yttrium OxyorthoSilicate (LYSO) crystals and Multi Pixel Photon Counter (MPPC) arrays. The Position-Energy-Timing Application Specific Integrated Circuit, version 6, Single Ended (PETA6SE) digitizes the MPPC signals and provides time stamps and energy information. (3) Results: SAFIR-I is MR-compatible. The system's Coincidence Resolving Time (CRT) and energy resolution are between separate-uncertainty 209.0(3)ps and separate-uncertainty 12.41(02) Full Width at Half Maximum (FWHM) at low activity and separate-uncertainty 326.89(12)ps and separate-uncertainty 20.630(011) FWHM at 550MBq, respectively. The peak sensitivity is ∼1.6. The excellent performance facilitated the successful execution of first in vivo rat studies beyond 300MBq. Based on features visible in the acquired images, we estimate the spatial resolution to be ∼2mm in the center of the Field Of View (FOV). (4) Conclusion: The SAFIR-I PET insert provides excellent performance, permitting simultaneous in vivo small animal PET/MR image acquisitions with time frames of a few seconds in length at activities of up to 500MBq.
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http://dx.doi.org/10.3390/s21217037 | DOI Listing |
Vet Res Forum
December 2024
Institute of Pathogenic Microbiology, College of Biological Science and Engineering, and Nanchang Key Laboratory of Animal Virus and Genetic Engineering, Jiangxi Agricultural University, Nanchang, China.
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the COVID-19 pandemic. The receptor binding domain (RBD), located at the spike protein of SARS-CoV-2, contains most of the neutralizing epitopes during viral infection and is an ideal antigen for vaccine development. In this study, bioinformatic analysis of the amino acid sequence data of SARS-CoV-2 RBD protein for the better understanding of molecular characteristics was performed.
View Article and Find Full Text PDFPhys Med Biol
January 2025
National Institute of Radiological Sciences, 4-9-1 Anagawa, Inage-ku, Chiba, 263-8555, JAPAN.
Med Phys
December 2024
Department of Physics, Lakehead University, Thunder Bay, Ontario, Canada.
Background: This study investigates a multi-angle acquisition method aimed at improving image quality in organ-targeted PET detectors with planar detector heads. Organ-targeted PET technologies have emerged to address limitations of conventional whole-body PET/CT systems, such as restricted axial field-of-view (AFOV), limited spatial resolution, and high radiation exposure associated with PET procedures. The AFOV in organ-targeted PET can be adjusted to the organ of interest, minimizing unwanted signals from other parts of the body, thus improving signal collection efficiency and reducing the dose of administered radiotracer.
View Article and Find Full Text PDFSheng Wu Gong Cheng Xue Bao
December 2024
State Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine, Lanzhou University, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730000, Gansu, China.
This study developed ferritin-based nanoparticles carrying the African swine fever virus (ASFV) p30 protein and evaluated their immunogenicity, aiming to provide an experimental basis for the research on nanoparticle vaccines against ASFV. Initially, the gene sequences encoding the p30 protein and SpyTag were fused and inserted into the pCold-I vector to create the pCold-p30 plasmid. The gene sequences encoding SpyCatcher and ferritin were fused and then inserted into the pET-28a(+) vector to produce the pET-F-np plasmid.
View Article and Find Full Text PDFZhonghua Yu Fang Yi Xue Za Zhi
December 2024
Clinical Research Center, The Affiliated Wuxi People's Hospital of Nanjing Medical University, Wuxi214023, China.
The present study was aimed to produce the recombinant protein of allergen component 32 (Tyr p 32) and to identify its immunoreactivity. The cDNA encoding Tyr p 32 was amplified from total RNA of and inserted into pET-28a (+) vector. The constructed plasmid pET-28a (+)-Tyr p 32 was transformed into BL21 (DE3) receptor cells.
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