Szu-Hsueh Lai's research while affiliated with National Cheng Kung University and other places
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Publications (8)
Due to their unique size-dependent properties, nanoparticles (NPs) have many industrial and biomedical applications. Although NPs are generally characterized based on the size or morphological analysis, the mass of whole particles can be of interest as it represents the total amount of material in the particle regardless of shape, density, or eleme...
Qualitative and quantitative mass analysis of antibodies and related macromolecular immune complexes is a prerequisite for determining their identity, binding partners, stoichiometries, and affinities. A plethora of bioanalytical technologies exist to determine such characteristics, typically based on size, interaction with functionalized surfaces,...
Native top-down mass spectrometry (MS) is gaining traction for the analysis and sequencing of intact proteins and protein assemblies, giving access to their mass and composition, as well as sequence information useful for identification. Herein, we extend and apply native top-down MS, using electron capture dissociation, to two submillion Da IgM- a...
Determining how antibodies interact with the spike (S) protein of the SARS-CoV-2 virus is critical for combating COVID-19. Structural studies typically employ simplified, truncated constructs that may not fully recapitulate the behavior of the original complexes. Here, we combine two single particle mass analysis techniques (mass photometry and cha...
Standard methods for mass analysis measure ensembles of thousand to millions of molecules. While this approach enables analysis of monodisperse recombinant proteins, some heterogeneous protein assemblies pose a significant challenge, whereby co-occurring stoichiometries, sub-complexes, and modifications hamper analysis using native mass spectrometr...
Due to their physical properties, nanomechanical sensors (NEMS) can achieve mass measurements in the mega- to gigadalton range, which is hardly obtained with conventional mass-spectrometers. However, NEMS signals are subject to noise, causing a loss of mass resolution and thus emphasizing the need of noise control. We propose a denoising model that...
When studying viruses, the most prevalent aspects that come to mind are their structural and functional features, but this leaves in the shadows a quite universal characteristic: their mass. Even if approximations can be derived from size and density measurements, the multi MDa to GDa mass range, featuring a majority of viruses, has so far remained...
Determining how antibodies interact with the spike (S) protein of the SARS-CoV-2 virus is critical for combating COVID-19. Structural studies typically employ simplified, truncated constructs that may not fully recapitulate the behaviour of the original complexes. Here, we combine two single particle mass analysis techniques (mass photometry and ch...
Citations
... Analyzing the kinetics and affinities of protein interactions is crucial in the biomedical field because the related parameters and information can unravel their roles in cellular function thus increasing insights into biological functions and structural/functional relationships of protein [1][2][3][4][5]. Among the research on binding proteins, the interactions between antibodies and natural binding ligands are important in the development of pharmaceutical science, biomedical engineering, and affinity chromatography [6,7]. ...
... The ability to observe and quantify intact immune complexes formed by IgE antibodies provides an important dimension in their characterization, which is complementary to the local structural information that can be obtained by fragmenting highly heterogeneous antibodies in solution 47,48 or in the gas phase. 49,50 Until recently, electron microscopy remained the only means of direct detection and stoichiometry analysis for intact complexes containing IgE molecules, 51 but the data interpretation (based on the negative stain image analysis) was not straightforward. ...
... In addition, factors such as avidity and (anti-) cooperativity are known to also influence binding between full-length IgG1 and the S-protein 22,23 . In any case, these binding differences between antibody clones are an important feature to consider when selecting antibodies for further development into biotherapeutics. ...
... Total IgA was captured from serum or milk from Donor 1 at collection 1 (C1), and subjected to mass analysis by mass photometry (MP) to assess the oligomeric state. MP is a label-free light scattering-based mass analysis technique, which allows for the determination of the mass of individual particles [34][35][36]. The resulting mass distribution Supplementary Table S1 for further details). ...