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  1. Article ; Online: Mass photometry reveals SARS-CoV-2 spike stabilisation to impede ACE2 binding through altered conformational dynamics.

    Burnap, Sean A / Struwe, Weston B

    Chemical communications (Cambridge, England)

    2022  Volume 58, Issue 93, Page(s) 12939–12942

    Abstract: Here we show using mass photometry how proline substitutions, commonly used for SARS-CoV-2 spike stabilisation in vaccine design, directly affects ACE2 receptor ... ...

    Abstract Here we show using mass photometry how proline substitutions, commonly used for SARS-CoV-2 spike stabilisation in vaccine design, directly affects ACE2 receptor interactions
    MeSH term(s) Humans ; SARS-CoV-2 ; Angiotensin-Converting Enzyme 2 ; Spike Glycoprotein, Coronavirus/chemistry ; Peptidyl-Dipeptidase A/metabolism ; COVID-19 ; Receptors, Virus/chemistry ; Receptors, Virus/metabolism ; Protein Binding ; Photometry ; Molecular Dynamics Simulation ; Binding Sites
    Chemical Substances Angiotensin-Converting Enzyme 2 (EC 3.4.17.23) ; Spike Glycoprotein, Coronavirus ; Peptidyl-Dipeptidase A (EC 3.4.15.1) ; Receptors, Virus ; spike protein, SARS-CoV-2
    Language English
    Publishing date 2022-11-22
    Publishing country England
    Document type Journal Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d2cc04711j
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  2. Article ; Online: Analysis of Protein Complex Formation at Micromolar Concentrations by Coupling Microfluidics with Mass Photometry.

    Claasen, Myndert / Kofinova, Zornitsa / Contino, Matteo / Struwe, Weston B

    Journal of visualized experiments : JoVE

    2024  , Issue 203

    Abstract: Mass photometry is a versatile mass measurement technology that enables the study of biomolecular interactions and complex formation in solution without labels. Mass photometry is generally suited to analyzing samples in the 100 pM-100 nM concentration ... ...

    Abstract Mass photometry is a versatile mass measurement technology that enables the study of biomolecular interactions and complex formation in solution without labels. Mass photometry is generally suited to analyzing samples in the 100 pM-100 nM concentration range. However, in many biological systems, it is necessary to measure more concentrated samples to study low-affinity or transient interactions. Here, we demonstrate a method that effectively expands the range of sample concentrations that can be analyzed by mass photometry from nanomolar to tens of micromolar. In this protocol, mass photometry is combined with a novel microfluidics system to investigate the formation of protein complexes in solution in the micromolar concentration range. With the microfluidics system, users can maintain a sample at a desired higher concentration followed by dilution to the nanomolar range - several milliseconds prior to the mass photometry measurement. Due to the speed of the dilution, data is obtained before the equilibrium of the sample has shifted (i.e., dissociation of the complex). The technique is applied to measure interactions between an immunoglobulin G (IgG) antibody and the neonatal Fc receptor, showing the formation of high-order complexes that were not quantifiable with static mass photometry measurements. In conclusion, the combination of mass photometry and microfluidics makes it possible to characterize samples in the micromolar concentration range and is proficient in measuring biomolecular interactions with weaker affinities. These capabilities can be applied in a range of contexts - including the development and design of biotherapeutics - enabling thorough characterization of diverse protein-protein interactions.
    MeSH term(s) Humans ; Infant, Newborn ; Microfluidics ; Immunoglobulin G ; Photometry/methods
    Chemical Substances Immunoglobulin G
    Language English
    Publishing date 2024-01-26
    Publishing country United States
    Document type Journal Article ; Video-Audio Media
    ZDB-ID 2259946-0
    ISSN 1940-087X ; 1940-087X
    ISSN (online) 1940-087X
    ISSN 1940-087X
    DOI 10.3791/65772
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  3. Article ; Online: Measuring Protein-Protein Interactions and Quantifying Their Dissociation Constants with Mass Photometry.

    Kofinova, Zornitsa / Karunanithy, Gogulan / Ferreira, Ana Sofia / Struwe, Weston B

    Current protocols

    2023  Volume 4, Issue 1, Page(s) e962

    Abstract: Protein-protein interactions underlie most biological processes, and determining the affinity and abundance of binding partners for each interaction is often a challenging task because these interactions often involve multiple ligands and binding sites. ... ...

    Abstract Protein-protein interactions underlie most biological processes, and determining the affinity and abundance of binding partners for each interaction is often a challenging task because these interactions often involve multiple ligands and binding sites. Standard methods for determining the affinity of protein interactions often require a large amount of starting material in addition to potentially disruptive labeling or immobilization of the binding partners. Mass photometry is a bioanalytical technique that measures the mass of single biomolecules in solution, quickly and with minimal sample requirements. This article describes how mass photometry can be used to determine the mass distribution of binding partners, the complexes they form, the relative abundance of each species, and, accordingly, the dissociation constant (K
    MeSH term(s) Protein Binding ; Binding Sites ; Photometry
    Language English
    Publishing date 2023-12-29
    Publishing country United States
    Document type Journal Article
    ISSN 2691-1299
    ISSN (online) 2691-1299
    DOI 10.1002/cpz1.962
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  4. Article ; Online: Label-free methods for optical

    Soltermann, Fabian / Struwe, Weston B / Kukura, Philipp

    Physical chemistry chemical physics : PCCP

    2021  Volume 23, Issue 31, Page(s) 16488–16500

    Abstract: Protein-protein interactions are involved in the regulation and function of the majority of cellular processes. As a result, much effort has been aimed at the development of methodologies capable of quantifying protein-protein interactions, with label- ... ...

    Abstract Protein-protein interactions are involved in the regulation and function of the majority of cellular processes. As a result, much effort has been aimed at the development of methodologies capable of quantifying protein-protein interactions, with label-free methods being of particular interest due to the associated simplified workflows and minimisation of label-induced perturbations. Here, we review recent advances in optical technologies providing label-free in vitro measurements of affinities and kinetics. We provide an overview and comparison of existing techniques and their principles, discussing advantages, limitations, and recent applications.
    MeSH term(s) Kinetics ; Optical Phenomena ; Protein Binding ; Proteins/chemistry ; Proteins/metabolism
    Chemical Substances Proteins
    Language English
    Publishing date 2021-07-29
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1476244-4
    ISSN 1463-9084 ; 1463-9076
    ISSN (online) 1463-9084
    ISSN 1463-9076
    DOI 10.1039/d1cp01072g
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  5. Article ; Online: Engineer RNA-Protein Nanowires as Light-Responsive Biomaterials.

    Younas, Tayyaba / Liu, Chang / Struwe, Weston B / Kukura, Philipp / He, Lizhong

    Small (Weinheim an der Bergstrasse, Germany)

    2023  Volume 19, Issue 12, Page(s) e2206513

    Abstract: RNA molecules have emerged as increasingly attractive biomaterials with important applications such as RNA interference (RNAi) for cancer treatment and mRNA vaccines against infectious diseases. However, it remains challenging to engineer RNA ... ...

    Abstract RNA molecules have emerged as increasingly attractive biomaterials with important applications such as RNA interference (RNAi) for cancer treatment and mRNA vaccines against infectious diseases. However, it remains challenging to engineer RNA biomaterials with sophisticated functions such as non-covalent light-switching ability. Herein, light-responsive RNA-protein nanowires are engineered to have such functions. It first demonstrates that the high affinity of RNA aptamer enables the formation of long RNA-protein nanowires through designing a dimeric RNA aptamer and an engineered green fluorescence protein (GFP) that contains two TAT-derived peptides at N- and C- termini. GFP is then replaced with an optogenetic protein pair system, LOV2 (light-oxygen-voltage) protein and its binding partner ZDK (Z subunit of protein A), to confer blue light-controlled photo-switching ability. The light-responsive nanowires are long (>500 nm) in the dark, but small (20-30 nm) when exposed to light. Importantly, the co-assembly of this RNA-protein hybrid biomaterial does not rely on the photochemistry commonly used for light-responsive biomaterials, such as bond formation, cleavage, and isomerization, and is thus reversible. These RNA-protein structures can serve as a new class of light-controlled biocompatible frameworks for incorporating versatile elements such as RNA, DNA, and enzymes.
    MeSH term(s) RNA/chemistry ; Aptamers, Nucleotide/chemistry ; Nanowires ; RNA Interference ; Peptides ; Green Fluorescent Proteins
    Chemical Substances RNA (63231-63-0) ; Aptamers, Nucleotide ; Peptides ; Green Fluorescent Proteins (147336-22-9)
    Language English
    Publishing date 2023-01-15
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2168935-0
    ISSN 1613-6829 ; 1613-6810
    ISSN (online) 1613-6829
    ISSN 1613-6810
    DOI 10.1002/smll.202206513
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  6. Article ; Online: Relating glycoprotein structural heterogeneity to function - insights from native mass spectrometry.

    Struwe, Weston B / Robinson, Carol V

    Current opinion in structural biology

    2019  Volume 58, Page(s) 241–248

    Abstract: Glycosylation is the most complex and prevalent protein modification that influences attributes ranging from cellular localization and signaling to half-life and proteolysis. Glycoconjugates are fundamental for cellular function and alterations in their ... ...

    Abstract Glycosylation is the most complex and prevalent protein modification that influences attributes ranging from cellular localization and signaling to half-life and proteolysis. Glycoconjugates are fundamental for cellular function and alterations in their structure are often observed in pathological states. Most biotherapeutic proteins are glycosylated, which influences drug safety and efficacy. Therefore, the ability to characterize glycoproteins is important in all areas of biomolecular and medicinal research. Here we discuss recent advances in native mass spectrometry that have significantly improved our ability to characterize heterogeneous glycoproteins and to relate glycan structure to protein function.
    MeSH term(s) Glycoproteins/chemistry ; Glycoproteins/metabolism ; Mass Spectrometry/methods ; Polysaccharides/metabolism
    Chemical Substances Glycoproteins ; Polysaccharides
    Language English
    Publishing date 2019-07-18
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1068353-7
    ISSN 1879-033X ; 0959-440X
    ISSN (online) 1879-033X
    ISSN 0959-440X
    DOI 10.1016/j.sbi.2019.05.019
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  7. Article ; Online: Ion Mobility-Mass Spectrometry of Glycoconjugates.

    Struwe, Weston B / Harvey, David J

    Methods in molecular biology (Clifton, N.J.)

    2019  Volume 2084, Page(s) 203–219

    Abstract: Glycoconjugates are diverse biomolecules that are dynamically assembled to regulate and fine-tune numerous cellular processes. Their biosynthesis is nontemplate-driven, achieved stepwise in discrete locations within the cell, giving rise to a range of ... ...

    Abstract Glycoconjugates are diverse biomolecules that are dynamically assembled to regulate and fine-tune numerous cellular processes. Their biosynthesis is nontemplate-driven, achieved stepwise in discrete locations within the cell, giving rise to a range of complex branched structures that pose a significant challenge in structural biology. Mass spectrometry is the leading method for analysis of glycoconjugates, and the addition of ion mobility has proven valuable for improving structural assignments of individual glycans in complex biological mixtures. In this chapter, we briefly discuss recent applications of IM for glycomics and describe how to acquire, interpret, and analyze IM-MS data for the analysis of glycans.
    MeSH term(s) Glycoconjugates/chemistry ; Glycomics/methods ; Ion Mobility Spectrometry ; Mass Spectrometry ; Polysaccharides/chemistry ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
    Chemical Substances Glycoconjugates ; Polysaccharides
    Language English
    Publishing date 2019-11-11
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-0030-6_13
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  8. Article ; Online: Epilogue—Unravelling Glycan Complexity

    Weston B. Struwe

    Perspectives in Science, Vol 11, Iss C, Pp 70-

    2017  Volume 71

    Keywords Science ; Q ; Science (General) ; Q1-390
    Language German
    Publishing date 2017-01-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
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  9. Article ; Online: Native Mass Spectrometry Meets Glycomics: Resolving Structural Detail and Occupancy of Glycans on Intact Glycoproteins.

    Chen, Siyun / Wu, Di / Robinson, Carol V / Struwe, Weston B

    Analytical chemistry

    2021  Volume 93, Issue 30, Page(s) 10435–10443

    Abstract: Glycoproteins are inherently heterogeneous and therefore resolving structures in their entirety remains a major challenge in structural biology. Native mass spectrometry has transformed our ability to study glycoproteins, and despite advances in high- ... ...

    Abstract Glycoproteins are inherently heterogeneous and therefore resolving structures in their entirety remains a major challenge in structural biology. Native mass spectrometry has transformed our ability to study glycoproteins, and despite advances in high-resolution instrumentation, there are comparatively a few studies demonstrating its potential with data largely limited to an overall measure of monosaccharide composition for all glycans across glycosylation sites for a given protein. Clearly, these readouts lack glycan topology information, namely, monosaccharide linkage and glycan branching. To address this deficiency, we developed a new approach that joins native mass spectrometry with glycan exoglycosidase sequencing, the combination of which provides remarkable glycoprotein structural details. We show how
    MeSH term(s) Glycomics ; Glycoproteins/metabolism ; Glycosylation ; Mass Spectrometry ; Polysaccharides
    Chemical Substances Glycoproteins ; Polysaccharides
    Language English
    Publishing date 2021-07-19
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/acs.analchem.1c01460
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  10. Article ; Online: Structural Studies of Fucosylated N-Glycans by Ion Mobility Mass Spectrometry and Collision-Induced Fragmentation of Negative Ions.

    Harvey, David J / Struwe, Weston B

    Journal of the American Society for Mass Spectrometry

    2018  Volume 29, Issue 6, Page(s) 1179–1193

    Abstract: There is considerable potential for the use of ion mobility mass spectrometry in structural glycobiology due in large part to the gas-phase separation attributes not typically observed by orthogonal methods. Here, we evaluate the capability of traveling ... ...

    Abstract There is considerable potential for the use of ion mobility mass spectrometry in structural glycobiology due in large part to the gas-phase separation attributes not typically observed by orthogonal methods. Here, we evaluate the capability of traveling wave ion mobility combined with negative ion collision-induced dissociation to provide structural information on N-linked glycans containing multiple fucose residues forming the Lewis
    MeSH term(s) Anions/chemistry ; Carbohydrate Sequence ; Epitopes/chemistry ; Fucose/analysis ; Humans ; Ion Mobility Spectrometry/methods ; Lewis Blood Group Antigens/chemistry ; Lewis X Antigen/chemistry ; Parotid Gland/chemistry ; Polysaccharides/chemistry
    Chemical Substances Anions ; Epitopes ; Lewis Blood Group Antigens ; Lewis X Antigen ; Lewis Y antigen ; Polysaccharides ; Fucose (28RYY2IV3F)
    Language English
    Publishing date 2018-05-22
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1073671-2
    ISSN 1879-1123 ; 1044-0305
    ISSN (online) 1879-1123
    ISSN 1044-0305
    DOI 10.1007/s13361-018-1950-x
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