Towards integrative structural mass spectrometry: Benefits from hybrid approaches

Methods ◽  
2015 ◽  
Vol 89 ◽  
pp. 4-12 ◽  
Author(s):  
Julien Marcoux ◽  
Sarah Cianférani
Keyword(s):  
Mass Spectrometry ◽  
Hybrid Approaches ◽  
Structural Mass Spectrometry ◽  
Structural Mass

Structural mass spectrometry comes of age: new insight into protein structure, function and interactions

2019 ◽  
Vol 47 (1) ◽  
pp. 317-327 ◽  
Author(s):  
Timothy M. Allison ◽  
Cherine Bechara
Keyword(s):  
Mass Spectrometry ◽  
Membrane Protein ◽  
Structure Function ◽  
Coming Of Age ◽  
Top Down ◽  
Single Experiment ◽  
Hybrid Approaches ◽  
Native Ms ◽  
Structural Mass Spectrometry ◽  
Structural Mass

Abstract Mass spectrometry (MS) provides an impressive array of information about the structure, function and interactions of proteins. In recent years, many new developments have been in the field of native MS and these exemplify a new coming of age of this field. In this mini review, we connect the latest methodological and instrumental developments in native MS to the new insights these have enabled. We highlight the prominence of an increasingly common strategy of using hybrid approaches, where multiple MS-based techniques are used in combination, and integrative approaches, where MS is used alongside other techniques such as ion-mobility spectrometry. We also review how the emergence of a native top-down approach, which combines native MS with top-down proteomics into a single experiment, is the pièce de résistance of structural mass spectrometry's coming of age. Finally, we outline key developments that have enabled membrane protein native MS to shift from being extremely challenging to routine, and how this technique is uncovering inaccessible details of membrane protein–lipid interactions.

The interaction between the natural metalloendopeptidase inhibitor BJ46a and its target toxin jararhagin analyzed by structural mass spectrometry and molecular modeling

2020 ◽  
Vol 221 ◽  
pp. 103761
Author(s):  
Viviane A. Bastos ◽  
Francisco Gomes-Neto ◽  
Surza Lucia G. Rocha ◽  
André Teixeira-Ferreira ◽  
Jonas Perales ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Modeling ◽  
Structural Mass Spectrometry ◽  
Structural Mass

The growing role of structural mass spectrometry in the discovery and development of therapeutic antibodies

The Analyst ◽  
2018 ◽  
Vol 143 (11) ◽  
pp. 2459-2468 ◽  
Author(s):  
Yuwei Tian ◽  
Brandon T. Ruotolo
Keyword(s):  
Mass Spectrometry ◽  
State Of The Art ◽  
Therapeutic Antibodies ◽  
Critical Importance ◽  
Current State ◽  
Measurement Science ◽  
Structural Mass Spectrometry ◽  
Structural Mass

The comprehensive structural characterization of therapeutic antibodies is of critical importance for the successful discovery and development of such biopharmaceuticals, yet poses many challenges to modern measurement science. Here, we review the current state-of-the-art mass spectrometry technologies focusing on the characterization of antibody-based therapeutics.

scholarly journals Structural mass spectrometry of tissue extracts to distinguish cancerous and non-cancerous breast diseases

2014 ◽  
Vol 10 (11) ◽  
pp. 2827-2837 ◽  
Author(s):  
Kelly M. Hines ◽  
Billy R. Ballard ◽  
Dana R. Marshall ◽  
John A. McLean
Keyword(s):  
Mass Spectrometry ◽  
Breast Tissue ◽  
Breast Diseases ◽  
Molecular Signatures ◽  
Human Breast ◽  
Human Breast Tissue ◽  
Tissue Extracts ◽  
Ms Analysis ◽  
Structural Mass Spectrometry ◽  
Structural Mass

UPLC-IM-MS/MS analysis of human breast tissue extracts distinguished cancerous and non-cancerous breast diseases by characteristic molecular signatures.

scholarly journals Structural Mass Spectrometry: Rapid Methods for Separation and Analysis of Peptide Natural Products

2012 ◽  
Vol 75 (1) ◽  
pp. 48-53 ◽  
Author(s):  
Cody R. Goodwin ◽  
Larissa S. Fenn ◽  
Dagmara K. Derewacz ◽  
Brian O. Bachmann ◽  
John A. McLean
Keyword(s):  
Mass Spectrometry ◽  
Natural Products ◽  
Rapid Methods ◽  
Structural Mass Spectrometry ◽  
Structural Mass

scholarly journals Streptococcus pyogenes forms serotype and local environment-dependent inter-species protein complexes

2021 ◽  
Author(s):  
Sounak Chowdhury ◽  
Hamed Khakzad ◽  
Gizem Ertürk Bergdahl ◽  
Rolf Lood ◽  
Simon Ekstrom ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Streptococcus Pyogenes ◽  
Protein Complexes ◽  
Specific Interaction ◽  
Plasma Concentrations ◽  
Mass Spectrometry Analysis ◽  
Secretory Iga ◽  
Structural Mass Spectrometry ◽  
Systemic Infections ◽  
Structural Mass

AbstractStreptococcus pyogenes is known to cause both mucosal and systemic infections in humans. In this study, we used a combination of quantitative and structural mass spectrometry techniques to determine the composition and structure of the interaction network formed between human plasma proteins and the surface of different S. pyogenes serotypes. Quantitative network analysis revealed that S. pyogenes form serotype-specific interaction networks that are highly dependent on the domain arrangement of the surface-attached M protein. Subsequent structural mass spectrometry analysis and computational modelling on one of the M proteins, M28 revealed that the network structure changes across different host microenvironments. We report that M28 binds secretory IgA via two separate binding sites with high affinity in saliva. During vascular leakage mimicked by increasing plasma concentrations in saliva, the binding of secretory IgA was replaced by binding of monomeric IgA and C4BP. This indicates that an upsurge of C4BP in the local microenvironment due to damage of the mucosal membrane drives binding of C4BP and monomeric IgA to M28. The results suggest that S. pyogenes has evolved to form microenvironment-dependent host-pathogen protein complexes to combat the human immune surveillance during both mucosal and systemic infections.

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