Publications by Luca Fornelli | EPFL Graph Search

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Coupling of motion of the ion clouds with close m/z values is a well-established phenomenon for ion-trapping mass analyzers. In Fourier transform ion cyclotron resonance mass spectrometry it is known as ion coalescence. Recently, ion coalescence was demons ...

The rapid growth of approved biotherapeutics, e.g., monoclonal antibodies or immunoglobulins G (IgGs), demands improved techniques for their quality control. Traditionally, proteolysis-based bottom-up mass spectrometry (MS) has been employed. However, the ...

In this study, a recombinant monoclonal IgG antibody was produced by transient gene expression (TGE) in suspension-adapted HEK-293E cells. The objective of the study was to determine the variation in recombinant IgG yield and glycosylation in ten independe ...

Tissue transglutaminase (tTGase) catalyzes both deamidation and transamidation of peptides and proteins by using a peptidyl glutamine as primary substrate. A precise consensus sequence for the enzyme is unknown and the ratio between deamidated and transami ...

Fourier transform mass spectrometry (FTMS) enables comprehensive analysis of complex molecular mixtures. Given the broad intensity ranges of components in the mass spectra, it is imperative to accurately determine a noise threshold level above which peak a ...

Improving qualitative and quantitative characterization of monoclonal antibodies is essential, because of their increasing popularity as therapeutic drug targets. Electron transfer dissociation (ETD)-based top-down mass spectrometry (MS) is the method of c ...

The increasing importance of immunoglobulins G (IgGs) as biotherapeutics calls for improved structural characterization methods designed for these large (similar to 150 kDa) macromolecules. Analysis workflows have to be rapid, robust, and require minimal s ...

Mass spectrometry (MS) is currently the most sensitive and selective analytical technique for routine peptide and protein structure analysis. Top-down proteomics is based on tandem mass spectrometry (MS/MS) of intact proteins, where multiply charged precur ...

Enhanced charging, or supercharging, of analytes in electrospray ionization mass spectrometry (ESI MS) facilitates high resolution MS by reducing an ion mass-to-charge (m/z) ratio, increasing tandem mass spectrometry (MS/MS) efficiency. ESI MS superchargin ...

Pairing light and heavy chains in monoclonal antibodies (mAbs) using top-down (TD) or middle-down (MD) mass spectrometry (MS) may complement the sequence information on single chains provided by high-throughput genomic sequencing and bottom-up proteomics, ...

This tutorial review describes the principles and practices of electron capture and transfer dissociation (ECD/ETD or ExD) mass spectrometry (MS) employed for peptide and protein structure analysis. ExD MS relies on interactions between gas phase peptide o ...

Despite the recent advances in structural analysis of monoclonal antibodies with bottom-up, middle-down, and top-down mass spectrometry (MS), further improvements in analysis accuracy, depth, and speed are needed. The remaining challenges include quantitat ...

Electron transfer dissociation (ETD)-based top-down mass spectrometry (MS) is the method of choice for in-depth structure characterization of large peptides, small- and medium-sized proteins, and non-covalent protein complexes. Here, we describe the perfor ...

Mass spectrometry-based qualitative and quantitative (bio)molecular analysis is a corner stone in the state-of-the-art pipelines in systems biology and environmental sciences. High-resolution and efficient tandem mass spectrometry methods and techniques ar ...

RATIONALE Similar to other mass spectrometric technologies based on ion trapping in a spatially restricted area, the performance of Orbitrap Fourier transform mass spectrometry (FTMS) is affected by the interaction between the trapped ion clouds. One of th ...

The primary structural information of proteins employed as biotherapeutics is essential if one wishes to understand their structure-function relationship, as well as in the rational design of new therapeutics and for quality control. Given both the large s ...

Luca Fornelli

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Ion coalescence in Fourier transform mass spectrometry: should we worry about this in shotgun proteomics?

Middle-down analysis of monoclonal antibodies with electron transfer dissociation Orbitrap FTMS

Glycan variability on a recombinant IgG antibody transiently produced in HEK-293E cells

Deamidation and Transamidation of Substance P by Tissue Transglutaminase Revealed by Electron-Capture Dissociation Fourier Transform Mass Spectrometry (Chem. Eur. J. 2/2011)

Distinguishing analyte from noise components in mass spectra of complex samples: where to cut the noise?

Structural analysis of intact monoclonal antibodies by electron transfer dissociation mass spectrometry

Top-down analysis of immunoglobulin G isotypes 1 and 2 with electron transfer dissociation on a high-field Orbitrap mass spectrometer

Practical Considerations for Improving the Productivity of Mass Spectrometry-based Proteomics

In-Spray Supercharging of Peptides and Proteins in Electrospray Ionization Mass Spectrometry

Multiplexed Middle-Down Mass Spectrometry as a Method for Revealing Light and Heavy Chain Connectivity in a Monoclonal Antibody

Principles of electron capture and transfer dissociation mass spectrometry applied to peptide and protein structure analysis

Advantages of Extended Bottom-Up Proteomics Using Sap9 for Analysis of Monoclonal Antibodies

Top-down analysis of 30–80 kDa proteins by electron transfer dissociation time-of-flight mass spectrometry

High-Resolution and Tandem Mass Spectrometry – the Indispensable Tools of the XXI Century

Top-down and middle-down mass spectrometry structural characterization of monoclonal antibodies

Observation of ion coalescence in Orbitrap Fourier transform mass spectrometry

Analysis of Intact Monoclonal Antibody IgG1 by Electron Transfer Dissociation Orbitrap FTMS