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Pot, S.

Publications and source records attributed to Pot, S..

2 recordsLinked to original sources

Increasing Applicability of Automated mD-LC-MS Peptide Mapping for Biopharmaceuticals via Streamlined In-Solution Digestion

Since the introduction of the first multidimensional liquid chromatography mass spectrometry (mD-LC-MS) approach for antibody peak characterization, multiple developments have been reported including integration of various chromatographic approaches and precise fractionation, providing high quality and reliable peptide data in a drastically decreased total analysis time. Most of these platforms rely on the use of immobilized enzyme reactors (IMERs) for digestion, limiting the applicability to few enzymes such as trypsin. Recently, the introduction of in-solution enzymatic digestion in mD-LC-MS systems has been proposed as an alternative to IMERs. Here, we make use of current innovations in 2D-LC commercial systems such as active solvent modulation valves, which permits direct mixing of the fractionated peaks with the endoprotease and reducing agent in an online manner, to integrate in-solution digestion in a straightforward manner in mD-LC-MS peak characterization platforms. Following antibody digestion, the generated peptides are automatically trapped, separated and detected by mass spectrometry. Efficient reduction and tryptic digestion was obtained using short incubation times (15 min). The approach was further expanded to alternative endoproteases such as chymotrypsin and thermolysine with other digestion specificities and allow an easy exchange between enzymes with similar buffer and digestion conditions. As a proof-of-principle that strategy was applied to achieve peptide maps from ion exchanged separated mAb peaks showing good digestion efficiency and high sequence coverages.

biochemistry↗

Tissue Transglutaminase 2 has higher affinity for relaxed than for stretched fibronectin fibers

Tissue transglutaminase 2 (TG2) plays a vital role in stabilizing extracellular matrix (ECM) proteins through enzymatic crosslinking during tissue growth, repair, and inflammation. TG2 also binds non-covalently to fibronectin (FN), an essential component of the ECM, facilitating cell adhesion, migration, proliferation, and survival. However, the interaction between TG2 and fibrillar FN remains poorly understood, as most studies have focused on soluble or surface-adsorbed FN or FN fragments, which differ in their conformations from insoluble FN fibers. Using a well-established in vitro FN-fiber stretch assay, we discovered that the binding of a crosslinking enzyme to ECM fibers is mechano-regulated. TG2 binding to FN is tuned by the mechanical tension of FN fibers, whereby TG2 predominantly co-localizes to low-tension FN fibers, while fiber stretching reduces their affinity for TG2. This mechano-regulated binding relies on the proximity between the N-terminal {beta}-sandwich and C-terminal {beta}-barrels of TG2. Crosslinking mass spectrometry (XL-MS) revealed a novel TG2-FN synergy site within TG2s C-terminal {beta}-barrels that interacts with FN regions outside of the canonical gelatin binding domain, specifically FNI2 and FNIII14-15. Combining XL-MS distance restraints with molecular docking reveals the mechano-regulated binding mechanism between TG2 and modules FNI7-9 by which mechanical forces regulate TG2-FN interactions. This highlights a previously unrecognized role of TG2 as a tension sensor for FN fibers. This novel interaction mechanism has significant implications in physiology and mechanobiology, including how force regulate ECM deposition and maturation, and how TG2 mediates cell-ECM adhesion in health and in various pathophysiological processes. Data are available via ProteomeXchange with identifier PXD043976.

molecular biology↗