Electrospray ionization mass spectrometry for the study of non-covalent complexes: an emerging technology

Identification of natural ligands of retinoic acid receptor-related orphan receptor α ligand-binding domain expressed in Sf9 cells––a mass spectrometry approach

“…Nevertheless, mass measurements under identical concentration, solvent, and instrumental conditions may allow one to compare the relative stability of the protein-ligand interaction in a series of different ligand-binding experiments involving the same protein host. Inducing source collisions by altering, e.g., increasing, Vc, is known to increases the internal energy imparted to the complex and often causes dissociation of the complex [26].…”

“…The strong dependence of complex abundance on parameters such as solvent, protein concentration, ionic strength, pH, counter ions, flow rate, ionization source temperature, and orificial potential does not yet allow the determination of the absolute dissociation constants [26,28,34]. Nevertheless, mass measurements under identical concentration, solvent, and instrumental conditions may allow one to compare the relative stability of the protein-ligand interaction in a series of different ligand-binding experiments involving the same protein host.…”

“…Electrospray ionization (ESI) is known to be a soft-ionization technique and was previously shown to yield multiply charged ion species of intact proteinligand complexes present in aqueous solution [26][27][28]. The use of ESI-MS for the identification and study of the protein-ligand in nuclear receptors such as peroxisome proliferator-activated receptor (PPAR), retinoid acid receptors (RARa and RXRa), and estrogen-related receptor (ERR3) has also been reported [29][30][31].…”

Noncovalent interaction between amyloid-β-peptide (1–40) and oleuropein studied by electrospray ionization mass spectrometry

“…In general, noncovalent interactions between proteins/ peptides and ligands may be involved in triggering diseases. Thus, the elucidation of the structure and the formation mechanism of noncovalent complexes between proteins and ligands may lead to a better understanding of a disease process and the development of a therapeutic approach [41]. This is the first report of detecting noncovalent complexes between A␤ and naturally occurring compounds by ESI MS.…”

Transmembrane Delivery and Biological Effect of Human Growth Hormone Via a Phage Displayed Peptide In Vivo and In Vitro

“…It has been established that cellular function is often triggered by weak noncovalent complex in molecular interactions. 41 Similarly, TD interaction with PC is very important in understanding the molecular mechanism of TD transmembrane activity. Here, the ESI-MS results demonstrated that TD was able to form a noncovalent complex and showed stronger binding affinities with PC, compared to cholesterol, whose lack of interaction could be attributed to cholesterol's structure lacking a phosphatidyl moiety.…”