Membrane proteins are important macromolecules that play crucial roles in many cellular and physiological processes. Over the past two decades, the use of mass spectrometry as a biophysical tool to characterise membrane proteins has grown steadily. By capturing these dynamic complexes in the gas phase, many unknown small molecule interactions have been revealed. One particular application of this research has been the focus on antibiotic resistance with considerable efforts being made to understand underlying mechanisms. Here we review recent advances in the application of mass spectrometry that have yielded both structural and dynamic information on the interactions of antibiotics with proteins involved in bacterial cell envelope biogenesis and drug efflux.
Mass spectrometry informs the structure and dynamics of membrane proteins involved in lipid and drug transport / Bolla, J. R.; Fiorentino, F.; Robinson, C. V.. - In: CURRENT OPINION IN STRUCTURAL BIOLOGY. - ISSN 0959-440X. - 70:(2021), pp. 53-60. [10.1016/j.sbi.2021.03.014]
Mass spectrometry informs the structure and dynamics of membrane proteins involved in lipid and drug transport
Fiorentino F.Secondo
;
2021
Abstract
Membrane proteins are important macromolecules that play crucial roles in many cellular and physiological processes. Over the past two decades, the use of mass spectrometry as a biophysical tool to characterise membrane proteins has grown steadily. By capturing these dynamic complexes in the gas phase, many unknown small molecule interactions have been revealed. One particular application of this research has been the focus on antibiotic resistance with considerable efforts being made to understand underlying mechanisms. Here we review recent advances in the application of mass spectrometry that have yielded both structural and dynamic information on the interactions of antibiotics with proteins involved in bacterial cell envelope biogenesis and drug efflux.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.