Table_3_Transmembrane Peptides as Sensors of the Membrane Physical State.DOCX (19.05 kB)

Table_3_Transmembrane Peptides as Sensors of the Membrane Physical State.DOCX

Download (19.05 kB)
posted on 24.05.2018 by Stefano Piotto, Luigi Di Biasi, Lucia Sessa, Simona Concilio

Cell membranes are commonly considered fundamental structures having multiple roles such as confinement, storage of lipids, sustain and control of membrane proteins. In spite of their importance, many aspects remain unclear. The number of lipid types is orders of magnitude larger than the number of amino acids, and this compositional complexity is not clearly embedded in any membrane model. A diffused hypothesis is that the large lipid palette permits to recruit and organize specific proteins controlling the formation of specialized lipid domains and the lateral pressure profile of the bilayer. Unfortunately, a satisfactory knowledge of lipid abundance remains utopian because of the technical difficulties in isolating definite membrane regions. More importantly, a theoretical framework where to fit the lipidomic data is still missing. In this work, we wish to utilize the amino acid sequence and frequency of the membrane proteins as bioinformatics sensors of cell bilayers. The use of an alignment-free method to find a correlation between the sequences of transmembrane portion of membrane proteins with the membrane physical state (MPS) suggested a new approach for the discovery of antimicrobial peptides.