Lactophoricin-I (LPcin-I), an antimicrobial cationic peptide with 23 amino acid residues isolated from bovine milk, and LPcin-II, which lacks six N-terminal amino acids with respect to LPcin-I, were investigated at a mercury-supported tethered bilayer lipid membrane (tBLM) consisting of a 2,3,di-O-phytanyl-sn-glycerol-1-tetraethylene-glycol-d,l-α lipoic acid ester thiolipid (DPTL) with a dioleoylphosphatidylcholine (DOPC) or dioleoylphosphatidylserine (DOPS) monolayer on top.
Channel-forming activity of lactophoricins I and II in mercury-supported tethered bilayer lipid membranes / Becucci, Lucia; Aloisi, Giovanni; Scaloni, Andrea; Guidelli, Rolando. - In: JOURNAL OF ELECTROANALYTICAL CHEMISTRY. - ISSN 1572-6657. - STAMPA. - ..:(2017), pp. 0-0. [10.1016/j.jelechem.2017.08.030]
Channel-forming activity of lactophoricins I and II in mercury-supported tethered bilayer lipid membranes
BECUCCI, LUCIA;ALOISI, GIOVANNI DOMENICO;GUIDELLI, ROLANDO
2017
Abstract
Lactophoricin-I (LPcin-I), an antimicrobial cationic peptide with 23 amino acid residues isolated from bovine milk, and LPcin-II, which lacks six N-terminal amino acids with respect to LPcin-I, were investigated at a mercury-supported tethered bilayer lipid membrane (tBLM) consisting of a 2,3,di-O-phytanyl-sn-glycerol-1-tetraethylene-glycol-d,l-α lipoic acid ester thiolipid (DPTL) with a dioleoylphosphatidylcholine (DOPC) or dioleoylphosphatidylserine (DOPS) monolayer on top.
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