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SUMMARY:Keynote talk - Models of biological membranes: complex lipid compo
 sition and membrane proteins
DTSTART;VALUE=DATE-TIME:20211208T090000Z
DTEND;VALUE=DATE-TIME:20211208T094000Z
DTSTAMP;VALUE=DATE-TIME:20260530T235605Z
UID:indico-contribution-1354@lindico453.srv.lu.se
DESCRIPTION:Speakers: Alessandra  Luchini ()\nBiological membranes are mai
 nly composed of lipids and proteins. Unfortunately\, the complex compositi
 on of biological membranes prevents their direct investigation with biophy
 sical methods. Therefore\, most physico-chemical and biophysical studies o
 n biological membranes rely on simple models composed of lipid bilayers in
 cluding only 1-3 lipid species and in fewer cases membrane proteins. Among
  all\, supported lipid bilayers represent suitable systems to mimic the li
 pid component of biological membranes and allow for structural and dynamic
  investigations by means of several surface sensitive techniques. However\
 , loading membrane proteins with controlled orientation in a supported lip
 id bilayer remains a challenge in this field.[1]\nRecently\, we showed the
  preparation and characterization of lipid bilayers including either compl
 ex lipid mixtures\, i.e. lipid extract from the yeast Pichia Pastoris\, or
  membrane proteins. Supported lipid bilayers with or without membrane prot
 eins were prepared by a recently developed protocol. The method is based\n
 on the application of peptide-discs [2]\, a specific kind of nanodiscs whe
 re the protein belt is composed by self-assembled 18A peptide molecules. T
 he peptide discs can be adsorbed on the hydrophilic surface of the solid s
 upport and since the formation of the 18A belt is reversible\, they can be
  disassembled by rinsing with fresh buffer solution. We showed that this m
 ethod can successfully lead to the production of supported lipid bilayer w
 ith biologically relevant lipid compositions [3] and also to the incorpora
 tion of membrane protein with asymmetric structure\, i.e. composed by one 
 large extramembrane domain (EMD) a transmembrane domain (TMD).[4]\nReferen
 ces:\n[1] G. Fragneto et al.\, Current Opinion in Colloid & Interface Scie
 nce\, 2018\, 38\, 108-121.\n[2] S. R. Mitdgaard et al.\, Soft Matter\, 201
 4\, 10\, 738-752.\n[3] A. Luchini et al.\, Anlytical Chemistry\, 2020\, 92
 \, 1\, 1081-1088.\n[4] A. Luchini et al.\, JCIS\, 2021\, 585\, 376-385.\n\
 nhttps://lindico453.srv.lu.se/event/250/contributions/1354/
LOCATION:
URL:https://lindico453.srv.lu.se/event/250/contributions/1354/
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