Design and use of model membranes to study biomolecular interactions using complementary surface-sensitive techniques
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Design and use of model membranes to study biomolecular interactions using complementary surface-sensitive techniques. / Clifton, L.A.; Campbell, R.A.; Sebastiani, F.; Campos-Terán, J.; Gonzalez-Martinez, J.F.; Björklund, S.; Sotres, J.; Cárdenas, Marité.
In: Advances in Colloid and Interface Science, Vol. 277, 102118, 2020.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Design and use of model membranes to study biomolecular interactions using complementary surface-sensitive techniques
AU - Clifton, L.A.
AU - Campbell, R.A.
AU - Sebastiani, F.
AU - Campos-Terán, J.
AU - Gonzalez-Martinez, J.F.
AU - Björklund, S.
AU - Sotres, J.
AU - Cárdenas, Marité
PY - 2020
Y1 - 2020
N2 - Cellular membranes are complex structures and simplified analogues in the form of model membranes or biomembranes are used as platforms to understand fundamental properties of the membrane itself as well as interactions with various biomolecules such as drugs, peptides and proteins. Model membranes at the air-liquid and solid-liquid interfaces can be studied using a range of complementary surface-sensitive techniques to give a detailed picture of both the structure and physicochemical properties of the membrane and its resulting interactions. In this review, we will present the main planar model membranes used in the field to date with a focus on monolayers at the air-liquid interface, supported lipid bilayers at the solid-liquid interface and advanced membrane models such as tethered and floating membranes. We will then briefly present the principles as well as the main type of information on molecular interactions at model membranes accessible using a Langmuir trough, quartz crystal microbalance with dissipation monitoring, ellipsometry, atomic force microscopy, Brewster angle microscopy, Infrared spectroscopy, and neutron and X-ray reflectometry. A consistent example for following biomolecular interactions at model membranes is used across many of the techniques in terms of the well-studied antimicrobial peptide Melittin. The overall objective is to establish an understanding of the information accessible from each technique, their respective advantages and limitations, and their complementarity.
AB - Cellular membranes are complex structures and simplified analogues in the form of model membranes or biomembranes are used as platforms to understand fundamental properties of the membrane itself as well as interactions with various biomolecules such as drugs, peptides and proteins. Model membranes at the air-liquid and solid-liquid interfaces can be studied using a range of complementary surface-sensitive techniques to give a detailed picture of both the structure and physicochemical properties of the membrane and its resulting interactions. In this review, we will present the main planar model membranes used in the field to date with a focus on monolayers at the air-liquid interface, supported lipid bilayers at the solid-liquid interface and advanced membrane models such as tethered and floating membranes. We will then briefly present the principles as well as the main type of information on molecular interactions at model membranes accessible using a Langmuir trough, quartz crystal microbalance with dissipation monitoring, ellipsometry, atomic force microscopy, Brewster angle microscopy, Infrared spectroscopy, and neutron and X-ray reflectometry. A consistent example for following biomolecular interactions at model membranes is used across many of the techniques in terms of the well-studied antimicrobial peptide Melittin. The overall objective is to establish an understanding of the information accessible from each technique, their respective advantages and limitations, and their complementarity.
U2 - 10.1016/j.cis.2020.102118
DO - 10.1016/j.cis.2020.102118
M3 - Journal article
VL - 277
JO - Advances in Colloid and Interface Science
JF - Advances in Colloid and Interface Science
SN - 0001-8686
M1 - 102118
ER -
ID: 348242626