TY - JOUR
T1 - Spontaneous Formation of Cushioned Model Membranes Promoted by an Intrinsically Disordered Protein
AU - Gerelli, Yuri
AU - Eriksson Skog, Amanda
AU - Jephthah, Stephanie
AU - Welbourn, Rebecca J.L.
AU - Klechikov, Alexey
AU - Skepö, Marie
PY - 2020/4/21
Y1 - 2020/4/21
N2 - In this article, it is shown that by exposing commonly used lipids for biomembrane mimicking studies, to a solution containing the histidine-rich intrinsically disordered protein histatin 5, a protein cushion spontaneously forms underneath the bilayer. The underlying mechanism is attributed to have an electrostatic origin, and it is hypothesized that the observed behavior is due to proton charge fluctuations promoting attractive electrostatic interactions between the positively charged proteins and the anionic surfaces, with concomitant counterion release. Hence, we anticipate that this novel "green" approach of forming cushioned bilayers can be an important tool to mimic the cell membrane without the disturbance of the solid substrate, thereby achieving a further understanding of protein-cell interactions.
AB - In this article, it is shown that by exposing commonly used lipids for biomembrane mimicking studies, to a solution containing the histidine-rich intrinsically disordered protein histatin 5, a protein cushion spontaneously forms underneath the bilayer. The underlying mechanism is attributed to have an electrostatic origin, and it is hypothesized that the observed behavior is due to proton charge fluctuations promoting attractive electrostatic interactions between the positively charged proteins and the anionic surfaces, with concomitant counterion release. Hence, we anticipate that this novel "green" approach of forming cushioned bilayers can be an important tool to mimic the cell membrane without the disturbance of the solid substrate, thereby achieving a further understanding of protein-cell interactions.
UR - http://www.scopus.com/inward/record.url?scp=85083912949&partnerID=8YFLogxK
U2 - 10.1021/acs.langmuir.0c00120
DO - 10.1021/acs.langmuir.0c00120
M3 - Article
C2 - 32212610
AN - SCOPUS:85083912949
SN - 0743-7463
VL - 36
SP - 3997
EP - 4004
JO - Langmuir
JF - Langmuir
IS - 15
ER -