journal article·2020-04-21Open access

Spontaneous Formation of Cushioned Model Membranes Promoted by an Intrinsically Disordered Protein

Yuri Gerelli, Amanda Eriksson Skog, Stephanie Jephthah, Rebecca J. L. Welbourn, Alexey Klechikov, Marie Skepö

Langmuir· Volume 36· Issue 15

Abstract

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.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Lipid Membrane Structure and Behavior · Nanopore and Nanochannel Transport Studies · Bacteriophages and microbial interactions

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Partnership for Soft Condensed Matter, Institut Laue-Langevin, 71 Avenue des Martyrs, 38000 Grenoble, France

Department of Life and Environmental Sciences, Polytechnic University of Marche, 60131 Ancona, Italy

Division of Theoretical Chemistry, Department of Chemistry, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden

ISIS Pulsed Neutron Facility, Rutherford Appleton Laboratory, Harwell Science and Innovation Campus, STFC, Didcot, Oxon OX11 0QX, United Kingdom

Department of Physics and Astronomy, Uppsala University, P.O. Box 516, SE-75120 Uppsala, Sweden

LINXS—Lund Institute of Advanced Neutron and X-ray Science, Scheelevägen 19, SE-233 70 Lund, Sweden

Funding

Crafoordska Stiftelsen · NordForsk

References (63)

Show source-provided references
1. 10.1021/la052687c10.1021/la052687c ↗
2. 10.1016/j.surfrep.2006.06.00110.1016/j.surfrep.2006.06.001 ↗
3. 10.1016/j.bbamem.2012.11.03310.1016/j.bbamem.2012.11.033 ↗
4. 10.3389/fchem.2018.0020410.3389/fchem.2018.00204 ↗
5. 10.1016/j.bbamem.2019.04.00310.1016/j.bbamem.2019.04.003 ↗
6. 10.1038/s41467-019-10058-710.1038/s41467-019-10058-7 ↗
7. 10.3390/antibiotics801001210.3390/antibiotics8010012 ↗
8. 10.1073/pnas.050458810210.1073/pnas.0504588102 ↗
9. 10.1021/acs.langmuir.9b0235010.1021/acs.langmuir.9b02350 ↗
10. 10.1021/la404580410.1021/la4045804 ↗
11. Wolfgang, K.; Wolfgang Peter, M. Polymer Membranes/Biomembranes; Springer: Berlin, Heidelberg, 2010; pp 78–111.
12. 10.1021/la401132c10.1021/la401132c ↗
13. 10.1016/j.jsb.2009.05.00810.1016/j.jsb.2009.05.008 ↗
14. 10.1021/la800018d10.1021/la800018d ↗
15. 10.1016/S0167-7799(99)01412-210.1016/S0167-7799(99)01412-2 ↗
16. 10.1016/S0006-3495(98)77680-510.1016/S0006-3495(98)77680-5 ↗
17. 10.1016/S0006-3495(99)76992-410.1016/S0006-3495(99)76992-4 ↗
18. 10.1016/S0006-3495(99)76993-610.1016/S0006-3495(99)76993-6 ↗
19. 10.1126/science.271.5245.4310.1126/science.271.5245.43 ↗
20. 10.1098/rsif.2014.023210.1098/rsif.2014.0232 ↗
21. Oppenheim F. G. · J. Biol. Chem. · 1988 · 263 · 747210.1016/S0021-9258(18)68522-9 ↗
22. 10.1016/S1093-3263(00)00138-810.1016/S1093-3263(00)00138-8 ↗
23. 10.1016/S0968-0004(02)02169-210.1016/S0968-0004(02)02169-2 ↗
24. 10.1128/EC.00095-1410.1128/EC.00095-14 ↗
25. 10.1042/bj356036110.1042/bj3560361 ↗
26. 10.1177/0022034590069001010110.1177/00220345900690010101 ↗
27. 10.1128/IAI.64.12.5000-5007.199610.1128/IAI.64.12.5000-5007.1996 ↗
28. 10.1177/15441113020130020810.1177/154411130201300208 ↗
29. 10.1046/j.1432-1327.2001.02350.x10.1046/j.1432-1327.2001.02350.x ↗
30. 10.1128/IAI.59.8.2549-2554.199110.1128/IAI.59.8.2549-2554.1991 ↗
31. 10.1074/jbc.M00822920010.1074/jbc.M008229200 ↗
32. 10.1021/ct501178z10.1021/ct501178z ↗
33. 10.1002/prot.2502510.1002/prot.25025 ↗
34. 10.1002/(SICI)1097-0282(199801)45:1<51::AID-BIP5>3.0.CO;2-Y10.1002/(SICI)1097-0282(199801)45:1<51::AID-BIP5>3.0.CO;2-Y ↗
35. 10.1139/o98-06610.1139/o98-066 ↗
36. 10.1021/acs.jctc.8b0128110.1021/acs.jctc.8b01281 ↗
37. 10.1016/j.jcis.2016.01.02510.1016/j.jcis.2016.01.025 ↗
38. 10.1002/prot.2444510.1002/prot.24445 ↗
39. 10.1016/j.jcis.2017.01.08710.1016/j.jcis.2017.01.087 ↗
40. 10.1007/BF0133793710.1007/BF01337937 ↗
41. Höök F. · 1997
42. 10.1016/0005-2736(92)90101-Q10.1016/0005-2736(92)90101-Q ↗
43. 10.1021/jp983996x10.1021/jp983996x ↗
44. 10.1021/la200683e10.1021/la200683e ↗
45. 10.1021/ja801111610.1021/ja8011116 ↗
46. 10.1016/0921-4526(91)90044-F10.1016/0921-4526(91)90044-F ↗
47. 10.1016/j.physb.2006.05.40010.1016/j.physb.2006.05.400 ↗
48. 10.1080/10448632.2015.105705410.1080/10448632.2015.1057054 ↗
49. 10.1107/S160057671800239X10.1107/S160057671800239X ↗
50. 10.1016/j.nima.2014.07.02910.1016/j.nima.2014.07.029 ↗
51. 10.1107/S160057671600010810.1107/S1600576716000108 ↗
52. 10.1103/PhysRevLett.122.24810110.1103/PhysRevLett.122.248101 ↗
53. Biomolecular Scattering Length Density Calculator. http://psldc.isis.rl.ac.uk/Psldc/.
54. 10.1099/00221287-86-1-11510.1099/00221287-86-1-115 ↗
55. 10.1016/j.colsurfb.2015.07.03910.1016/j.colsurfb.2015.07.039 ↗
56. 10.1016/j.bpj.2014.09.02710.1016/j.bpj.2014.09.027 ↗
57. Yeung J. C. I. · 2016
58. 10.1021/acs.jctc.6b0042910.1021/acs.jctc.6b00429 ↗
59. 10.1093/jxb/erq08210.1093/jxb/erq082 ↗
60. 10.1038/ncomms1244710.1038/ncomms12447 ↗
61. 10.1021/acs.langmuir.8b0347410.1021/acs.langmuir.8b03474 ↗
62. 10.1126/science.aat419110.1126/science.aat4191 ↗
63. 10.1021/acs.jpclett.9b0280410.1021/acs.jpclett.9b02804 ↗