Spectroscopic and AFM characterization of polypeptide-surface interactions: Controls and lipid quantitative analyses

Autor: Øyvind Halskau, Hanzhen Wen, Øyvind Strømland, Samuel Furse, Morten L. Govasli, Ørjan S. Handegård
Rok vydání: 2017
Předmět:
0301 basic medicine
Circular dichroism
Conformational change
PC
Phosphatidylcholine

Lipid bilayers
DPX
p-Xylene-Bis-Pyridinium Bromide

PS
Phosphatidylserine

NMR
Nuclear Magnetic Resonance

lcsh:Computer applications to medicine. Medical informatics
FRET
Förster Resonance Energy Transfer

Solid-supported bilayers
Fluorescence spectroscopy
Fluorescence
03 medical and health sciences
Quantitiative 31P NMR
EYPC
egg yolk phosphatidylcholine

Spin-coating
Lipid bilayer
lcsh:Science (General)
Data Article
Multidisciplinary
ANTS
8-Aminonaphthalene-1
3
6-Trisulfonic Acid Disodium Salt

030102 biochemistry & molecular biology
CD
Circular Dichroism

PBPS
porcine brain phosphatidylserine

Chemistry
CUBO solvent
Culeddu-Bosco solvent

Vesicle
Polypeptide aggregation
DLS
Dynamic Light Scattering

PA
Phosphatidic Acid

PC-plas
Phosphatidylcholine plasmalogen

Chemical degradation
Crystallography
030104 developmental biology
Förster resonance energy transfer
Membrane
AFM
Atomic Force Microscopy

SLB
Solid-supported Lipid Bilayers

PS-plas
Phosphatidylserine plasmalogen

lcsh:R858-859.7
LUV
Large Unilamellar Vesicles

lcsh:Q1-390
Zdroj: Data in Brief
Data in Brief, Vol 12, Iss C, Pp 113-122 (2017)
ISSN: 2352-3409
Popis: This article is related to http://dx.doi.org/10.1016/j.bbamem.2017.01.005 (O. Stromland, O.S. Handegard, M.L. Govasli, H. Wen, O. Halskau, 2017) [1]. In protein and polypeptide-membrane interaction studies, negatively charged lipids are often used as they are a known driver for membrane interaction. When using fluorescence spectroscopy and CD as indicators of polypeptide binding and conformational change, respectively, the effect of zwitterionic lipids only should be documented. The present data documents several aspects of how two engineered polypeptides (A-Cage-C and A-Lnk-C) derived from the membrane associating protein alpha-Lactalbumin affects and are affected by the presence of zwitterionic bilayers in the form of vesicles. We here document the behavior or the Cage and Lnk segments with respect to membrane interaction and their residual fold, using intrinsic tryptophan fluorescence assays. This data description also documents the coverage of solid-supported bilayers prepared by spin-coating mica using binary lipid mixes, a necessary step to ensure that AFM is performed on areas that are covered by lipid bilayers when performing experiments. Uncovered patches are detectable by both force curve measurements and height measurements. We tested naked mica׳s ability to cause aggregation as seen by AFM, and found this to be low compared to preparations containing negatively charged lipids. Work with lipids also carries the risk of chemical degradation taking place during vesicles preparation or other handling of the lipids. We therefor use 31P NMR to quantify the head-group content of commonly used commercial extracts before and after a standard protocol for vesicle production is applied.
Databáze: OpenAIRE