Show/Hide Menu
Hide/Show Apps
Logout
Türkçe
Türkçe
Search
Search
Login
Login
OpenMETU
OpenMETU
About
About
Open Science Policy
Open Science Policy
Open Access Guideline
Open Access Guideline
Postgraduate Thesis Guideline
Postgraduate Thesis Guideline
Communities & Collections
Communities & Collections
Help
Help
Frequently Asked Questions
Frequently Asked Questions
Guides
Guides
Thesis submission
Thesis submission
MS without thesis term project submission
MS without thesis term project submission
Publication submission with DOI
Publication submission with DOI
Publication submission
Publication submission
Supporting Information
Supporting Information
General Information
General Information
Copyright, Embargo and License
Copyright, Embargo and License
Contact us
Contact us
Effect of progesterone on DPPC membrane: Evidence for lateral phase separation and inverse action in lipid dynamics
Date
2005-08-15
Author
Korkmaz, F
Severcan, Feride
Metadata
Show full item record
This work is licensed under a
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
.
Item Usage Stats
217
views
0
downloads
Cite This
Interactions of progesterone with zwitterionic dipalmitoyl phosphatidylcholine (DPPC) triultilamellar liposomes were investigated as a function of temperature and progesterone concentration by using three non-invasive techniques namely Fourier transform infrared spectroscopy, turbidity at 440 nm, and differential scanning calorimetry. The results reveal that progesterone changes the physical properties of DPPC bilayers by decreasing the main phase-transition temperature, abolishing the pre-transition, broadening the phase-transition profile, disordering the system both in gel and liquid crystalline phase, increasing the dynamics at low concentrations whereas stabilizing the membrane at high concentrations, and inducing phase separation. Progesterone does not change the hydration of the C=O groups, while it strengthens the hydrogen bonding between the PO (2) over bar groups of lipids and the water molecules around. (c) 2005 Elsevier Inc. All rights reserved.
Subject Keywords
Biophysics
,
Biochemistry
,
Molecular Biology
URI
https://hdl.handle.net/11511/57281
Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
DOI
https://doi.org/10.1016/j.abb.2005.06.013
Collections
Department of Biology, Article
Suggestions
OpenMETU
Core
IR and turbidity studies of vitamin E-cholesterol-phospholipid membrane interactions
Severcan, Feride; Kazanci, Nadide; Baykal, Ülkü; Süzer, Şefik (Portland Press Ltd., 1995-8-1)
Binary and tertiary mixture of α-tocophenol, cholesterol and dimyristoylphosphatidylcholine in the form of multilamellar liposomes were investigated by Fourier Transform Infrared and visible spectroscopy. Results of the FTIR and turbidity experiments indicate that α T decreases or diminishes the effect of cholesterol on the frequency and the bandwidth of the C-H stretching, CH2 scissoring and C=O stretching bands in FTIR spectra and the turbidity measurements (recorded as absorbance values at 440 nm) in pho...
Using artificially generated spectral data to improve protein secondary structure prediction from Fourier transform infrared spectra of proteins
Severcan, M; Haris, PI; Severcan, Feride (Elsevier BV, 2004-09-15)
Secondary structures of proteins have been predicted using neural networks from their Fourier transform infrared spectra. To improve the generalization ability of the neural networks, the training data set has been artificially increased by linear interpolation. The leave-one-out approach has been used to demonstrate the applicability of the method. Bayesian regularization has been used to train the neural networks and the predictions have been further improved by the maximum-likelihood estimation method. T...
The effect of cysteine-43 mutation on thermostability and kinetic properties of citrate synthase from Thermoplasma acidophilum
Kocabıyık, Semra; Russel, RJM; Danson, MJ; Hough, DW (Elsevier BV, 1996-07-05)
In this study, we have substituted serine-43 by cysteine in the recombinant citrate synthase from a moderately thermophilic Archaeon Thermoplasma acidophilum, for site-specific attachment of labels and have investigated the effects of this mutation on the biochemical properties and thermal stability of the enzyme. Both wild-type and the mutant enzymes were purified to homogenity using affinity chromatography on Matrex Gel Red A. The mutant Thermoplasma citrate synthase is very similar to wild-type citrate s...
Effect of gramicidin S on the dipalmitoylphosphatidyl-glycerol thermotropic phase transition in DPPG/GS systems: A mathematical approach
Stan, Cristina; Cristescu, C. P.; Severcan, Feride; Dorohoi, Dana (Informa UK Limited, 2006-01-01)
We present a mathematical approach to the experimental data recorded via Fourier transform-infrared spectroscopy regarding the influence of the concentration of the antimicrobial peptide gramicidin S (GS) on the thermotropic phase transition of the dipalmitoylphosphatidyl-glycerol (DPPG) lipid bilayer membrane in DPPG/GS systems. The model is based on the influence of the GS concentration on the parameters of a nonlinear damped oscillator, which models the CH2 symmetric stretching band.
Interactions of tamoxifen with distearoyl phosphatidylcholine multilamellar vesicles: FTIR and DSC studies
Bilge, Duygu; ŞAHİN, İPEK; KAZANCI, NADİDE; Severcan, Feride (Elsevier BV, 2014-09-15)
Interactions of a non-steroidal antiestrogen drug, tamoxifen (TAM), with distearoyl-sn-glycero-3-phosphatidylcholine (DSPC) multilamellar liposomes (MLVs) were investigated as a function of drug concentration (1-15 mol%) by using two noninvasive techniques, namely Fourier transform infrared (FTIR) spectroscopy and differential scanning calorimetry (DSC). FTIR spectroscopy results show that increasing TAM concentrations (except 1 mol%) increased the wavenumbers of the CH2 stretching modes, implying an disord...
Citation Formats
IEEE
ACM
APA
CHICAGO
MLA
BibTeX
F. Korkmaz and F. Severcan, “Effect of progesterone on DPPC membrane: Evidence for lateral phase separation and inverse action in lipid dynamics,”
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
, pp. 141–147, 2005, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/57281.