A calorimetric investigation of the interaction of short chain alcohols with unilamellar DMPC liposomes
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
A calorimetric investigation of the interaction of short chain alcohols with unilamellar DMPC liposomes. / Trandum, Christa; Westh, Peter; Jørgensen, Kent; Mouritsen, Ole G.
In: Journal of Physical Chemistry B, Vol. 103, No. 22, 03.06.1999, p. 4751-4756.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - A calorimetric investigation of the interaction of short chain alcohols with unilamellar DMPC liposomes
AU - Trandum, Christa
AU - Westh, Peter
AU - Jørgensen, Kent
AU - Mouritsen, Ole G.
PY - 1999/6/3
Y1 - 1999/6/3
N2 - The molecular mechanisms by which ethanol and other short-chain alcohols perturb biological systems have been suggested to involve specific interactions with proteins and/or nonspecific interactions with the lipid bilayer part of biological membranes. To gain insight into the influence of alcohols on well-defined lipid bilayers, isothermal titration calorimetry (ITC) is used to determine the excess partial molar enthalpy of alcohol in liposome suspensions as well as the excess partial molar enthalpy of liposomes in dilute alcohol-water mixtures at temperatures above the main phase transition of dimyristoyl phosphatidylcholine (DMPC). The alcohols investigated were ethanol, 1-propanol, and 1-butanol. The calorimetric data were used to evaluate molecular interactions and based on a simple partitioning model the standard molar enthalpy of transferring alcohol from water into unilamellar DMPC liposomes was determined. The results reveal that the interaction of short-chain alcohols with the DMPC lipid bilayer is endothermic and strongly dependent on temperature indicating that a major contribution to the energetics of the association is dehydration of nonpolar moieties. Furthermore the data show that the interactions become increasingly unfavorable in terms of enthalpy with increasing size of the nonpolar surface area of the alcohol.
AB - The molecular mechanisms by which ethanol and other short-chain alcohols perturb biological systems have been suggested to involve specific interactions with proteins and/or nonspecific interactions with the lipid bilayer part of biological membranes. To gain insight into the influence of alcohols on well-defined lipid bilayers, isothermal titration calorimetry (ITC) is used to determine the excess partial molar enthalpy of alcohol in liposome suspensions as well as the excess partial molar enthalpy of liposomes in dilute alcohol-water mixtures at temperatures above the main phase transition of dimyristoyl phosphatidylcholine (DMPC). The alcohols investigated were ethanol, 1-propanol, and 1-butanol. The calorimetric data were used to evaluate molecular interactions and based on a simple partitioning model the standard molar enthalpy of transferring alcohol from water into unilamellar DMPC liposomes was determined. The results reveal that the interaction of short-chain alcohols with the DMPC lipid bilayer is endothermic and strongly dependent on temperature indicating that a major contribution to the energetics of the association is dehydration of nonpolar moieties. Furthermore the data show that the interactions become increasingly unfavorable in terms of enthalpy with increasing size of the nonpolar surface area of the alcohol.
UR - http://www.scopus.com/inward/record.url?scp=0000445890&partnerID=8YFLogxK
M3 - Journal article
AN - SCOPUS:0000445890
VL - 103
SP - 4751
EP - 4756
JO - Journal of Physical Chemistry B Materials
JF - Journal of Physical Chemistry B Materials
SN - 1089-5647
IS - 22
ER -
ID: 236895097