Isothermal Calorimetry Study of the Interactions of Type I Antifreeze Proteins with a Lipid Model Membrane

被引：6

作者：

Kun, Hagit ^{[1
]}

Mastai, Yitzhak ^{[1
]}

机构：

[1] Bar Ilan Univ, Dept Chem, Inst Nanotechnol, IL-52900 Ramat Gan, Israel

来源：

PROTEIN AND PEPTIDE LETTERS | 2010年 / 17卷 / 06期

关键词：

Antifreeze proteins; model membrane; isothermal titration calorimetry; thermal hysteresis; THERMOTROPIC PHASE-TRANSITIONS; PHOSPHOLIPID-VESICLES; SOMATOSTATIN ANALOG; THERMAL HYSTERESIS; PEPTIDE BINDING; HUMAN PLATELETS; SIGNAL PEPTIDE; TEMPERATURES; BILAYERS; LEAKAGE;

D O I：

10.2174/092986610791190354

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In this paper, we report our study of thermodynamic parameters of the interactions of antifreeze proteins (AFP) type I and it short segments with DMPC unilamellar vesicles as model for cell membrane. The heat of interactions between AFP's and the model cell membrane were studied by Isothermal Titration Calorimetry (ITC) at temperatures above and below phase transition temperatures of the membrane. It is shown that heat of interactions is linearly dependent on the temperatures below the phase transition of the membrane and constant at temperatures above phase. The heat of interaction above phase transition is assigned to the interaction of the AFP with the membrane, while below phase transition the ordering effect of the AFP influence the heat of interaction.

引用

页码：739 / 743

页数：5

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