Computational evaluation on the binding affinity of non-specific lipid-transfer protein-2 with fatty acids

被引：11
|
作者：
Tousheh, Mojtaba [1 ]
Miroliaei, Mehran [1 ]
Rastegari, Ali Asghar [2 ]
Ghaedi, Kamran [1 ]
Esmaeili, Abolghasem [2 ]
Matkowski, Adam [3 ]
机构：
[1] Univ Isfahan, Fac Sci, Dept Biol, Esfahan, Iran
[2] Islamic Azad Univ, Falavarjan Branch, Dept Mol & Cell Biochem, Esfahan, Iran
[3] Med Univ Wroclaw, Dept Pharmaceut Biol & Bot, PL-50556 Wroclaw, Poland
来源：
COMPUTERS IN BIOLOGY AND MEDICINE | 2013年 / 43卷 / 11期
基金：
美国国家科学基金会;
关键词：
Lipid binding proteins; Fatty acids; Drug carriers; Protein Data Bank; POTENTIAL APPLICATION; ACCURACY; REVEALS;
D O I：
10.1016/j.compbiomed.2013.08.012
中图分类号：
Q [生物科学];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
A computational study was carried out to identify the structural determinant controlling the affinity, specificity and binding strength of several saturated and unsaturated fatty acids with Oryza sativa (Indica group) nonspecific lipid transfer protein (nsLTP2). Association between the number, position and conformation of hydrophobic patches and lipid binding properties of the protein was evidenced by docking analysis. Binding affinity is influenced by the number of carbon atoms, location of double bonds and hydroxyl group in the acyl chain. The results may direct at developing applications in LTP-mediated transport and controlled release of low molecular weight drugs. (C) 2013 Elsevier Ltd. All rights reserved.
引用
收藏
页码：1732 / 1738
页数：7
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