Chaperone activities of bovine and camel β-caseins: Importance of their surface hydrophobicity in protection against alcohol dehydrogenase aggregation

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• 作者：Abolfazl Barzegar ; Reza Yousefi ; Ahmad Sharifzadeh ; Michè ; le Dalgalarrondo ; Jean-Marc Chobert ; Mohammad Reza Ganjali ; Parviz Norouzi ; Mohammad Reza Ehsani ; Amir Niasari-Naslaji ; Ali Akbar Saboury
• 关键词：Intrinsically unstructured proteins (IUP) ; β ; -Casein ; Aggregation ; Alcohol dehydrogenase (ADH) ; Chaperone ; Hydrophobicity
• 刊名：International Journal of Biological Macromolecules
• 出版年：2008
• 期刊代码：62_01418130
• 类别：abs
• 出版时间：1 May 2008
• 卷：42
• 期：4
• 页码：392-399
• 文件大小：729 K

摘要

β-Casein (β-CN) showing properties of intrinsically unstructured proteins (IUP) displays many similarities with molecular chaperones and shows anti-aggregation activity in vitro. Chaperone activities of bovine and camel β-CN were studied using alcohol dehydrogenase (ADH) as a substrate. To obtain an adequate relevant information about the chaperone capacities of studied caseins, three different physical parameters including chaperone constant (k_c, μM⁻¹), thermal aggregation constant (k_T, °C⁻¹) and aggregation rate constant (k_t, min⁻¹) were measured. Bovine β-CN displays greater chaperone activity than camel β-CN. Fluorescence studies of 8-anilino-1-naphthalenesulfonic acid (ANS) binding demonstrated that bovine β-CN is doted with larger effective hydrophobic surfaces at all studied temperatures than camel β-CN. Greater relative hydrophobicity of bovine β-CN than camel β-CN may be a factor responsible for stronger interactions of bovine β-CN with the aggregation-prone pre denatured molecular species of the substrate ADH, which resulted in greater chaperone activity of bovine β-CN.