Please use this identifier to cite or link to this item:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/43148
Title: | 研究精胺酸與牛血清蛋白的聚集體之交互作用 Research of the Interaction Between L-Arginine and Bovine Serum Albumin Aggregates |
Authors: | Chih-Yuan Chen 陳志遠 |
Advisor: | 王勝仕(Sheng-Shih Wang) |
Keyword: | 類澱粉纖維,牛血清蛋白,精胺酸,還原劑,聚集體,雙硫鍵,TCEP, amyloid fibril,BSA,L-arginine,reducing agent,aggregates,disulfide bond,TCEP, |
Publication Year : | 2009 |
Degree: | 碩士 |
Abstract: | 精胺酸(L-arginine, L-Arg)為人體內二十種胺基酸之ㄧ,被證實可被用來抑制蛋白質的聚集體。然而,精胺酸對於抑制蛋白質聚集的機制與路徑仍未被了解。此論文中,主要是探討精胺酸對於牛血清蛋白形成聚集體之影響。蛋白質的聚集體大致可分為兩種:不規則性(amorphous)與規則性(amyloid fibril)聚集體。研究發現,精胺酸對於牛血清蛋白的不規則性之聚集體有抑制效果,但對於牛血清蛋白形成之類澱粉纖維卻沒有抑制的效果。探討牛血清蛋白形成類澱粉纖維之作用力,發現精胺酸與牛血清蛋白間有疏水性作用力存在,但卻無法阻止類澱粉纖維形成,只能減緩類澱粉纖維生成之速率;而當牛血清蛋白形成類澱粉纖維的過程中存在三(2-氯乙基)磷酸酯 (TCEP),則有抑制之效果。由此可知,牛血清蛋白應該主要是藉著雙硫鍵形成類澱粉纖維。在某些研究提到,精胺酸對於特定幾種蛋白質的類澱粉纖維有抑制之效果,而這些蛋白質的共通點都是類澱粉纖維主要是藉著疏水或氫鍵作用力而形成。因此,可推測精胺酸只能抑制藉由疏水或氫鍵作用力形成之類澱粉纖維,而無法抑制藉由雙硫鍵形成之類澱粉纖維。 L-arginine (L-Arg) which is one of the twenty amino acids in vivo has been demonstrated to exhibit an inhibitory effect against protein aggregation. However, the pathways and mechanism of the aggregate suppression by L-Arg remain largely unknown. In this research, attempts were directed toward examining the influence of L-Arg on the aggregated species of bovine serum albumin (BSA). The BSA aggregates can be generally divided into two groups: disordered (amorphous) and ordered (amyloid fibril) aggregates. We first explored how BSA was converted into amyloid fibril and then found that hydrophobic interaction exists between BSA and L-Arg. Furthermore, our data revealed that L-Arg could inhibit the formation of disordered BSA aggregate but not prevent amyloid fibril. Besides, the addition of reducing agent TCEP led to an inhibition of BSA amyloid fibrils, suggestive of the key role of disulfide bonds in forming BSA amyloid fibrils. Findings from previous studies indicated that L-Arg possesses an inhibitory potency against the formation of amyloid fibrils which is mainly governed by the hydrophobic interaction or hydrogen bonding. Therefore, along with our results, we can conjecture that L-Arg probably can not inhibit the amyloid fibrillation associated with disulfide bonds. |
URI: | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/43148 |
Fulltext Rights: | 有償授權 |
Appears in Collections: | 化學工程學系 |
Files in This Item:
File | Size | Format | |
---|---|---|---|
ntu-98-1.pdf Restricted Access | 18.78 MB | Adobe PDF |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.