Research of the Interaction Between L-Arginine and Bovine Serum Albumin Aggregates
Date Issued
2009
Date
2009
Author(s)
Chen, Chih-Yuan
Abstract
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.
Subjects
amyloid fibril
BSA
L-arginine
reducing agent
aggregates
disulfide bond
Type
thesis
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