Optimization of hydrolysis conditions, isolation, and identification of neuroprotective peptides derived from seahorse Hippocampus trimaculatus

Pangestuti, Ratih, Ryu, BoMi, Himaya, S. W. A. and Kim, Se-Kwon (2013) Optimization of hydrolysis conditions, isolation, and identification of neuroprotective peptides derived from seahorse Hippocampus trimaculatus. Amino Acids, 45 2: 369-381. doi:10.1007/s00726-013-1510-4


Author Pangestuti, Ratih
Ryu, BoMi
Himaya, S. W. A.
Kim, Se-Kwon
Title Optimization of hydrolysis conditions, isolation, and identification of neuroprotective peptides derived from seahorse Hippocampus trimaculatus
Formatted title
Optimization of hydrolysis conditions, isolation, and identification of neuroprotective peptides derived from seahorse Hippocampus trimaculatus
Journal name Amino Acids   Check publisher's open access policy
ISSN 0939-4451
1438-2199
Publication date 2013-08
Sub-type Article (original research)
DOI 10.1007/s00726-013-1510-4
Volume 45
Issue 2
Start page 369
End page 381
Total pages 13
Place of publication Vienna, Austria
Publisher Springer Wien
Collection year 2014
Language eng
Formatted abstract
Hippocampus trimaculatus is one of the most heavily traded seahorse species for traditional medicine purposes in many countries. In the present study, we showed neuroprotective effects of peptide derived from H. trimaculatus against amyloid-β42 (Aβ42) toxicity which are central to the pathogenesis of Alzheimer’s diseases (AD). Firstly, H. trimaculatus was separately hydrolyzed by four different enzymes and tested for their protective effect on Aβ42-induced neurotoxicity in differentiated PC12 cells. Pronase E hydrolysate exerted highest protection with cell viability value of 88.33 ± 3.33 %. Furthermore, we used response surface methodology to optimize pronase E hydrolysis conditions and found that temperature at 36.69 °C with the hydrolysis time 20.01 h, enzyme to substrate (E/S) ratio of 2.02 % and pH 7.34 were the most optimum conditions. Following several purification steps, H. trimaculatus-derived neuroprotective peptides (HTP-1) sequence was identified as Gly-Thr-Glu-Asp-Glu-Leu-Asp-Lys (906.4 Da). HTP-1 protected PC12 cells from Aβ42-induced neuronal death with the cell viability value of 85.52 ± 2.22 % and up-regulated pro-survival gene (Bcl-2) expressions. These results suggest that HTP-1 has the potential to be used in treatment of neurodegenerative diseases, particularly AD. Identification, characterization, and synthesis of bioactive components derived from H. trimaculatus have the potential to replace or at least complement the use of seahorse as traditional medicine, which further may become an approach to minimize seahorse exploitation in traditional medicine.
Keyword H. trimaculatus
A beta(42)
PC12
RSM
Pronase E
HTP-1
Response-surface methodology
Biochemical-composition
Growth-factor
Kuda Bleeker
Protein
Syngnathidae
Activation
Cells
beta
Aβ42
Aβ(42)
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2014 Collection
School of Pharmacy Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 6 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 5 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Sun, 01 Sep 2013, 00:11:00 EST by System User on behalf of School of Pharmacy