Characterisation and Bioactivity Analysis of Peridinin-Chlorophyll a-Protein (PCP) Isolated from Symbiodinium tridacnidorum CS-73

Supasri, KM; Kumar, M; Segečová, A; McCauley, JI; Herdean, A; Padula, MP; O’Meara, T; Ralph, PJ

Characterisation and Bioactivity Analysis of Peridinin-Chlorophyll a-Protein (PCP) Isolated from Symbiodinium tridacnidorum CS-73

Supasri, KM Kumar, M

Segečová, A McCauley, JI Herdean, A

Padula, MP O’Meara, T Ralph, PJ

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Publisher:: MDPI AG
Publication Type:: Journal Article
Citation:: Journal of Marine Science and Engineering, 2021, 9, (12), pp. 1387
Issue Date:: 2021-12-06

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Field	Value	Language
dc.contributor.author	Supasri, KM
dc.contributor.author	Kumar, M https://orcid.org/0000-0002-5247-3059
dc.contributor.author	Segečová, A
dc.contributor.author	McCauley, JI
dc.contributor.author	Herdean, A https://orcid.org/0000-0003-2143-0213
dc.contributor.author	Padula, MP
dc.contributor.author	O’Meara, T
dc.contributor.author	Ralph, PJ
dc.date.accessioned	2022-01-10T01:59:23Z
dc.date.available	2022-01-10T01:59:23Z
dc.date.issued	2021-12-06
dc.identifier.citation	Journal of Marine Science and Engineering, 2021, 9, (12), pp. 1387
dc.identifier.issn	2077-1312
dc.identifier.issn	2077-1312
dc.identifier.uri	http://hdl.handle.net/10453/152861
dc.description.abstract	<jats:p>Peridinin-Chlorophyll a-Proteins (PCP) are the major light harvesting proteins in photosynthetic dinoflagellates. PCP shows great variation in protein length, pigment ratio, sequence, and spectroscopic properties. PCP conjugates (PerCP) are widely used as fluorescent probes for cellular and tissue analysis in the biomedical field. PCP consists of a peridinin carotenoid; thereby, it can potentially be used as a bioactive compound in pharmaceutical applications. However, the biological activities of PCP are yet to be explored. In this study, we extracted, purified, and partially characterised the PCP from Symbiodinium tridacnidorum (CS-73) and explored its antioxidant, anti-cancer and anti-inflammation bioactivities. The PCP was purified using an ÄKTA™ PURE system and predicted to be of 17.3 kDa molecular weight (confirmed as a single band on SDS-PAGE) with an isoelectric point (pI) 5.6. LC-MS/MS and bioinformatic analysis of purified PCP digested with trypsin indicated it was 164 amino acids long with >90% sequence similarity to PCP of SymA3.s6014_g3 (belonging to clade A of Symbiodinium sp.) confirmed with 59 peptide combinations matched across its protein sequence. The spectroscopic properties of purified PCP showed a slight shift in absorption and emission spectra to previously documented analysis in Symbiodinium species possibly due to variation in amino acid sequences that interact with chl a and peridinin. Purified PCP consisted of a 19-amino-acid-long signal peptide at its N terminal and nine helixes in its secondary structure, with several protein binding sites and no DNA/RNA binding site. Furthermore, purified PCP exhibited antioxidant and in vitro anti-inflammation bioactivities, and anti-cancer activities against human metastatic breast adenocarcinoma (MDA-MB-231) and human colorectal (HTC-15) cancer cell lines. Together, all these findings present PCP as a promising candidate for continued investigations for pharmaceutical applications to cure chronic diseases, apart from its existing application as a fluorescent-probe.</jats:p>
dc.language	en
dc.publisher	MDPI AG
dc.relation	http://purl.org/au-research/grants/arc/LP150100751
dc.relation.ispartof	Journal of Marine Science and Engineering
dc.relation.isbasedon	10.3390/jmse9121387
dc.rights	Copyright: © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https:// creativecommons.org/licenses/by/ 4.0/).
dc.rights	info:eu-repo/semantics/openAccess
dc.subject	0405 Oceanography, 0704 Fisheries Sciences, 0911 Maritime Engineering
dc.title	Characterisation and Bioactivity Analysis of Peridinin-Chlorophyll a-Protein (PCP) Isolated from Symbiodinium tridacnidorum CS-73
dc.type	Journal Article
utslib.citation.volume	9
utslib.for	0405 Oceanography
utslib.for	0704 Fisheries Sciences
utslib.for	0911 Maritime Engineering
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - C3 - Climate Change Cluster
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
utslib.copyright.status	open_access	*
dc.date.updated	2022-01-10T01:59:20Z
pubs.issue	12
pubs.publication-status	Published online
pubs.volume	9
utslib.citation.issue	12

Abstract:

Peridinin-Chlorophyll a-Proteins (PCP) are the major light harvesting proteins in photosynthetic dinoflagellates. PCP shows great variation in protein length, pigment ratio, sequence, and spectroscopic properties. PCP conjugates (PerCP) are widely used as fluorescent probes for cellular and tissue analysis in the biomedical field. PCP consists of a peridinin carotenoid; thereby, it can potentially be used as a bioactive compound in pharmaceutical applications. However, the biological activities of PCP are yet to be explored. In this study, we extracted, purified, and partially characterised the PCP from Symbiodinium tridacnidorum (CS-73) and explored its antioxidant, anti-cancer and anti-inflammation bioactivities. The PCP was purified using an ÄKTA™ PURE system and predicted to be of 17.3 kDa molecular weight (confirmed as a single band on SDS-PAGE) with an isoelectric point (pI) 5.6. LC-MS/MS and bioinformatic analysis of purified PCP digested with trypsin indicated it was 164 amino acids long with >90% sequence similarity to PCP of SymA3.s6014_g3 (belonging to clade A of Symbiodinium sp.) confirmed with 59 peptide combinations matched across its protein sequence. The spectroscopic properties of purified PCP showed a slight shift in absorption and emission spectra to previously documented analysis in Symbiodinium species possibly due to variation in amino acid sequences that interact with chl a and peridinin. Purified PCP consisted of a 19-amino-acid-long signal peptide at its N terminal and nine helixes in its secondary structure, with several protein binding sites and no DNA/RNA binding site. Furthermore, purified PCP exhibited antioxidant and in vitro anti-inflammation bioactivities, and anti-cancer activities against human metastatic breast adenocarcinoma (MDA-MB-231) and human colorectal (HTC-15) cancer cell lines. Together, all these findings present PCP as a promising candidate for continued investigations for pharmaceutical applications to cure chronic diseases, apart from its existing application as a fluorescent-probe.

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http://hdl.handle.net/10453/152861