Peptidomic strategy for purification and identification of potential ACE-inhibitory and antioxidant peptides in Tetradesmus obliquus microalgae

Research output: Contribution to journalJournal articleResearchpeer-review

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Peptidomic strategy for purification and identification of potential ACE-inhibitory and antioxidant peptides in Tetradesmus obliquus microalgae. / Montone, Carmela Maria; Capriotti, Anna Laura; Cavaliere, Chiara; La Barbera, Giorgia; Piovesana, Susy; Zenezini Chiozzi, Riccardo; Laganà, Aldo.

In: Analytical and Bioanalytical Chemistry, Vol. 410, No. 15, 01.06.2018, p. 3573-3586.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Montone, CM, Capriotti, AL, Cavaliere, C, La Barbera, G, Piovesana, S, Zenezini Chiozzi, R & Laganà, A 2018, 'Peptidomic strategy for purification and identification of potential ACE-inhibitory and antioxidant peptides in Tetradesmus obliquus microalgae', Analytical and Bioanalytical Chemistry, vol. 410, no. 15, pp. 3573-3586. https://doi.org/10.1007/s00216-018-0925-x

APA

Montone, C. M., Capriotti, A. L., Cavaliere, C., La Barbera, G., Piovesana, S., Zenezini Chiozzi, R., & Laganà, A. (2018). Peptidomic strategy for purification and identification of potential ACE-inhibitory and antioxidant peptides in Tetradesmus obliquus microalgae. Analytical and Bioanalytical Chemistry, 410(15), 3573-3586. https://doi.org/10.1007/s00216-018-0925-x

Vancouver

Montone CM, Capriotti AL, Cavaliere C, La Barbera G, Piovesana S, Zenezini Chiozzi R et al. Peptidomic strategy for purification and identification of potential ACE-inhibitory and antioxidant peptides in Tetradesmus obliquus microalgae. Analytical and Bioanalytical Chemistry. 2018 Jun 1;410(15):3573-3586. https://doi.org/10.1007/s00216-018-0925-x

Author

Montone, Carmela Maria ; Capriotti, Anna Laura ; Cavaliere, Chiara ; La Barbera, Giorgia ; Piovesana, Susy ; Zenezini Chiozzi, Riccardo ; Laganà, Aldo. / Peptidomic strategy for purification and identification of potential ACE-inhibitory and antioxidant peptides in Tetradesmus obliquus microalgae. In: Analytical and Bioanalytical Chemistry. 2018 ; Vol. 410, No. 15. pp. 3573-3586.

Bibtex

@article{d8201ec4c29e44e69cb74b632a7f0546,
title = "Peptidomic strategy for purification and identification of potential ACE-inhibitory and antioxidant peptides in Tetradesmus obliquus microalgae",
abstract = "Microalgae are unicellular marine organisms that have promoted complex biochemical pathways to survive in greatly competitive marine environments. They could contain significant amounts of high-quality proteins which, because of their structural diversity, contain a range of yet undiscovered novel bioactive peptides. In this work, a peptidomic platform was developed for the separation and identification of bioactive peptides in protein hydrolysates. In this work, a peptidomic platform was developed for the extraction, separation, and identification of bioactive peptides in protein hydrolysates. Indeed, extraction of proteins from recalcitrant tissues is still a challenge due to their strong cell walls and high levels of non-protein interfering compounds. Therefore, seven different protein extraction protocols, based on mechanical and chemical methods, were tested in order to produce high-quality protein extracts. Proteins obtained by means of the best protocol, consisting of milling the recalcitrant tissue with glass beads, were subjected to enzymatic digestion with Alcalase{\circledR} and subsequently the hydrolysate was purified by two-dimensional semi-preparative reversed phase liquid chromatography. Fractions were assayed for antioxidant and antihypertensive activities and only the most active ones were finally analyzed by RP nanoHPLC-MS/MS. Around 500 peptide sequences were identified in these fractions. The identified peptides were subjected to an in silico analysis by PeptideRanker algorithm in order to assign a score of bioactivity probability. Twenty-five sequenced peptides were found with potential antioxidant and angiotensin-converting-enzyme-inhibitory activities. Four of these peptides, WPRGYFL, GPDRPKFLGPF, WYGPDRPKFL, SDWDRF, were selected for synthesis and in vitro tested for specific bioactivity, exhibiting good values of antioxidant and ACE-inhibitory activity. [Figure not available: see fulltext.].",
keywords = "ACE-inhibitory peptides, Antioxidant peptides, High resolution mass spectrometry, Microalgae, Off-line two-dimensional chromatography, Peptidomics, Protein extraction methods",
author = "Montone, {Carmela Maria} and Capriotti, {Anna Laura} and Chiara Cavaliere and {La Barbera}, Giorgia and Susy Piovesana and {Zenezini Chiozzi}, Riccardo and Aldo Lagan{\`a}",
year = "2018",
month = "6",
day = "1",
doi = "10.1007/s00216-018-0925-x",
language = "English",
volume = "410",
pages = "3573--3586",
journal = "Analytical and Bioanalytical Chemistry",
issn = "1618-2642",
publisher = "Springer",
number = "15",

}

RIS

TY - JOUR

T1 - Peptidomic strategy for purification and identification of potential ACE-inhibitory and antioxidant peptides in Tetradesmus obliquus microalgae

AU - Montone, Carmela Maria

AU - Capriotti, Anna Laura

AU - Cavaliere, Chiara

AU - La Barbera, Giorgia

AU - Piovesana, Susy

AU - Zenezini Chiozzi, Riccardo

AU - Laganà, Aldo

PY - 2018/6/1

Y1 - 2018/6/1

N2 - Microalgae are unicellular marine organisms that have promoted complex biochemical pathways to survive in greatly competitive marine environments. They could contain significant amounts of high-quality proteins which, because of their structural diversity, contain a range of yet undiscovered novel bioactive peptides. In this work, a peptidomic platform was developed for the separation and identification of bioactive peptides in protein hydrolysates. In this work, a peptidomic platform was developed for the extraction, separation, and identification of bioactive peptides in protein hydrolysates. Indeed, extraction of proteins from recalcitrant tissues is still a challenge due to their strong cell walls and high levels of non-protein interfering compounds. Therefore, seven different protein extraction protocols, based on mechanical and chemical methods, were tested in order to produce high-quality protein extracts. Proteins obtained by means of the best protocol, consisting of milling the recalcitrant tissue with glass beads, were subjected to enzymatic digestion with Alcalase® and subsequently the hydrolysate was purified by two-dimensional semi-preparative reversed phase liquid chromatography. Fractions were assayed for antioxidant and antihypertensive activities and only the most active ones were finally analyzed by RP nanoHPLC-MS/MS. Around 500 peptide sequences were identified in these fractions. The identified peptides were subjected to an in silico analysis by PeptideRanker algorithm in order to assign a score of bioactivity probability. Twenty-five sequenced peptides were found with potential antioxidant and angiotensin-converting-enzyme-inhibitory activities. Four of these peptides, WPRGYFL, GPDRPKFLGPF, WYGPDRPKFL, SDWDRF, were selected for synthesis and in vitro tested for specific bioactivity, exhibiting good values of antioxidant and ACE-inhibitory activity. [Figure not available: see fulltext.].

AB - Microalgae are unicellular marine organisms that have promoted complex biochemical pathways to survive in greatly competitive marine environments. They could contain significant amounts of high-quality proteins which, because of their structural diversity, contain a range of yet undiscovered novel bioactive peptides. In this work, a peptidomic platform was developed for the separation and identification of bioactive peptides in protein hydrolysates. In this work, a peptidomic platform was developed for the extraction, separation, and identification of bioactive peptides in protein hydrolysates. Indeed, extraction of proteins from recalcitrant tissues is still a challenge due to their strong cell walls and high levels of non-protein interfering compounds. Therefore, seven different protein extraction protocols, based on mechanical and chemical methods, were tested in order to produce high-quality protein extracts. Proteins obtained by means of the best protocol, consisting of milling the recalcitrant tissue with glass beads, were subjected to enzymatic digestion with Alcalase® and subsequently the hydrolysate was purified by two-dimensional semi-preparative reversed phase liquid chromatography. Fractions were assayed for antioxidant and antihypertensive activities and only the most active ones were finally analyzed by RP nanoHPLC-MS/MS. Around 500 peptide sequences were identified in these fractions. The identified peptides were subjected to an in silico analysis by PeptideRanker algorithm in order to assign a score of bioactivity probability. Twenty-five sequenced peptides were found with potential antioxidant and angiotensin-converting-enzyme-inhibitory activities. Four of these peptides, WPRGYFL, GPDRPKFLGPF, WYGPDRPKFL, SDWDRF, were selected for synthesis and in vitro tested for specific bioactivity, exhibiting good values of antioxidant and ACE-inhibitory activity. [Figure not available: see fulltext.].

KW - ACE-inhibitory peptides

KW - Antioxidant peptides

KW - High resolution mass spectrometry

KW - Microalgae

KW - Off-line two-dimensional chromatography

KW - Peptidomics

KW - Protein extraction methods

UR - http://www.scopus.com/inward/record.url?scp=85044957222&partnerID=8YFLogxK

U2 - 10.1007/s00216-018-0925-x

DO - 10.1007/s00216-018-0925-x

M3 - Journal article

C2 - 29476230

AN - SCOPUS:85044957222

VL - 410

SP - 3573

EP - 3586

JO - Analytical and Bioanalytical Chemistry

JF - Analytical and Bioanalytical Chemistry

SN - 1618-2642

IS - 15

ER -

ID: 231310912