Antibacterial Peptides from Tryptic Hydrolysate of Ricinus communis Seed Protein Fractionated Using Cation Exchange Chromatography

Antimicrobial peptide (AMP) peptide-based lead compound has become interesting target in developing new antibiotics. AMP is possibly generated through the digestion of protein. The protein of castor (Ricinus communis) seed is characterized as a ribosome-inactivating protein (RIP) that can be a sourc...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Tri Raharjo, Woro Utami, Atdrian Fajr, Winarto Haryadi, Respati Swasono
Formato:	article
Lenguaje:	EN
Publicado:	Universitas Gadjah Mada 2021
Materias:	peptides; antimicrobial; ricinus communis; sds extract; protein; hrms Pharmacy and materia medica RS1-441
Acceso en línea:	https://doaj.org/article/d4e566c5935643c48afa70f46ee53b9b
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:d4e566c5935643c48afa70f46ee53b9b
record_format	dspace
spelling	oai:doaj.org-article:d4e566c5935643c48afa70f46ee53b9b2021-11-15T06:08:47ZAntibacterial Peptides from Tryptic Hydrolysate of Ricinus communis Seed Protein Fractionated Using Cation Exchange Chromatography2338-94272338-948610.22146/ijp.1260https://doaj.org/article/d4e566c5935643c48afa70f46ee53b9b2021-03-01T00:00:00Zhttps://jurnal.ugm.ac.id/v3/IJP/article/view/1260https://doaj.org/toc/2338-9427https://doaj.org/toc/2338-9486Antimicrobial peptide (AMP) peptide-based lead compound has become interesting target in developing new antibiotics. AMP is possibly generated through the digestion of protein. The protein of castor (Ricinus communis) seed is characterized as a ribosome-inactivating protein (RIP) that can be a source of AMP. The objectives of this research are to identify antibacterial peptides from Ricinus communis seed protein hydrolysate. The seed protein was isolated using sodium dodecyl sulfate and subsequently digested using trypsin. The hydrolysate was fractionated using a strong cation exchange chromatography system, and the resulting fractions were tested for antibacterial activity. The peptides present in the active fraction were identified using high-resolution mass spectrometry. As the result, the pH 4 and pH 5 fractions of the elution buffer indicated antibacterial activity, with the pH 4 fraction of the hydrolysate having high activity against both gram-negative (Escherichia coli) and gram-positive (Staphylococcus aureus) bacteria. Three peptides that have the sequences EESETVGQR, GQSTGTGQQER, and LDALEPDNR could be responsible for the activity of the pH 4 fraction. The antibacterial activity of these peptides, which is due to their ionic properties and secondary structure, supports the disruption of the bacterial cell membrane. It can be concluded that Ricinus communis seed protein hydrolysate contains peptides with sequence EESETVGQR, GQSTGTGQQER, and LDALEPDNR that potent to be used as AMP lead compoundsTri RaharjoWoro UtamiAtdrian FajrWinarto HaryadiRespati SwasonoUniversitas Gadjah Madaarticlepeptides; antimicrobial; ricinus communis; sds extract; protein; hrmsPharmacy and materia medicaRS1-441ENIndonesian Journal of Pharmacy, Pp 74-85 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	peptides; antimicrobial; ricinus communis; sds extract; protein; hrms Pharmacy and materia medica RS1-441
spellingShingle	peptides; antimicrobial; ricinus communis; sds extract; protein; hrms Pharmacy and materia medica RS1-441 Tri Raharjo Woro Utami Atdrian Fajr Winarto Haryadi Respati Swasono Antibacterial Peptides from Tryptic Hydrolysate of Ricinus communis Seed Protein Fractionated Using Cation Exchange Chromatography
description	Antimicrobial peptide (AMP) peptide-based lead compound has become interesting target in developing new antibiotics. AMP is possibly generated through the digestion of protein. The protein of castor (Ricinus communis) seed is characterized as a ribosome-inactivating protein (RIP) that can be a source of AMP. The objectives of this research are to identify antibacterial peptides from Ricinus communis seed protein hydrolysate. The seed protein was isolated using sodium dodecyl sulfate and subsequently digested using trypsin. The hydrolysate was fractionated using a strong cation exchange chromatography system, and the resulting fractions were tested for antibacterial activity. The peptides present in the active fraction were identified using high-resolution mass spectrometry. As the result, the pH 4 and pH 5 fractions of the elution buffer indicated antibacterial activity, with the pH 4 fraction of the hydrolysate having high activity against both gram-negative (Escherichia coli) and gram-positive (Staphylococcus aureus) bacteria. Three peptides that have the sequences EESETVGQR, GQSTGTGQQER, and LDALEPDNR could be responsible for the activity of the pH 4 fraction. The antibacterial activity of these peptides, which is due to their ionic properties and secondary structure, supports the disruption of the bacterial cell membrane. It can be concluded that Ricinus communis seed protein hydrolysate contains peptides with sequence EESETVGQR, GQSTGTGQQER, and LDALEPDNR that potent to be used as AMP lead compounds
format	article
author	Tri Raharjo Woro Utami Atdrian Fajr Winarto Haryadi Respati Swasono
author_facet	Tri Raharjo Woro Utami Atdrian Fajr Winarto Haryadi Respati Swasono
author_sort	Tri Raharjo
title	Antibacterial Peptides from Tryptic Hydrolysate of Ricinus communis Seed Protein Fractionated Using Cation Exchange Chromatography
title_short	Antibacterial Peptides from Tryptic Hydrolysate of Ricinus communis Seed Protein Fractionated Using Cation Exchange Chromatography
title_full	Antibacterial Peptides from Tryptic Hydrolysate of Ricinus communis Seed Protein Fractionated Using Cation Exchange Chromatography
title_fullStr	Antibacterial Peptides from Tryptic Hydrolysate of Ricinus communis Seed Protein Fractionated Using Cation Exchange Chromatography
title_full_unstemmed	Antibacterial Peptides from Tryptic Hydrolysate of Ricinus communis Seed Protein Fractionated Using Cation Exchange Chromatography
title_sort	antibacterial peptides from tryptic hydrolysate of ricinus communis seed protein fractionated using cation exchange chromatography
publisher	Universitas Gadjah Mada
publishDate	2021
url	https://doaj.org/article/d4e566c5935643c48afa70f46ee53b9b
work_keys_str_mv	AT triraharjo antibacterialpeptidesfromtryptichydrolysateofricinuscommunisseedproteinfractionatedusingcationexchangechromatography AT woroutami antibacterialpeptidesfromtryptichydrolysateofricinuscommunisseedproteinfractionatedusingcationexchangechromatography AT atdrianfajr antibacterialpeptidesfromtryptichydrolysateofricinuscommunisseedproteinfractionatedusingcationexchangechromatography AT winartoharyadi antibacterialpeptidesfromtryptichydrolysateofricinuscommunisseedproteinfractionatedusingcationexchangechromatography AT respatiswasono antibacterialpeptidesfromtryptichydrolysateofricinuscommunisseedproteinfractionatedusingcationexchangechromatography
_version_	1718428585071476736

Antibacterial Peptides from Tryptic Hydrolysate of Ricinus communis Seed Protein Fractionated Using Cation Exchange Chromatography

Ejemplares similares