BIOPEP-PBIL Tool for the Analysis of the Structure of Biologically Active Motifs Derived from Food Proteins
This work describes a flexible technique for the analysis of protein sequences as a source of motifs affecting bodily functions. The BIOPEP database, along with the Pôle Bioinformatique Lyonnais (PBIL) server, were applied to define which activities of peptides dominated in their protein precursors...
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Format: | Article |
Language: | English |
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University of Zagreb Faculty of Food Technology and Biotechnology
2011-01-01
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Series: | Food Technology and Biotechnology |
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Online Access: | http://hrcak.srce.hr/file/98223 |
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author | Jerzy Dziuba Anna Iwaniak |
author_facet | Jerzy Dziuba Anna Iwaniak |
author_sort | Jerzy Dziuba |
collection | DOAJ |
description | This work describes a flexible technique for the analysis of protein sequences as a source of motifs affecting bodily functions. The BIOPEP database, along with the Pôle Bioinformatique Lyonnais (PBIL) server, were applied to define which activities of peptides dominated in their protein precursors and which structure of the protein contained the most of the revealed activities. Such an approach could be helpful in finding some structural requirements for peptide(s) to be regarded as biologically active (bioactive). It was found that apart from the activities of peptides that commonly occur in the majority of proteins (e.g. ACE inhibitors), all analyzed proteins can be a source of motifs involved in e.g. activation of ubiquitin-mediated proteolysis. This could be important in designing diets for patients who suffer from neural diseases. The structure and bioactivity analyses revealed that if peptides were to be 'bioactive', it is essential that they assume the position of a coil (or combination of coil and a-helix) in the sequence of their protein precursors. However, it is recommended to consider the factors such as the length of peptide chains, the number of peptides in the database as well as the repeatability of the occurrence of characteristic amino acids, both in the peptide and in the protein when studying the bioactivity and structure of biomolecules. |
first_indexed | 2024-03-09T09:14:28Z |
format | Article |
id | doaj.art-03c2b424d68f45b19ae06440ca5af711 |
institution | Directory Open Access Journal |
issn | 1330-9862 1334-2606 |
language | English |
last_indexed | 2024-03-09T09:14:28Z |
publishDate | 2011-01-01 |
publisher | University of Zagreb Faculty of Food Technology and Biotechnology |
record_format | Article |
series | Food Technology and Biotechnology |
spelling | doaj.art-03c2b424d68f45b19ae06440ca5af7112023-12-02T07:12:34ZengUniversity of Zagreb Faculty of Food Technology and BiotechnologyFood Technology and Biotechnology1330-98621334-26062011-01-01491118127BIOPEP-PBIL Tool for the Analysis of the Structure of Biologically Active Motifs Derived from Food ProteinsJerzy Dziuba0Anna Iwaniak1University of Warmia and Mazury in Olsztyn, Chair of Food Biochemistry, Pl. Cieszynski 1, PL-10-726 Olsztyn-Kortowo, PolandUniversity of Warmia and Mazury in Olsztyn, Chair of Food Biochemistry, Pl. Cieszynski 1, PL-10-726 Olsztyn-Kortowo, PolandThis work describes a flexible technique for the analysis of protein sequences as a source of motifs affecting bodily functions. The BIOPEP database, along with the Pôle Bioinformatique Lyonnais (PBIL) server, were applied to define which activities of peptides dominated in their protein precursors and which structure of the protein contained the most of the revealed activities. Such an approach could be helpful in finding some structural requirements for peptide(s) to be regarded as biologically active (bioactive). It was found that apart from the activities of peptides that commonly occur in the majority of proteins (e.g. ACE inhibitors), all analyzed proteins can be a source of motifs involved in e.g. activation of ubiquitin-mediated proteolysis. This could be important in designing diets for patients who suffer from neural diseases. The structure and bioactivity analyses revealed that if peptides were to be 'bioactive', it is essential that they assume the position of a coil (or combination of coil and a-helix) in the sequence of their protein precursors. However, it is recommended to consider the factors such as the length of peptide chains, the number of peptides in the database as well as the repeatability of the occurrence of characteristic amino acids, both in the peptide and in the protein when studying the bioactivity and structure of biomolecules.http://hrcak.srce.hr/file/98223databasesproteinsbioactive peptidesbioinformatics |
spellingShingle | Jerzy Dziuba Anna Iwaniak BIOPEP-PBIL Tool for the Analysis of the Structure of Biologically Active Motifs Derived from Food Proteins Food Technology and Biotechnology databases proteins bioactive peptides bioinformatics |
title | BIOPEP-PBIL Tool for the Analysis of the Structure of Biologically Active Motifs Derived from Food Proteins |
title_full | BIOPEP-PBIL Tool for the Analysis of the Structure of Biologically Active Motifs Derived from Food Proteins |
title_fullStr | BIOPEP-PBIL Tool for the Analysis of the Structure of Biologically Active Motifs Derived from Food Proteins |
title_full_unstemmed | BIOPEP-PBIL Tool for the Analysis of the Structure of Biologically Active Motifs Derived from Food Proteins |
title_short | BIOPEP-PBIL Tool for the Analysis of the Structure of Biologically Active Motifs Derived from Food Proteins |
title_sort | biopep pbil tool for the analysis of the structure of biologically active motifs derived from food proteins |
topic | databases proteins bioactive peptides bioinformatics |
url | http://hrcak.srce.hr/file/98223 |
work_keys_str_mv | AT jerzydziuba biopeppbiltoolfortheanalysisofthestructureofbiologicallyactivemotifsderivedfromfoodproteins AT annaiwaniak biopeppbiltoolfortheanalysisofthestructureofbiologicallyactivemotifsderivedfromfoodproteins |