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Modeling of the Relationship between Dipeptide Structure and Dipeptide Stability, Permeability, and ACE Inhibitory Activity
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| Zeitschriftentitel: | Journal of Food Science |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | Journal of Food Science, 74, 2009, 7 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
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| Schlagwörter: |
| author_facet |
Foltz, Martin Van Buren, Leo Klaffke, Werner Duchateau, Guus S.M.J.E. Foltz, Martin Van Buren, Leo Klaffke, Werner Duchateau, Guus S.M.J.E. |
|---|---|
| author |
Foltz, Martin Van Buren, Leo Klaffke, Werner Duchateau, Guus S.M.J.E. |
| spellingShingle |
Foltz, Martin Van Buren, Leo Klaffke, Werner Duchateau, Guus S.M.J.E. Journal of Food Science Modeling of the Relationship between Dipeptide Structure and Dipeptide Stability, Permeability, and ACE Inhibitory Activity Food Science |
| author_sort |
foltz, martin |
| spelling |
Foltz, Martin Van Buren, Leo Klaffke, Werner Duchateau, Guus S.M.J.E. 0022-1147 1750-3841 Wiley Food Science http://dx.doi.org/10.1111/j.1750-3841.2009.01301.x <jats:p><jats:bold>ABSTRACT: </jats:bold> Selected di‐ and tripeptides exhibit angiotensin‐I converting enzyme (ACE) inhibitory activity <jats:italic>in vitro</jats:italic>. However, the efficacy <jats:italic>in vivo</jats:italic> is most likely limited for most peptides due to low bioavailability. The purpose of this study was to identify descriptors of intestinal stability, permeability, and ACE inhibitory activity of dipeptides. A total of 228 dipeptides were synthesized; intestinal stability was obtained by <jats:italic>in vitro</jats:italic> digestion, intestinal permeability using Caco‐2 cells and ACE inhibitory activity by an <jats:italic>in vitro</jats:italic> assay. Databases were constructed to study the relationship between structure and activity, permeability, and stability. Quantitative structure–activity relationship (QSAR) modeling was performed based on computed models using partial least squares regression based on 400 molecular descriptors. QSAR modeling of dipeptide stability revealed high correlation coefficients (<jats:italic>R</jats:italic> > 0.65) for models based on <jats:italic>Z</jats:italic> and <jats:italic>X</jats:italic> scales. However, amino acid (AA) clustering showed the best results in describing stability of dipeptides. The N‐terminal AA residues Asp, Gly, and Pro as well as the C‐terminal residues Pro, Ser, Thr, and Asp stabilize dipeptides toward luminal enzymatic peptide hydrolysis. QSAR modeling did not reveal significant correlation models for intestinal permeability. 2D‐fingerprint models were identified describing ACE inhibitory activity of dipeptides. The intestinal stability of 12 peptides was predicted. Peptides were synthesized and stability was confirmed in simulated digestion experiments. Based on the results, specific dipeptides can be designed to meet both stability and activity criteria. However, postabsorptive ACE inhibitory activities of dipeptides <jats:italic>in vivo</jats:italic> are most likely limited due to the very low intestinal permeability of dipeptides.</jats:p> Modeling of the Relationship between Dipeptide Structure and Dipeptide Stability, Permeability, and ACE Inhibitory Activity Journal of Food Science |
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10.1111/j.1750-3841.2009.01301.x |
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| title |
Modeling of the Relationship between Dipeptide Structure and Dipeptide Stability, Permeability, and ACE Inhibitory Activity |
| title_unstemmed |
Modeling of the Relationship between Dipeptide Structure and Dipeptide Stability, Permeability, and ACE Inhibitory Activity |
| title_full |
Modeling of the Relationship between Dipeptide Structure and Dipeptide Stability, Permeability, and ACE Inhibitory Activity |
| title_fullStr |
Modeling of the Relationship between Dipeptide Structure and Dipeptide Stability, Permeability, and ACE Inhibitory Activity |
| title_full_unstemmed |
Modeling of the Relationship between Dipeptide Structure and Dipeptide Stability, Permeability, and ACE Inhibitory Activity |
| title_short |
Modeling of the Relationship between Dipeptide Structure and Dipeptide Stability, Permeability, and ACE Inhibitory Activity |
| title_sort |
modeling of the relationship between dipeptide structure and dipeptide stability, permeability, and ace inhibitory activity |
| topic |
Food Science |
| url |
http://dx.doi.org/10.1111/j.1750-3841.2009.01301.x |
| publishDate |
2009 |
| physical |
|
| description |
<jats:p><jats:bold>ABSTRACT: </jats:bold> Selected di‐ and tripeptides exhibit angiotensin‐I converting enzyme (ACE) inhibitory activity <jats:italic>in vitro</jats:italic>. However, the efficacy <jats:italic>in vivo</jats:italic> is most likely limited for most peptides due to low bioavailability. The purpose of this study was to identify descriptors of intestinal stability, permeability, and ACE inhibitory activity of dipeptides. A total of 228 dipeptides were synthesized; intestinal stability was obtained by <jats:italic>in vitro</jats:italic> digestion, intestinal permeability using Caco‐2 cells and ACE inhibitory activity by an <jats:italic>in vitro</jats:italic> assay. Databases were constructed to study the relationship between structure and activity, permeability, and stability. Quantitative structure–activity relationship (QSAR) modeling was performed based on computed models using partial least squares regression based on 400 molecular descriptors. QSAR modeling of dipeptide stability revealed high correlation coefficients (<jats:italic>R</jats:italic> > 0.65) for models based on <jats:italic>Z</jats:italic> and <jats:italic>X</jats:italic> scales. However, amino acid (AA) clustering showed the best results in describing stability of dipeptides. The N‐terminal AA residues Asp, Gly, and Pro as well as the C‐terminal residues Pro, Ser, Thr, and Asp stabilize dipeptides toward luminal enzymatic peptide hydrolysis. QSAR modeling did not reveal significant correlation models for intestinal permeability. 2D‐fingerprint models were identified describing ACE inhibitory activity of dipeptides. The intestinal stability of 12 peptides was predicted. Peptides were synthesized and stability was confirmed in simulated digestion experiments. Based on the results, specific dipeptides can be designed to meet both stability and activity criteria. However, postabsorptive ACE inhibitory activities of dipeptides <jats:italic>in vivo</jats:italic> are most likely limited due to the very low intestinal permeability of dipeptides.</jats:p> |
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| author | Foltz, Martin, Van Buren, Leo, Klaffke, Werner, Duchateau, Guus S.M.J.E. |
| author_facet | Foltz, Martin, Van Buren, Leo, Klaffke, Werner, Duchateau, Guus S.M.J.E., Foltz, Martin, Van Buren, Leo, Klaffke, Werner, Duchateau, Guus S.M.J.E. |
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| description | <jats:p><jats:bold>ABSTRACT: </jats:bold> Selected di‐ and tripeptides exhibit angiotensin‐I converting enzyme (ACE) inhibitory activity <jats:italic>in vitro</jats:italic>. However, the efficacy <jats:italic>in vivo</jats:italic> is most likely limited for most peptides due to low bioavailability. The purpose of this study was to identify descriptors of intestinal stability, permeability, and ACE inhibitory activity of dipeptides. A total of 228 dipeptides were synthesized; intestinal stability was obtained by <jats:italic>in vitro</jats:italic> digestion, intestinal permeability using Caco‐2 cells and ACE inhibitory activity by an <jats:italic>in vitro</jats:italic> assay. Databases were constructed to study the relationship between structure and activity, permeability, and stability. Quantitative structure–activity relationship (QSAR) modeling was performed based on computed models using partial least squares regression based on 400 molecular descriptors. QSAR modeling of dipeptide stability revealed high correlation coefficients (<jats:italic>R</jats:italic> > 0.65) for models based on <jats:italic>Z</jats:italic> and <jats:italic>X</jats:italic> scales. However, amino acid (AA) clustering showed the best results in describing stability of dipeptides. The N‐terminal AA residues Asp, Gly, and Pro as well as the C‐terminal residues Pro, Ser, Thr, and Asp stabilize dipeptides toward luminal enzymatic peptide hydrolysis. QSAR modeling did not reveal significant correlation models for intestinal permeability. 2D‐fingerprint models were identified describing ACE inhibitory activity of dipeptides. The intestinal stability of 12 peptides was predicted. Peptides were synthesized and stability was confirmed in simulated digestion experiments. Based on the results, specific dipeptides can be designed to meet both stability and activity criteria. However, postabsorptive ACE inhibitory activities of dipeptides <jats:italic>in vivo</jats:italic> are most likely limited due to the very low intestinal permeability of dipeptides.</jats:p> |
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| spelling | Foltz, Martin Van Buren, Leo Klaffke, Werner Duchateau, Guus S.M.J.E. 0022-1147 1750-3841 Wiley Food Science http://dx.doi.org/10.1111/j.1750-3841.2009.01301.x <jats:p><jats:bold>ABSTRACT: </jats:bold> Selected di‐ and tripeptides exhibit angiotensin‐I converting enzyme (ACE) inhibitory activity <jats:italic>in vitro</jats:italic>. However, the efficacy <jats:italic>in vivo</jats:italic> is most likely limited for most peptides due to low bioavailability. The purpose of this study was to identify descriptors of intestinal stability, permeability, and ACE inhibitory activity of dipeptides. A total of 228 dipeptides were synthesized; intestinal stability was obtained by <jats:italic>in vitro</jats:italic> digestion, intestinal permeability using Caco‐2 cells and ACE inhibitory activity by an <jats:italic>in vitro</jats:italic> assay. Databases were constructed to study the relationship between structure and activity, permeability, and stability. Quantitative structure–activity relationship (QSAR) modeling was performed based on computed models using partial least squares regression based on 400 molecular descriptors. QSAR modeling of dipeptide stability revealed high correlation coefficients (<jats:italic>R</jats:italic> > 0.65) for models based on <jats:italic>Z</jats:italic> and <jats:italic>X</jats:italic> scales. However, amino acid (AA) clustering showed the best results in describing stability of dipeptides. The N‐terminal AA residues Asp, Gly, and Pro as well as the C‐terminal residues Pro, Ser, Thr, and Asp stabilize dipeptides toward luminal enzymatic peptide hydrolysis. QSAR modeling did not reveal significant correlation models for intestinal permeability. 2D‐fingerprint models were identified describing ACE inhibitory activity of dipeptides. The intestinal stability of 12 peptides was predicted. Peptides were synthesized and stability was confirmed in simulated digestion experiments. Based on the results, specific dipeptides can be designed to meet both stability and activity criteria. However, postabsorptive ACE inhibitory activities of dipeptides <jats:italic>in vivo</jats:italic> are most likely limited due to the very low intestinal permeability of dipeptides.</jats:p> Modeling of the Relationship between Dipeptide Structure and Dipeptide Stability, Permeability, and ACE Inhibitory Activity Journal of Food Science |
| spellingShingle | Foltz, Martin, Van Buren, Leo, Klaffke, Werner, Duchateau, Guus S.M.J.E., Journal of Food Science, Modeling of the Relationship between Dipeptide Structure and Dipeptide Stability, Permeability, and ACE Inhibitory Activity, Food Science |
| title | Modeling of the Relationship between Dipeptide Structure and Dipeptide Stability, Permeability, and ACE Inhibitory Activity |
| title_full | Modeling of the Relationship between Dipeptide Structure and Dipeptide Stability, Permeability, and ACE Inhibitory Activity |
| title_fullStr | Modeling of the Relationship between Dipeptide Structure and Dipeptide Stability, Permeability, and ACE Inhibitory Activity |
| title_full_unstemmed | Modeling of the Relationship between Dipeptide Structure and Dipeptide Stability, Permeability, and ACE Inhibitory Activity |
| title_short | Modeling of the Relationship between Dipeptide Structure and Dipeptide Stability, Permeability, and ACE Inhibitory Activity |
| title_sort | modeling of the relationship between dipeptide structure and dipeptide stability, permeability, and ace inhibitory activity |
| title_unstemmed | Modeling of the Relationship between Dipeptide Structure and Dipeptide Stability, Permeability, and ACE Inhibitory Activity |
| topic | Food Science |
| url | http://dx.doi.org/10.1111/j.1750-3841.2009.01301.x |