Cargando…
“Bottom-Up” Strategy for the Identification of Novel Soybean Peptides with Angiotensin-Converting Enzyme Inhibitory Activity
[Image: see text] IAVPTGVA (Soy1) and LPYP are two soybean peptides, which display a multifunctional behavior, showing in vitro hypocholesterolemic and hypoglycemic activities. A preliminary screening of their structures using BIOPEP suggested that they might be potential angiotensin-converting enzy...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2020
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7997397/ https://www.ncbi.nlm.nih.gov/pubmed/31984733 http://dx.doi.org/10.1021/acs.jafc.9b07361 |
_version_ | 1783670319498657792 |
---|---|
author | Dellafiora, Luca Pugliese, Raffaele Bollati, Carlotta Gelain, Fabrizio Galaverna, Gianni Arnoldi, Anna Lammi, Carmen |
author_facet | Dellafiora, Luca Pugliese, Raffaele Bollati, Carlotta Gelain, Fabrizio Galaverna, Gianni Arnoldi, Anna Lammi, Carmen |
author_sort | Dellafiora, Luca |
collection | PubMed |
description | [Image: see text] IAVPTGVA (Soy1) and LPYP are two soybean peptides, which display a multifunctional behavior, showing in vitro hypocholesterolemic and hypoglycemic activities. A preliminary screening of their structures using BIOPEP suggested that they might be potential angiotensin-converting enzyme (ACE) inhibitors. Therefore, a bottom-up-aided approach was developed in order to clarify the in vitro hypotensive activity. Soy1 and LPYP dropped the intestinal and renal ACE enzyme activity with IC(50) values equal to 14.7 ± 0.28 and 5.0 ± 0.28 μM (Caco-2 cells), and 6.0 ± 0.35 and 6.8 ± 0.20 μM (HK-2 cells), respectively. In parallel, a molecular modeling study suggested their capability to act as competitive inhibitors of this enzyme. Finally, in order to increase both their stability and hypotensive properties, a suitable strategy for the harmless control of their release from a nanomaterial was developed through their encapsulation into the RADA16-assembling peptide. |
format | Online Article Text |
id | pubmed-7997397 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-79973972021-03-29 “Bottom-Up” Strategy for the Identification of Novel Soybean Peptides with Angiotensin-Converting Enzyme Inhibitory Activity Dellafiora, Luca Pugliese, Raffaele Bollati, Carlotta Gelain, Fabrizio Galaverna, Gianni Arnoldi, Anna Lammi, Carmen J Agric Food Chem [Image: see text] IAVPTGVA (Soy1) and LPYP are two soybean peptides, which display a multifunctional behavior, showing in vitro hypocholesterolemic and hypoglycemic activities. A preliminary screening of their structures using BIOPEP suggested that they might be potential angiotensin-converting enzyme (ACE) inhibitors. Therefore, a bottom-up-aided approach was developed in order to clarify the in vitro hypotensive activity. Soy1 and LPYP dropped the intestinal and renal ACE enzyme activity with IC(50) values equal to 14.7 ± 0.28 and 5.0 ± 0.28 μM (Caco-2 cells), and 6.0 ± 0.35 and 6.8 ± 0.20 μM (HK-2 cells), respectively. In parallel, a molecular modeling study suggested their capability to act as competitive inhibitors of this enzyme. Finally, in order to increase both their stability and hypotensive properties, a suitable strategy for the harmless control of their release from a nanomaterial was developed through their encapsulation into the RADA16-assembling peptide. American Chemical Society 2020-01-27 2020-02-19 /pmc/articles/PMC7997397/ /pubmed/31984733 http://dx.doi.org/10.1021/acs.jafc.9b07361 Text en Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Dellafiora, Luca Pugliese, Raffaele Bollati, Carlotta Gelain, Fabrizio Galaverna, Gianni Arnoldi, Anna Lammi, Carmen “Bottom-Up” Strategy for the Identification of Novel Soybean Peptides with Angiotensin-Converting Enzyme Inhibitory Activity |
title | “Bottom-Up” Strategy for the Identification
of Novel Soybean Peptides with Angiotensin-Converting Enzyme Inhibitory
Activity |
title_full | “Bottom-Up” Strategy for the Identification
of Novel Soybean Peptides with Angiotensin-Converting Enzyme Inhibitory
Activity |
title_fullStr | “Bottom-Up” Strategy for the Identification
of Novel Soybean Peptides with Angiotensin-Converting Enzyme Inhibitory
Activity |
title_full_unstemmed | “Bottom-Up” Strategy for the Identification
of Novel Soybean Peptides with Angiotensin-Converting Enzyme Inhibitory
Activity |
title_short | “Bottom-Up” Strategy for the Identification
of Novel Soybean Peptides with Angiotensin-Converting Enzyme Inhibitory
Activity |
title_sort | “bottom-up” strategy for the identification
of novel soybean peptides with angiotensin-converting enzyme inhibitory
activity |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7997397/ https://www.ncbi.nlm.nih.gov/pubmed/31984733 http://dx.doi.org/10.1021/acs.jafc.9b07361 |
work_keys_str_mv | AT dellafioraluca bottomupstrategyfortheidentificationofnovelsoybeanpeptideswithangiotensinconvertingenzymeinhibitoryactivity AT puglieseraffaele bottomupstrategyfortheidentificationofnovelsoybeanpeptideswithangiotensinconvertingenzymeinhibitoryactivity AT bollaticarlotta bottomupstrategyfortheidentificationofnovelsoybeanpeptideswithangiotensinconvertingenzymeinhibitoryactivity AT gelainfabrizio bottomupstrategyfortheidentificationofnovelsoybeanpeptideswithangiotensinconvertingenzymeinhibitoryactivity AT galavernagianni bottomupstrategyfortheidentificationofnovelsoybeanpeptideswithangiotensinconvertingenzymeinhibitoryactivity AT arnoldianna bottomupstrategyfortheidentificationofnovelsoybeanpeptideswithangiotensinconvertingenzymeinhibitoryactivity AT lammicarmen bottomupstrategyfortheidentificationofnovelsoybeanpeptideswithangiotensinconvertingenzymeinhibitoryactivity |