Unveiling antihypertensive and antimicrobial peptides from wine lees: Enzymatic hydrolysis, peptidomics profiling, virtual screening, functional characterization, and molecular doc...

Autores
Monasterio, Romina Paula; Iram, Daraksha; Knuf, Franziska; Caspers Weiffenbach, Rita; Fontana, Ariel Ramón
Año de publicación
2026
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Wine lees proteins hydrolysates obtained with alcalase, flavourzyme and protease either individually or in combination displayed varied degrees of angiotensin-converting enzyme inhibitory (ACEi) activity and growth inhibition of food-borne microorganisms. Peptidomics by nano-liquid chromatography-orbitrap tandem mass spectrometry together with virtual screening categorized the peptides according to their bioactivity. High proportion of positive charged peptides in protease hydrolysate associated with a higher growth inhibition activity against Escherichia coli. Prediction of ACEi-active di- and tri-motives encrypted within peptides with scores above 0.90 was performed by in silico simulated gastrointestinal digestion. The peptides released after digestion were predicted as non-toxic, highly soluble, having human intestinal absorption (HIA) and adequate bioavailabilities. Out of these 34 ACEi active sequences liberated, AF, AW, GF, GL, GW, PL, PM and VW showed positive HIA. The prediction of adsorption, digestion, metabolism, excretion and toxicity using physicochemical properties and Lipinski's rule-of-five exposed that the peptides were non-toxic and had desirable drug-like properties (flexibility, lipophilicity, molecular weight, gastrointestinal absorption, and bioavailability). Molecular docking revealed stronger ACEi potential for VW and AW compared to the other structures with binding energies lower than −8.0 kcal mol−1. Peptides inhibited ACE through hydrogen bonds, Van der Waals interactions and π–π stacking. Insights into the molecular interactions of ACEi peptides with physiological targets are presented, highlighting the potential of wine lees as a source of multifunctional peptides. Prospective multifunctional in vitro and in vivo effects of these sequences, and peptides containing them, need to be evaluated for understanding their potential therapeutic properties.
Fil: Monasterio, Romina Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Biología Agrícola de Mendoza. Universidad Nacional de Cuyo. Facultad de Ciencias Agrarias. Instituto de Biología Agrícola de Mendoza; Argentina
Fil: Iram, Daraksha. National Dairy Research Institute; India
Fil: Knuf, Franziska. Universitat Bonn; Alemania
Fil: Caspers Weiffenbach, Rita. Universitat Bonn; Alemania
Fil: Fontana, Ariel Ramón. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Biología Agrícola de Mendoza. Universidad Nacional de Cuyo. Facultad de Ciencias Agrarias. Instituto de Biología Agrícola de Mendoza; Argentina
Materia
FOOD INDUSTRY SIDE-STREAMS
CIRCULA BIOECONOMY
BIOINFORMATICS TOOLS
PEPTIDOMICS
ANGIOTENSIN I CONVERTIN ENZYME INHIBITORY ACTIVITY
MULTIFUNCTIONAL PEPTIDES
IN SILICO SIMULATED GASTROINTESTINAL DIGESTION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/287776
Acceder
id CONICETDig_5adf6c12e30820bdc58d1ebb8df9d012
oai_identifier_str oai:ri.conicet.gov.ar:11336/287776
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Unveiling antihypertensive and antimicrobial peptides from wine lees: Enzymatic hydrolysis, peptidomics profiling, virtual screening, functional characterization, and molecular dockingMonasterio, Romina PaulaIram, DarakshaKnuf, FranziskaCaspers Weiffenbach, RitaFontana, Ariel RamónFOOD INDUSTRY SIDE-STREAMSCIRCULA BIOECONOMYBIOINFORMATICS TOOLSPEPTIDOMICSANGIOTENSIN I CONVERTIN ENZYME INHIBITORY ACTIVITYMULTIFUNCTIONAL PEPTIDESIN SILICO SIMULATED GASTROINTESTINAL DIGESTIONhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Wine lees proteins hydrolysates obtained with alcalase, flavourzyme and protease either individually or in combination displayed varied degrees of angiotensin-converting enzyme inhibitory (ACEi) activity and growth inhibition of food-borne microorganisms. Peptidomics by nano-liquid chromatography-orbitrap tandem mass spectrometry together with virtual screening categorized the peptides according to their bioactivity. High proportion of positive charged peptides in protease hydrolysate associated with a higher growth inhibition activity against Escherichia coli. Prediction of ACEi-active di- and tri-motives encrypted within peptides with scores above 0.90 was performed by in silico simulated gastrointestinal digestion. The peptides released after digestion were predicted as non-toxic, highly soluble, having human intestinal absorption (HIA) and adequate bioavailabilities. Out of these 34 ACEi active sequences liberated, AF, AW, GF, GL, GW, PL, PM and VW showed positive HIA. The prediction of adsorption, digestion, metabolism, excretion and toxicity using physicochemical properties and Lipinski's rule-of-five exposed that the peptides were non-toxic and had desirable drug-like properties (flexibility, lipophilicity, molecular weight, gastrointestinal absorption, and bioavailability). Molecular docking revealed stronger ACEi potential for VW and AW compared to the other structures with binding energies lower than −8.0 kcal mol−1. Peptides inhibited ACE through hydrogen bonds, Van der Waals interactions and π–π stacking. Insights into the molecular interactions of ACEi peptides with physiological targets are presented, highlighting the potential of wine lees as a source of multifunctional peptides. Prospective multifunctional in vitro and in vivo effects of these sequences, and peptides containing them, need to be evaluated for understanding their potential therapeutic properties.Fil: Monasterio, Romina Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Biología Agrícola de Mendoza. Universidad Nacional de Cuyo. Facultad de Ciencias Agrarias. Instituto de Biología Agrícola de Mendoza; ArgentinaFil: Iram, Daraksha. National Dairy Research Institute; IndiaFil: Knuf, Franziska. Universitat Bonn; AlemaniaFil: Caspers Weiffenbach, Rita. Universitat Bonn; AlemaniaFil: Fontana, Ariel Ramón. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Biología Agrícola de Mendoza. Universidad Nacional de Cuyo. Facultad de Ciencias Agrarias. Instituto de Biología Agrícola de Mendoza; ArgentinaElsevier Science2026-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/287776Monasterio, Romina Paula; Iram, Daraksha; Knuf, Franziska; Caspers Weiffenbach, Rita; Fontana, Ariel Ramón; Unveiling antihypertensive and antimicrobial peptides from wine lees: Enzymatic hydrolysis, peptidomics profiling, virtual screening, functional characterization, and molecular docking; Elsevier Science; Food Research International; 229; 4-2026; 118462-1184620963-9969CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0963996926001365info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodres.2026.118462info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-08-25T14:40:30Zoai:ri.conicet.gov.ar:11336/287776instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982026-08-25 14:40:30.771CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Unveiling antihypertensive and antimicrobial peptides from wine lees: Enzymatic hydrolysis, peptidomics profiling, virtual screening, functional characterization, and molecular docking
title Unveiling antihypertensive and antimicrobial peptides from wine lees: Enzymatic hydrolysis, peptidomics profiling, virtual screening, functional characterization, and molecular docking
spellingShingle Unveiling antihypertensive and antimicrobial peptides from wine lees: Enzymatic hydrolysis, peptidomics profiling, virtual screening, functional characterization, and molecular docking
Monasterio, Romina Paula
FOOD INDUSTRY SIDE-STREAMS
CIRCULA BIOECONOMY
BIOINFORMATICS TOOLS
PEPTIDOMICS
ANGIOTENSIN I CONVERTIN ENZYME INHIBITORY ACTIVITY
MULTIFUNCTIONAL PEPTIDES
IN SILICO SIMULATED GASTROINTESTINAL DIGESTION
title_short Unveiling antihypertensive and antimicrobial peptides from wine lees: Enzymatic hydrolysis, peptidomics profiling, virtual screening, functional characterization, and molecular docking
title_full Unveiling antihypertensive and antimicrobial peptides from wine lees: Enzymatic hydrolysis, peptidomics profiling, virtual screening, functional characterization, and molecular docking
title_fullStr Unveiling antihypertensive and antimicrobial peptides from wine lees: Enzymatic hydrolysis, peptidomics profiling, virtual screening, functional characterization, and molecular docking
title_full_unstemmed Unveiling antihypertensive and antimicrobial peptides from wine lees: Enzymatic hydrolysis, peptidomics profiling, virtual screening, functional characterization, and molecular docking
title_sort Unveiling antihypertensive and antimicrobial peptides from wine lees: Enzymatic hydrolysis, peptidomics profiling, virtual screening, functional characterization, and molecular docking
dc.creator.none.fl_str_mv Monasterio, Romina Paula
Iram, Daraksha
Knuf, Franziska
Caspers Weiffenbach, Rita
Fontana, Ariel Ramón
author Monasterio, Romina Paula
author_facet Monasterio, Romina Paula
Iram, Daraksha
Knuf, Franziska
Caspers Weiffenbach, Rita
Fontana, Ariel Ramón
author_role author
author2 Iram, Daraksha
Knuf, Franziska
Caspers Weiffenbach, Rita
Fontana, Ariel Ramón
author2_role author
author
author
author
dc.subject.none.fl_str_mv FOOD INDUSTRY SIDE-STREAMS
CIRCULA BIOECONOMY
BIOINFORMATICS TOOLS
PEPTIDOMICS
ANGIOTENSIN I CONVERTIN ENZYME INHIBITORY ACTIVITY
MULTIFUNCTIONAL PEPTIDES
IN SILICO SIMULATED GASTROINTESTINAL DIGESTION
topic FOOD INDUSTRY SIDE-STREAMS
CIRCULA BIOECONOMY
BIOINFORMATICS TOOLS
PEPTIDOMICS
ANGIOTENSIN I CONVERTIN ENZYME INHIBITORY ACTIVITY
MULTIFUNCTIONAL PEPTIDES
IN SILICO SIMULATED GASTROINTESTINAL DIGESTION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Wine lees proteins hydrolysates obtained with alcalase, flavourzyme and protease either individually or in combination displayed varied degrees of angiotensin-converting enzyme inhibitory (ACEi) activity and growth inhibition of food-borne microorganisms. Peptidomics by nano-liquid chromatography-orbitrap tandem mass spectrometry together with virtual screening categorized the peptides according to their bioactivity. High proportion of positive charged peptides in protease hydrolysate associated with a higher growth inhibition activity against Escherichia coli. Prediction of ACEi-active di- and tri-motives encrypted within peptides with scores above 0.90 was performed by in silico simulated gastrointestinal digestion. The peptides released after digestion were predicted as non-toxic, highly soluble, having human intestinal absorption (HIA) and adequate bioavailabilities. Out of these 34 ACEi active sequences liberated, AF, AW, GF, GL, GW, PL, PM and VW showed positive HIA. The prediction of adsorption, digestion, metabolism, excretion and toxicity using physicochemical properties and Lipinski's rule-of-five exposed that the peptides were non-toxic and had desirable drug-like properties (flexibility, lipophilicity, molecular weight, gastrointestinal absorption, and bioavailability). Molecular docking revealed stronger ACEi potential for VW and AW compared to the other structures with binding energies lower than −8.0 kcal mol−1. Peptides inhibited ACE through hydrogen bonds, Van der Waals interactions and π–π stacking. Insights into the molecular interactions of ACEi peptides with physiological targets are presented, highlighting the potential of wine lees as a source of multifunctional peptides. Prospective multifunctional in vitro and in vivo effects of these sequences, and peptides containing them, need to be evaluated for understanding their potential therapeutic properties.
Fil: Monasterio, Romina Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Biología Agrícola de Mendoza. Universidad Nacional de Cuyo. Facultad de Ciencias Agrarias. Instituto de Biología Agrícola de Mendoza; Argentina
Fil: Iram, Daraksha. National Dairy Research Institute; India
Fil: Knuf, Franziska. Universitat Bonn; Alemania
Fil: Caspers Weiffenbach, Rita. Universitat Bonn; Alemania
Fil: Fontana, Ariel Ramón. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Biología Agrícola de Mendoza. Universidad Nacional de Cuyo. Facultad de Ciencias Agrarias. Instituto de Biología Agrícola de Mendoza; Argentina
description Wine lees proteins hydrolysates obtained with alcalase, flavourzyme and protease either individually or in combination displayed varied degrees of angiotensin-converting enzyme inhibitory (ACEi) activity and growth inhibition of food-borne microorganisms. Peptidomics by nano-liquid chromatography-orbitrap tandem mass spectrometry together with virtual screening categorized the peptides according to their bioactivity. High proportion of positive charged peptides in protease hydrolysate associated with a higher growth inhibition activity against Escherichia coli. Prediction of ACEi-active di- and tri-motives encrypted within peptides with scores above 0.90 was performed by in silico simulated gastrointestinal digestion. The peptides released after digestion were predicted as non-toxic, highly soluble, having human intestinal absorption (HIA) and adequate bioavailabilities. Out of these 34 ACEi active sequences liberated, AF, AW, GF, GL, GW, PL, PM and VW showed positive HIA. The prediction of adsorption, digestion, metabolism, excretion and toxicity using physicochemical properties and Lipinski's rule-of-five exposed that the peptides were non-toxic and had desirable drug-like properties (flexibility, lipophilicity, molecular weight, gastrointestinal absorption, and bioavailability). Molecular docking revealed stronger ACEi potential for VW and AW compared to the other structures with binding energies lower than −8.0 kcal mol−1. Peptides inhibited ACE through hydrogen bonds, Van der Waals interactions and π–π stacking. Insights into the molecular interactions of ACEi peptides with physiological targets are presented, highlighting the potential of wine lees as a source of multifunctional peptides. Prospective multifunctional in vitro and in vivo effects of these sequences, and peptides containing them, need to be evaluated for understanding their potential therapeutic properties.
publishDate 2026
dc.date.none.fl_str_mv 2026-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/287776
Monasterio, Romina Paula; Iram, Daraksha; Knuf, Franziska; Caspers Weiffenbach, Rita; Fontana, Ariel Ramón; Unveiling antihypertensive and antimicrobial peptides from wine lees: Enzymatic hydrolysis, peptidomics profiling, virtual screening, functional characterization, and molecular docking; Elsevier Science; Food Research International; 229; 4-2026; 118462-118462
0963-9969
CONICET Digital
CONICET
url http://hdl.handle.net/11336/287776
identifier_str_mv Monasterio, Romina Paula; Iram, Daraksha; Knuf, Franziska; Caspers Weiffenbach, Rita; Fontana, Ariel Ramón; Unveiling antihypertensive and antimicrobial peptides from wine lees: Enzymatic hydrolysis, peptidomics profiling, virtual screening, functional characterization, and molecular docking; Elsevier Science; Food Research International; 229; 4-2026; 118462-118462
0963-9969
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0963996926001365
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodres.2026.118462
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.24418

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