Alonso Herreros-Isidro
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Alonso Herreros-Isidro has a total of 5 co-authors. Here are the top co-authors by number of shared publications:
- Elvira Marquez-Paradas
Department of Medical Biochemistry, Molecular Biology, and Immunology, School of Medicine, University of Seville, Av. Sanchez Pizjuan s/n, 41009 Seville, Spain
1 shared publication - Luna Barrera-Chamorro
Department of Medical Biochemistry, Molecular Biology, and Immunology, School of Medicine, University of Seville, 41009 Seville, Spain
1 shared publication - Maria Jose Leon
Department of Microbiology and Parasitology, School of Pharmacy, University of Seville, C. Profesor Garcia Gonzalez 2, 41012 Seville, Spain
1 shared publication - Sergio Montserrat-De la Paz
Department of Medical Biochemistry, Molecular Biology, and Immunology, School of Medicine, University of Seville, 41009 Seville, Spain
1 shared publication - Teresa Gonzalez-De la Rosa
Department of Medical Biochemistry, Molecular Biology, and Immunology, School of Medicine, University of Seville, Av. Sanchez Pizjuan s/n, 41009 Seville, Spain
1 shared publication
Latest Publications
- Open Access
Olive Leaf Protein Hydrolysate as a Novel Source of Antimicrobial Peptides: Peptidomic Characterization and In Silico Evaluation
Olive (Olea europaea) leaves, a by-product of olive oil production, represent a promising source of bioactive peptides. In this study, the peptidome of an olive leaf protein hydrolysate (OLPH) obtained via enzymatic hydrolysis with Alcalase was identified and analyzed for the first time. Liquid Chromatography coupled to Trapped Ion Mobility Spectrometry and Tandem Mass Spectrometry (LC-TIMS-MS/MS) analysis revealed over 7000 peptide sequences. Peptides with PeptideRanker scores above 0.79 were selected for in silico evaluation of antimicrobial potential, including physicochemical characterization and molecular docking. Several peptides—such as NYPAWGY, SSKGSLGGGF, QWDQGYF, and SGPAFNAGR—exhibited strong predicted antimicrobial potential, supported by favorable interactions with bacterial, viral, and fungal targets in docking simulations. Correlation analysis revealed that physicochemical features, such as net hydrogen, amphipathicity, and isoelectric point, were positively associated with predicted antimicrobial activity. These findings highlight the potential of olive leaf-derived peptides as natural antimicrobial agents and support the valorization of olive by-products as a sustainable source of functional ingredients for applications in food safety and health. Further experimental validation is needed to confirm the efficacy and mechanism of action of the identified peptides.
Open AccessOlive Leaf Protein Hydrolysate as a Novel Source of Antimicrobial Peptides: Peptidomic Characterization and In Silico Evaluation
Olive (Olea europaea) leaves, a by-product of olive oil production, represent a promising source of bioactive peptides. In this study, the peptidome of an olive leaf protein hydrolysate (OLPH) obtained via enzymatic hydrolysis with Alcalase was identified and analyzed for the first time. Liquid Chromatography coupled to Trapped Ion Mobility Spectrometry and Tandem Mass Spectrometry (LC-TIMS-MS/MS) analysis revealed over 7000 peptide sequences. Peptides with PeptideRanker scores above 0.79 were selected for in silico evaluation of antimicrobial potential, including physicochemical characterization and molecular docking. Several peptides—such as NYPAWGY, SSKGSLGGGF, QWDQGYF, and SGPAFNAGR—exhibited strong predicted antimicrobial potential, supported by favorable interactions with bacterial, viral, and fungal targets in docking simulations. Correlation analysis revealed that physicochemical features, such as net hydrogen, amphipathicity, and isoelectric point, were positively associated with predicted antimicrobial activity. These findings highlight the potential of olive leaf-derived peptides as natural antimicrobial agents and support the valorization of olive by-products as a sustainable source of functional ingredients for applications in food safety and health. Further experimental validation is needed to confirm the efficacy and mechanism of action of the identified peptides.