| dc.creator | Alba, Antonella | |
| dc.creator | Báez, Jessica | |
| dc.creator | Fernández Fernández, Adriana Maite | |
| dc.creator | Nardo, Agustina Estefanía | |
| dc.creator | Añón, María Cristina | |
| dc.creator | Medrano, Alejandra | |
| dc.creator | Paulino, Margot | |
| dc.date | 2022 | |
| dc.date | 2023-08-28T14:44:44Z | |
| dc.date.accessioned | 2024-07-24T03:44:51Z | |
| dc.date.available | 2024-07-24T03:44:51Z | |
| dc.identifier | http://sedici.unlp.edu.ar/handle/10915/156960 | |
| dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/9535031 | |
| dc.description | Alpha-lactalbumin is a whey protein that is a cheese-making industrial residue of high biological value. The antihypertensive capacity of three peptides obtained from the simulated gastrointestinal digestion of alpha-lactalbumin hydrolysates was studied. The alpha-lactalbumin hydrolysis was performed using the Alcalase enzyme and was subsequently subjected to a simulated digestion process using pepsin and pancreatin enzymes to mimic digestion conditions. The peptides were identified from a RP-HPLC fractionation of the digest and subsequent identification by mass spectrometry analysis. Three peptides from the alpha-lactalbumin sequence were obtained: IWCKDDQNPH (P1), KFLDDDLTDDIM (P2), and DKFLDDDLTDDIM (P3). The in vitro antihypertensive activity of the peptides was determined by studying the inhibition of the angiotensin-converting enzyme, with P1 being the only peptide with antihypertensive activity detected by this methodology (IC₅₀ = 3.91 ± 0.2 mg/mL). In order to correlate the structural (molecular dynamics simulations) and physicochemical properties with potential mechanisms of antihypertensive capacity, in silico methods were performed. The peptides P1, P2, and P3 had a negative global charge and were hydrophilic. After molecular modeling, the peptide structures were submitted to a refinement based on an energy minimization and further molecular dynamics simulation to assess their global size and conformational space. After a 50-nanosecond simulation, the global structures, solvated and immersed in an ionic water solution similar to that of blood, were studied in their solvent-accessible surfaces. A secondary structure (alpha-helix) was observed in the P1 peptide, but in general, all peptides showed an extended folding. The surfaces were charge code colored and in a visual inspection it could be conjectured that all of them exposed the charge, mainly a negative charge, to the solvent surface, in agreement with the GRAVY index, which was also evaluated. In conclusion, the structure and amino acid composition of peptide 1 assessed by in silico studies agrees with the antihypertensive activity obtained by the in vitro study. | |
| dc.description | Centro de Investigación y Desarrollo en Criotecnología de Alimentos | |
| dc.format | application/pdf | |
| dc.language | en | |
| dc.rights | http://creativecommons.org/licenses/by/4.0/ | |
| dc.rights | Creative Commons Attribution 4.0 International (CC BY 4.0) | |
| dc.subject | Ciencias Exactas | |
| dc.subject | Biología | |
| dc.subject | antihypertensive | |
| dc.subject | peptides | |
| dc.subject | molecular dynamics simulations | |
| dc.subject | simulated digestion | |
| dc.title | Study of the Antihypertensive Peptides Derived from Alpha-Lactalbumin Hydrolysate after Simulation of Digestion | |
| dc.type | Articulo | |
| dc.type | Articulo | |
