Back to Search Start Over

Insertion of antihypertensive peptides in acidic subunit from amaranth 11S induces contrasting effects in stability.

Authors :
Morales-Camacho JI
Espinosa-Hernández E
Fernández-Velasco DA
Benítez-Cardoza CG
Luna-Suárez S
Source :
Applied microbiology and biotechnology [Appl Microbiol Biotechnol] 2018 Nov; Vol. 102 (22), pp. 9595-9606. Date of Electronic Publication: 2018 Sep 12.
Publication Year :
2018

Abstract

The insertion of peptides is a biotechnology tool widely used to improve the nutraceutical properties of proteins. Because the effect of these insertions in protein stability and function is difficult to predict, it should be determined experimentally. In this study, we created two variants of amarantin acidic subunit and analyzed them along with other four proteins reported previously. We measured their response against two destabilizing agents: temperature and urea. The six proteins presented the insertion of antihypertensive peptides (VYVYVYVY or RIPP) in the variable regions of the protein. We observed that their effect strongly depended on the site of the insertion. The insertion in the variable region I stabilized the protein both thermally and chemically, but it affected the inhibitory activity of the angiotensin-converting enzyme in vitro. In contrast, insertions in other three regions were severely destabilizing, producing molten globules. Our findings reveal that the insertion of bioactive peptides in variable regions of a protein can increase or decrease the protein's thermal and chemical stability and that these conformational changes may also alter its final activity.

Details

Language :
English
ISSN :
1432-0614
Volume :
102
Issue :
22
Database :
MEDLINE
Journal :
Applied microbiology and biotechnology
Publication Type :
Academic Journal
Accession number :
30209550
Full Text :
https://doi.org/10.1007/s00253-018-9300-2