TY - JOUR
T1 - Insertion of antihypertensive peptides in acidic subunit from amaranth 11S induces contrasting effects in stability
AU - Morales-Camacho, Jocksan I.
AU - Espinosa-Hernández, Edgar
AU - Fernández-Velasco, D. Alejandro
AU - Benítez-Cardoza, Claudia G.
AU - Luna-Suárez, Silvia
N1 - Publisher Copyright:
© 2018, Springer-Verlag GmbH Germany, part of Springer Nature.
PY - 2018/11/1
Y1 - 2018/11/1
N2 - 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.
AB - 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.
KW - Globulin 11S
KW - Protein engineering
KW - Protein expression
KW - Protein stability
KW - Tm
UR - http://www.scopus.com/inward/record.url?scp=85053534956&partnerID=8YFLogxK
U2 - 10.1007/s00253-018-9300-2
DO - 10.1007/s00253-018-9300-2
M3 - Artículo
C2 - 30209550
SN - 0175-7598
VL - 102
SP - 9595
EP - 9606
JO - Applied Microbiology and Biotechnology
JF - Applied Microbiology and Biotechnology
IS - 22
ER -