The insertion of bioactive peptides at the C-terminal end of an 11S globulin changes the structural stability and improves the antihypertensive activity
Electron. j. biotechnol
;
37: 18-24, Jan. 2019. tab, ilus, graf
Article
Dans Anglais
| LILACS
| ID: biblio-1049076
ABSTRACT
BACKGROUND:
The 11S globulin from amaranth is the most abundant storage protein in mature seeds and is well recognized for its nutritional value. We used this globulin to engineer a new protein by adding a four valinetyrosine antihypertensive peptide at its C-terminal end to improve its functionality. The new protein was named AMR5 and expressed in the Escherichia coli BL21-CodonPlus(DE3)-RIL strain using a custom medium (F8PW) designed for this work.RESULTS:
The alternative medium allowed for the production of 652 mg/L expressed protein at the flask level, mostly in an insoluble form, and this protein was subjected to in vitro refolding. The spectrometric analysis suggests that the protein adopts a ß/α structure with a small increment of α-helix conformation relative to the native amaranth 11S globulin. Thermal and urea denaturation experiments determined apparent Tm and C1/2 values of 50.4°C and 3.04 M, respectively, thus indicating that the antihypertensive peptide insertion destabilized the modified protein relative to the native one. AMR5 hydrolyzed by trypsin and chymotrypsin showed 14- and 1.3-fold stronger inhibitory activity against angiotensin I-converting enzyme (IC50 of 0.034 mg/mL) than the unmodified protein and the previously reported amaranth acidic subunit modified with antihypertensive peptides, respectively.CONCLUSION:
The inserted peptide decreases the structural stability of amaranth 11S globulin and improves its antihypertensive activity.
Texte intégral:
Disponible
Indice:
LILAS (Amériques)
Sujet Principal:
Peptides
/
Protéines
/
Globulines
/
Antihypertenseurs
langue:
Anglais
Texte intégral:
Electron. j. biotechnol
Thème du journal:
Biotechnologie
Année:
2019
Type:
Article
Pays d'affiliation:
Mexique
Institution/Pays d'affiliation:
ENMyH-IPN/MX
/
Instituto Politécnico Nacional, CIBA-IPN/MX
/
UNAM/MX
/
Universidad de las Américas Puebla/MX
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