[HTML][HTML] The insertion of bioactive peptides at the C-terminal end of an 11S globulin changes the structural stability and improves the antihypertensive activity
E Espinosa-Hernández, JI Morales-Camacho… - Electronic Journal of …, 2019 - Elsevier
E Espinosa-Hernández, JI Morales-Camacho, DA Fernández-Velasco, CG Benítez-Cardoza…
Electronic Journal of Biotechnology, 2019•ElsevierBackground 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 valine-tyrosine 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 …
seeds and is well recognized for its nutritional value. We used this globulin to engineer a
new protein by adding a four valine-tyrosine 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 …
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 valine-tyrosine 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 β/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.
How to cite: Espinosa-Hernández E, Morales-Camacho JI, Fernández-Velasco DA, et al. 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 2019;37. https://doi.org/10.1016/j.ejbt.2018.11.001.
Elsevier
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