Rational design of novel α-amylase inhibitor peptide derived from quinoa seed peptide with <i>in silico</i> approaches
values of 40.80 ± 0.10 μM (IQAEGGLT) to 9.75 ± 0.05 μM (RQAEGRLT). The CD showed the peptide exhibited a random coil structure that is effective to adjusting its structure in the interaction with receptor. The results showed that the derivative exhibited promising α-amylase inhibitory activity, suggesting it potential to combat diabetes.
Authors
- Tri Joko Raharjo
- Tendy Oktriawan
- Ahmad Habibie
- Rachmannisa Amalia Putri
Institutions
- Bandung Institute of Technology (ID)
- Universitas Gadjah Mada (ID)
Publication Details
- Journal
- Journal of Biomolecular Structure and Dynamics
- Published
- 2026-04-16
- DOI
- https://doi.org/10.1080/07391102.2026.2653794
- Primary Topic
- Protein Hydrolysis and Bioactive Peptides
- Type
- article
- Field-Weighted Citation Impact
- 0.00