Thermodynamic binding properties of a novel umami octapeptide K1ADEDSLA8 and its mutational variants p.A2G, p.D5E, and p.A2G + p.D5E (BMP) in complex with the umami receptor hT1R1/hT1R3

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Andac C. A., ÖZEL C., Rababah T. M., Kececiler-Emir C., KÖKLÜ K., Tekdaş D. A., ...More

Food Chemistry, vol.473, 2025 (SCI-Expanded)

• Publication Type: Article / Article
• Volume: 473
• Publication Date: 2025
• Doi Number: 10.1016/j.foodchem.2025.142966
• Journal Name: Food Chemistry
• Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, PASCAL, Aerospace Database, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, CAB Abstracts, Chemical Abstracts Core, Chimica, Communication Abstracts, Compendex, EMBASE, Food Science & Technology Abstracts, Metadex, Veterinary Science Database, Civil Engineering Abstracts
• Keywords: MM-PBSA, Molecular docking, Molecular dynamics, Mutational affinity prediction (MAP), T1R1/T1R3, Umami peptide
• Yıldız Technical University Affiliated: Yes

Abstract

Umami taste properties of a novel octameric peptide K1ADEDSLA8 and its mutants p.A2G, p.D5E, and BMP (KGDEESLA, beef meaty peptide) were assessed by molecular docking, and molecular dynamics (MD) (>1 μsec), MM-PBSA, and Mutational Affinity Prediction (MAP) methods. 3D-structure of the human umami taste receptor (hT1R1/hT1R3) was homology modeled and refined MD. Docking studies yielded three primary binding sites (PBS) for K1ADEDSLA8 and BMP, one on hT1R1 and two on hT1R3. Upto 1200 nsec of MD studies revealed that K1ADEDSLA8 binds only to Venus Flytrap Domains (VFTD) region of hT1R1 at high affinity (ΔGo = −11.94 kcal/mol), while BMP does not exhibit affinity towards hT1R1/hT1R3 in the absence of glutamate. MAP analysis for p.A2G (ΔGo = −7.77 kcal/mol) and p.D5E (ΔGo = −2.88 kcal/mol) strongly suggest that A2 and D5 in KA2DED5SLA increase the affinity and specificity of binding, posing great potential for the development of a novel umami peptide in future studies.