1.D.323. The Fe²⁺-Transporting Octapeptide, SGYGYGYG (SGYGYGYG) Family A ferrous ion-transport capacity of a multifunctional octapeptide from Camellia oleifera globulin has been reported (Li et al. 2025). It is not known if it functions by a channel or carrier mechanism. It has the sequence SGYGYGYG. It has ferrous ion chelating (8.67 mg/g) and hydroxyl radical quenching abilities (93.06%). The intestinal stability and transmembrane absorption of ferrous ions were improved by SGYGYGYG-ferrous chelate, though SGYGYGYG had poor gastrointestinal stability. Thus, SGYGYGYG may be exploited as ingredients of hypotensive, antioxidant, and iron supplementary agents. Another octapeptide that can transport Fe²⁺is PVDFAGFY. Ferrous ions were primarily chelated by γ-hydroxyl, carboxyl, and/or amino groups of PVDFAGFY via ionic forces (Jin et al. 2025). The activity of PVDFAGFY was not altered by iron chelation.
References:
Jin, Z., L. Dang, Y. Li, C. Feng, X. Song, Z. Wei, J. Liu, H. Wang, and Y. Zhang. (2025). Purification, identification, and screening of a multifunctional octapeptide from glutelin-2 hydrolysates: restraining mechanisms to Keap1 and ACE, stability, and ferrous-transport efficiency. Front Nutr 12: 1571161.
Li, Y., Y. Yang, C. Feng, J. Liu, J. Wang, and L. Wang. (2025). Identification, In Silico Screening, Inhibition Mechanisms to Keap1 and Angiotensin-I-Converting Enzyme, and Ferrous-Transport Capacity of a Multifunctional Octapeptide from Camellia oleifera Globulin. Plant Foods Hum Nutr 80: 109.