Akademik Veri Yönetim Sistemi
CHEMBIOCHEM, cilt.25, sa.12, 2024 (SCI-Expanded)
Histamine is a biogenic amine that poses a potential threat to public health due to its toxicological effects. In this study, we identified histamine-binding peptides by screening a random 12-mer peptide library, employing a novel biopanning approach that excluded histidine-binding sequences in the final round. This additional step enhanced the selectivity of the peptides and prevented interference from histidine during detection. The binding affinities of synthesized peptides to histamine were assessed using isothermal titration calorimetry (ITC). Among the identified peptides, HBF10 (SGFRDGIEDFLW) and HBF26 (IPLENQHKIYST) showed significant affinity to histamine, with Ka values of 2.56x104 (M-1) and 8.94x104 (M-1), respectively. Notably, the identified peptides did not demonstrate binding affinity towards histidine, despite its structural similarity to histamine. Subsequently, the surface plasmon resonance (SPR) sensor surface was prepared by immobilizing the peptide HBF26 to investigate the potential of the peptide as a recognition agent for histamine detection. The findings suggest that the identified peptides have an affinity to histamine specifically, showcasing their potential applications as diagnostic agents with specific targeting capabilities. Histamine is a biogenic amine that affects food quality and causes health problems. This study presents a unique biopanning method to identify histamine-binding peptides, excluding histidine-binding sequences. Synthesizing 12-mer peptides from selected phage sequences, our findings reveal these peptides as potential ligands for biosensor (SPR) applications. image