Screening and Activity Evaluation of Peptides With Anti-Ice-Nucleation Activity Using the Phage Display Library Method.
- 1Department of Chemistry and Materials Engineering, Faculty of Chemistry Materials and Bioengineering, Kansai University, Suita, Japan.
Abstract
We screened for anti-ice-nucleation peptides using the phage display library method, with silver iodide as the target for artificial ice nucleation The phage interacted with the silver iodide in a dispersed state, rather than in an immobilized state. Based on DNA analysis, we identified five peptides with high expression levels. Five peptide sequences were synthesized by hand using the Fmoc solid-phase peptide synthesis and evaluated their anti-ice-nucleation activity. Three peptide sequences exhibited anti-ice-nucleation activity, and two of them were insoluble in water. Among the three peptides, SHIARSV exhibited the highest anti-ice-nucleation activity. To determine the importance of each amino acid in SHIARSV, we designed five peptides in which Ala was substituted and examined their anti-ice-nucleation activity. As a result, we identified AHIARSV, a peptide sequence with higher anti-ice-nucleation activity than the original SHIARSV sequence. This peptide exhibited high levels of both anti-nucleation activity and ice recrystallization inhibition activity. It is our conclusion that the design of antifreeze peptides with activities comparable with those of natural ones is highly feasible.
Related
- Hydrophobic Ion Pairing with Cationic Surfactant Modifies Surface Activity and Colloidal Behavior of PFAS
- Wave-ice interaction strengthens eddy activity in Fram Strait
- Phytochemical Composition, Elemental Profiles, Antioxidant Activity, and Xenobiotic Relevance of Rosehip and Sea Buckthorn Fruits from Armenia
- A Project-based Learning Activity Involving Hybrid Intelligence in the Undergraduate Engineering Class
- Increasing favorability for intense tropical cyclone activity in the northern South China Sea
BibTeX
@article{okamoto2026screening,
title = {{Screening and Activity Evaluation of Peptides With Anti-Ice-Nucleation Activity Using the Phage Display Library Method.}},
author = {Sora Okamoto and Seijiro Matsuki and Yoshiaki Hirano},
journal = {Journal of peptide science : an official publication of the European Peptide Society},
year = {2026},
month = oct,
doi = {10.1002/psc.70141},
url = {https://europepmc.org/article/MED/42910641},
note = {CC BY},
}
RIS
TY - JOUR
TI - Screening and Activity Evaluation of Peptides With Anti-Ice-Nucleation Activity Using the Phage Display Library Method.
AU - Sora Okamoto
AU - Seijiro Matsuki
AU - Yoshiaki Hirano
PY - 2026
DA - 2026/10/30
JO - Journal of peptide science : an official publication of the European Peptide Society
DO - 10.1002/psc.70141
UR - https://europepmc.org/article/MED/42910641
AB - We screened for anti-ice-nucleation peptides using the phage display library method, with silver iodide as the target for artificial ice nucleation The phage interacted with the silver iodide in a dispersed state, rather than in an immobilized state. Based on DNA analysis, we identified five peptides with high expression levels. Five peptide sequences were synthesized by hand using the Fmoc solid-phase peptide synthesis and evaluated their anti-ice-nucleation activity. Three peptide sequences exhibited anti-ice-nucleation activity, and two of them were insoluble in water. Among the three peptides, SHIARSV exhibited the highest anti-ice-nucleation activity. To determine the importance of each amino acid in SHIARSV, we designed five peptides in which Ala was substituted and examined their anti-ice-nucleation activity. As a result, we identified AHIARSV, a peptide sequence with higher anti-ice-nucleation activity than the original SHIARSV sequence. This peptide exhibited high levels of both anti-nucleation activity and ice recrystallization inhibition activity. It is our conclusion that the design of antifreeze peptides with activities comparable with those of natural ones is highly feasible.
SN - 1075-2617
SN - 1099-1387
ER -