Cold temperatures are a major source of stress for plants and negatively impact crop yield. A possible way to protect plants is to treat them with antifreeze proteins (AFPs). Here, we investigated whether fish AFPs can shield the rare ornamental species from low-temperature stress. We elucidated the expression patterns of the cold-inducible genes C-repeat binding factor 1 () and dehydrin 1 (), as well as the antioxidant genes superoxide dismutase () and catalase (). All were upregulated at low temperature (4 °C). With increasing exposure time, and expression generally rose (except at 48 h). In contrast, and expression gradually declined from 6 to 48 h. Depending on exposure duration, AFP regulation of gene transcription varied with concentration. However, compared with other concentrations, 100 µg/L AFP reduced and expression and increased and expression in plants, regardless of exposure time. Both AFP I and III were likely to be most effective at protecting plants against cold stress at concentrations of 100 µg/L. Their involvement in cold-stress treatment occurred through regulating the expression of important stress-response genes.
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http://dx.doi.org/10.1007/s13205-019-1859-5 | DOI Listing |
J Am Chem Soc
January 2025
Department of Materials Science and Engineering, City University of Hong Kong, Hong Kong, Kowloon 999077, China.
Heterogeneous ice nucleation is a widespread phenomenon in nature. Despite extensive research on ice nucleation near biological antifreeze proteins, a probe for ice nucleation and growth processes at the atomic level is still lacking. Herein, we present simulation evidence of the heterogeneous ice nucleation process on the ice-binding surface (IBS) of the antifreeze protein (TmAFP).
View Article and Find Full Text PDFLangmuir
January 2025
School of Physical Science and Technology, ShanghaiTech University, Shanghai 201210, China.
The antifreeze mechanism of antifreeze glycoproteins (AFGPs) remains incompletely understood, which limits the design of new antifreeze molecules for practical applications. For instance, the ice growth inhibition of AFGP8 (the shortest AFGPs) is primarily driven by hydrophobic methyl and hydrogen-bonding hydroxyl groups. However, altering the C3-β linkage in the disaccharide moiety of AFGP8, denoted as variant GP8-LacNAc, significantly reduces its antifreeze activity.
View Article and Find Full Text PDFTheriogenology
January 2025
Veterinary Clinic for Reproductive Medicine and Neonatology, Justus Liebig-University of Giessen, Germany.
Sperm cryopreservation is crucial in reproductive biotechnology; however, the longevity of frozen and thawed semen is limited by the deterioration of sperm cell integrity. This study aimed to examine the effects of adding antifreeze protein III (AFP III) to the diluent, using samples from eight healthy mature dogs. The ejaculates were divided into aliquots and diluted with a standard Tris-fructose-egg yolk extender containing AFP III at concentrations of 0, 0.
View Article and Find Full Text PDFNano Lett
January 2025
Department of Biochemical Engineering, School of Chemical Engineering and Technology, State Key Laboratory of Synthetic Biology, Frontier Science Center for Synthetic Biology and Key Laboratory of Systems Bioengineering (MOE), Tianjin University, Tianjin 300350, China.
Organisms that survive at freezing temperatures produce antifreeze proteins (AFPs) to manage ice nucleation and growth. Inspired by AFPs, a series of synthetic materials have been developed to mimic these proteins in order to avoid the limitations of natural AFPs. Despite their great importance in various antifreeze applications, the relationship between structure and performance of AFP mimics remains unclear, especially whether their molecular charge-specific effects on ice inhibition exist.
View Article and Find Full Text PDFFood Chem
December 2024
Department of Food Science, The University of Tennessee, Knoxville (UTK), TN 37996, United States. Electronic address:
The glycomacropeptide (GMP) present in the cheese whey byproduct can be an excellent antifreezing agent due to its unique molecular structure. The objective of this study was to concentrate this peptide and investigate its ice recrystallization inhibition (IRI) ability. Heat denaturation of the non-GMP proteins and preparative liquid chromatography were used to create fraction 1 (F1) and fraction 2 (F2) and these were tested using the splat assay and a modified sucrose sandwich assay to investigate their IRI activity.
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