Multivalent Display of Antifreeze Proteins by Fusion to Self-Assembling Protein Cages Enhances Ice-Binding Activities.
作者： Sean W. Phippen , Corey A. Stevens , Tyler D. R. Vance , Neil P. King , David Baker
DOI: 10.1021/ACS.BIOCHEM.6B00864
关键词: Bacteria 、 Ice crystals 、 Biology 、 Conjugated system 、 Ice binding 、 Nanoparticle 、 Monomer 、 Antifreeze protein 、 Biochemistry 、 Freezing-point depression
摘要: Antifreeze proteins (AFPs) are small monomeric that adsorb to the surface of ice inhibit crystal growth and impart freeze resistance organisms producing them. Previously, AFPs have been conjugated termini branched polymers increase their activity through simultaneous binding more than one AFP ice. Here, we describe a superior approach increasing oligomerization eliminates need for conjugation reactions with varying levels efficiency. A moderately active from fish hyperactive an Antarctic bacterium were genetically fused C-termini component 24-subunit protein cage T33-21, resulting in nanoparticles multivalently display exactly 12 AFPs. The exhibited freezing point depression >50-fold greater seen same concentration similar level ice-recrystallization inhibition. These results s...
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