Structure and Dynamics of Antifreeze Protein--Model Membrane Interactions: A Combined Spectroscopic and Molecular Dynamics Study

The Journal of Physical Chemistry. B
Rajiv K KarAnirban Bhunia

Abstract

Antifreeze proteins (AFPs) are the key biomolecules that enable species to survive under subzero temperature conditions. The physiologically relevant activities of AFPs are based on the adsorption to ice crystals, followed by the inhibition of subsequent crystal layer growth of ice, routed with depression in freezing point in a noncolligative manner. The functional attributes governing the mechanism by which AFPs inhibit freezing of body fluids in bacteria, fungi, plants, and fishes are mainly attributed to their adsorption onto the surface of ice within the physiological system. Importantly, AFPs are also known for their application in cryopreservation of biological samples that might be related to membrane interaction. To date, there is a paucity of information detailing the interaction of AFPs with membrane structures. Here, we focus on elucidating the biophysical properties of the interactions between AFPs and micelle models that mimic the membrane system. Micelle model systems of zwitterionic DPC and negatively charged SDS were utilized in this study, against which a significant interaction is experienced by two AFP molecules, namely, Peptide 1m and wfAFP (the popular AFP sourced from winter flounder). Using low- and high-...Continue Reading

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Citations

Feb 1, 2019·Physical Chemistry Chemical Physics : PCCP·Poonam Pandey, Sairam S Mallajosyula
Mar 12, 2020·International Journal of Biological Macromolecules·Hong XiangYong Hu
May 22, 2020·The Journal of Physical Chemistry. B·Ralph SchwidetzkyKonrad Meister
Nov 27, 2020·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·Elizabeth R EvansElizabeth L Crockett

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