On the engulfment of antifreeze proteins by ice
成果类型:
Article
署名作者:
Thosar, Aniket U.; Cai, Yusheng; Marks, Sean M.; Vicars, Zachariah; Choi, Jeongmoon; Pallath, Akash; Patel, Amish J.
署名单位:
University of Pennsylvania
刊物名称:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
ISSN/ISSBN:
0027-13941
DOI:
10.1073/pnas.2320205121
发表日期:
2024-06-11
关键词:
binding site
freezing resistance
thermal hysteresis
mechanism
GROWTH
recrystallization
inhibition
adsorption
摘要:
Antifreeze proteins (AFPs) are remarkable biomolecules that suppress ice formation at trace concentrations. To inhibit ice growth, AFPs must not only bind to ice crystals, but also resist engulfment by ice. The highest supercooling, A T * , for which AFPs are able to resist engulfment is widely believed to scale as the inverse of the separation, L , between bound AFPs, whereas its dependence on the molecular characteristics of the AFP remains poorly understood. By using specialized molecular simulations and interfacial thermodynamics, here, we show that in contrast with conventional wisdom, A T * scales as L - 2 and not as L - 1 . We further show that A T * is proportional to AFP size and that diverse naturally occurring AFPs are optimal at resisting engulfment by ice. By facilitating the development of AFP structure-function relationships, we hope that our findings will pave the way for the rational design of AFPs.