Collaborative Research: Experimental and Computational Examination of Biomimetic Peptides Acting as Anti-freeze Molecules

这一奖项来自美国国家科学基金会化学分部的环境化学科学项目，支持教授们的这一合作项目。石溪大学的丹尼尔·克诺夫和罗伯特·格拉布斯以及耶鲁大学的阿米尔·阿吉-阿克巴里教授共同研究并产生可以控制水冻结的有机分子。抑制结冰的能力在关键技术应用中至关重要，例如生物材料的保存、食品加工和储存，以及防止飞机和海上平台等裸露表面上的冰增长。在自然界中，一些生物可以产生所谓的抗冻蛋白(AFP)来控制冰的形成，从而使它们能够在冰冻的温度下生存。这个合作项目旨在理解和模拟这些AFP，以允许产生可用于各种研究领域和行业的设计的合成防冻剂分子。该项目将培训三名研究生和两名本科生，并为高中生的暑期拓展计划提供课程模块。该团队将设计AFP模拟物(AFP)，其结构比天然AFP更简单，可以生产实用且成本效益高的结冰抑制剂和防冰涂层。通过将在β-螺旋AFP的冰结合面上发现的亲水和疏水氨基酸侧链的排列转化为覆盖从单分子到底物锚定的AFP阵列的不同长度尺度的多肽-聚合物偶联物，将寻求对抗冻能力的机理理解。冰核和冰重结晶抑制实验将决定合成生物分子的防冻效果。使用路径采样的理论研究将在类似于实验的长度尺度上解决水-甲胎蛋白的模拟相互作用。这一综合方法将确定疏水和亲水基团的位置和强度的重要性，以及AFPM在防冻效果方面的灵活性，从而促进影响冰核形成和生长的仿生设计。该奖项反映了NSF的法定使命，并通过使用基金会的智力价值和更广泛的影响审查标准进行评估，被认为值得支持。

This award from the Environmental Chemical Sciences Program in the NSF Division of Chemistry supports this collaborative project of Profs. Daniel Knopf and Robert Grubbs at Stony Brook University and Prof. Amir Haji-Akbari at Yale University to examine and generate organic molecules that can control the freezing of water. The ability to inhibit ice formation is crucial in critical technological applications such as preservation of biological materials, food processing and storage, and preventing ice growth on exposed surfaces such as those on aircraft and offshore platforms. In nature some organisms can produce so-called antifreeze proteins (AFPs) to control ice formation allowing their survival at freezing temperatures. This collaborative project aims to understand and mimic those AFPs to allow for generation of designed synthetic antifreeze molecules that can be used in various research areas and industries. This project will train three graduate and two undergraduate students and provide a course module for a summer outreach program for high school students.The team will design AFP mimetics (AFPMs) with less complex structures than natural AFPs that can lead to practical and cost-efficient ice inhibitors and anti-icing coatings. A mechanistic understanding of the antifreezing capability will be sought by translating arrangements of hydrophilic and hydrophobic amino acid side chains found in ice-binding faces of β-helical AFPs to peptide-polymer conjugates covering various length scales from single molecules to arrays of substrate-anchored AFPMs. Ice nucleation and ice recrystallization inhibition experiments will determine the antifreezing efficacy of synthesized biomolecules. Theoretical studies using path-sampling will resolve the water-AFP mimetic interactions on length scales similar to those in the experiments. This comprehensive approach will determine the importance of the location and strength of the hydrophobic and hydrophilic groups and the flexibility of the AFPMs for antifreezing efficacy, thereby advancing the design of biomimetics that influence ice nucleation and growth.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.