RUI: Investigations of hydrogels formed by semenogelin I-derived peptide sequences

水凝胶是一种具有巨大吸水能力的材料，这使它们适用于各种日常应用，如婴儿尿布、隐形眼镜和药物包装。水凝胶由聚合物网络组成，新型水凝胶聚合物正在不断开发。人们很有兴趣了解水凝胶的详细结构是什么，网络结构如何影响水凝胶的性能，以及如何随心所欲地对水凝胶聚合物进行改性。这项研究的目的是研究天然蛋白质形成水凝胶的过程。这种水凝胶，因为它是天然来源，无毒，生物相容，可生物降解和环境友好。这项研究涉及美国哈弗福德学院、瑞典隆德大学和英国剑桥大学的研究小组之间的国际合作。该项目为本科生提供跨学科和国际化的研究机会。该项目还包括来自代表性不足群体的学生参与，为他们在各种化学相关领域的研究生学习以及在工业中的职业生涯做好准备。这个项目的本科生参与者在固相蛋白质合成和纯化的最新方法方面获得了直接的实践经验和培训。本研究旨在了解多肽支架形成凝胶的机理。研究中的寡肽自组装形成由扩展的β-折叠组成的纤维。这种由10个残基组成的短肽形成了一种水凝胶，其性质特别适合系统研究。本项目通过研究寡肽的一系列突变体和截断版本来探索水凝胶形成的序列特异性决定因素，使用主要的圆二色谱和傅里叶变换红外光谱对其进行表征。研究通过将同位素标记的残基加入到序列中来询问自组装过程。最后，研究人员使用基于硫代黄素的分析来跟踪纤维形成的动力学，这也被用作评估外部变量(如pH)对聚集的影响的工具。

Hydrogels are materials with a tremendous capacity to absorb water, which makes them useful for a variety of every-day applications such as baby diapers, contact lenses and drug encapsulation. Hydrogels consist of polymer networks and new types of hydrogel polymers are continuously being developed. There is a considerable interest in learning what the detailed structure of a hydrogel looks like and how the structure of the network influences the hydrogel properties as well as how the hydrogel polymers can be modified at will. The aim of this research is to investigate the formation of a hydrogel from natural proteins. This hydrogel, because it is of natural origin, is non-toxic, biocompatible, biodegradable and environmentally friendly. This research involves an international collaboration between research groups at Haverford College, US; Lund University, Sweden; and the University of Cambridge, UK. The project provides interdisciplinary and international research opportunities to undergraduate students. The project also includes participation by students from underrepresented groups, preparing them for graduate studies in a variety of chemically related fields, as well as for careers in industry. The undergraduate participants of this project gain direct hands-on experience and training in state-of-the-art methodologies for solid-phase protein synthesis and purification. This research aims to understand gel formation by peptide scaffolds. The oligopeptide under investigation self-assembles to form fibrils consisting of extended beta-sheets. This short 10-residue peptide forms a hydrogel with properties that are particularly well suited for systematic investigations. This project probes the sequence-specific determinants of hydrogel formation by studying a series of mutants and truncated versions of the oligopeptide, employing predominantly circular dichroism and Fourier transform infrared spectroscopy for their characterization The research interrogates the self-assembly process by incorporating isotopically labeled residues into the sequence. Finally, the researchers follow the kinetics of fibril formation using a thioflavine-based assay, which is also used as a tool to assess the effects of external variables, such as pH, on aggregation.