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

水凝胶是具有巨大吸水能力的材料，这使得它们可用于各种日常应用，如婴儿尿布，隐形眼镜和药物封装。 水凝胶由聚合物网络组成，并且新型水凝胶聚合物不断被开发。 人们对了解水凝胶的详细结构、网络结构如何影响水凝胶性能以及水凝胶聚合物如何随意改性非常感兴趣。本研究的目的是研究从天然蛋白质形成水凝胶。 这种水凝胶，因为它是天然来源的，是无毒的，生物相容性，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研究机会。 该项目还包括来自代表性不足群体的学生的参与，为他们在各种化学相关领域的研究生学习以及工业职业做好准备。 该项目的本科生参与者获得直接的实践经验和最先进的固相蛋白质合成和纯化方法的培训。 本研究旨在了解肽支架的凝胶形成。 研究中的寡肽自组装形成由延伸的β-折叠组成的原纤维。 这种短的10-残基肽形成具有特别适合系统研究的性质的水凝胶。 该项目通过研究寡肽的一系列突变体和截短版本来探索水凝胶形成的序列特异性决定因素，主要采用圆二色性和傅立叶变换红外光谱进行表征。该研究通过将同位素标记的残基并入序列来询问自组装过程。 最后，研究人员使用基于硫代嘌呤的测定法跟踪原纤维形成的动力学，该测定法也被用作评估外部变量（如pH值）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.