{"title":"Raman spectroscopy and imaging of protein droplet formation and aggregation","authors":"Matthew D. Watson, Jennifer C. Lee","doi":"10.1016/j.sbi.2025.103041","DOIUrl":null,"url":null,"abstract":"<div><div>Raman microscopy offers a unique combination of chemical and spatial resolution with structural sensitivity. This makes it an ideal tool for studies of protein structural changes in heterogenous samples such as protein liquid–liquid phase separation (LLPS) and amyloid formation. These processes are characterized by the spontaneous assembly of proteins to form either microscopic liquid droplets or insoluble filaments stabilized by β-sheets. LLPS and amyloid formation are closely related, with many proteins that undergo LLPS also forming amyloids. This has led to the proposal that development of β-sheets in droplets is an initiating event in toxic amyloid formation. This review surveys recent applications of Raman microscopic methods to studies of LLPS and amyloid formation both <em>in vitro</em> and <em>in cellulo</em>.</div></div>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"92 ","pages":"Article 103041"},"PeriodicalIF":6.1000,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current opinion in structural biology","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0959440X25000594","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Raman microscopy offers a unique combination of chemical and spatial resolution with structural sensitivity. This makes it an ideal tool for studies of protein structural changes in heterogenous samples such as protein liquid–liquid phase separation (LLPS) and amyloid formation. These processes are characterized by the spontaneous assembly of proteins to form either microscopic liquid droplets or insoluble filaments stabilized by β-sheets. LLPS and amyloid formation are closely related, with many proteins that undergo LLPS also forming amyloids. This has led to the proposal that development of β-sheets in droplets is an initiating event in toxic amyloid formation. This review surveys recent applications of Raman microscopic methods to studies of LLPS and amyloid formation both in vitro and in cellulo.
期刊介绍:
Current Opinion in Structural Biology (COSB) aims to stimulate scientifically grounded, interdisciplinary, multi-scale debate and exchange of ideas. It contains polished, concise and timely reviews and opinions, with particular emphasis on those articles published in the past two years. In addition to describing recent trends, the authors are encouraged to give their subjective opinion of the topics discussed.
In COSB, we help the reader by providing in a systematic manner:
1. The views of experts on current advances in their field in a clear and readable form.
2. Evaluations of the most interesting papers, annotated by experts, from the great wealth of original publications.
[...]
The subject of Structural Biology is divided into twelve themed sections, each of which is reviewed once a year. Each issue contains two sections, and the amount of space devoted to each section is related to its importance.
-Folding and Binding-
Nucleic acids and their protein complexes-
Macromolecular Machines-
Theory and Simulation-
Sequences and Topology-
New constructs and expression of proteins-
Membranes-
Engineering and Design-
Carbohydrate-protein interactions and glycosylation-
Biophysical and molecular biological methods-
Multi-protein assemblies in signalling-
Catalysis and Regulation