To be launched on Aug 2015
 
Sponsored by Biophysical Society of China and Institute of Biophysics, CAS, P.R. China.
Online published by SpringerLink.
  Links


 
Online First
The manuscripts published below will continue to be available from this page until they are assigned to an issue.
Please wait a minute...
For Selected: View Abstracts Toggle Thumbnails
Animal protein toxins: origins and therapeutic applications
Na Chen, Siqi Xu, Yuhan Zhang, Feng Wang
Biophysics Reports    DOI: 10.1007/s41048-018-0067-x
Abstract   PDF (687KB)
Venomous animals on the earth have been found to be valuable resources for the development of therapeutics. Enzymatic and non-enzymatic proteins and peptides are the major components of animal venoms, many of which can target various ion channels, receptors, and membrane transporters. Compared to traditional small molecule drugs, natural proteins and peptides exhibit higher specificity and potency to their targets. In this review, we summarize the varieties and characteristics of toxins from a few representative venomous animals, and describe the components and applications of animal toxins as potential drug candidates in the treatment of human diseases, including cancer, neurodegenerative diseases, cardiovascular diseases, neuropathic pain, as well as autoimmune diseases. In the meantime, there are many obstacles to translate new toxin discovery to their clinical applications. The challenges, strategies, and perspectives in the development of the protein toxin-based drugs are discussed as well.
Reference | Related Articles | Metrics
Proteomic analysis of insulin secretory granules in INS-1 cells by protein correlation profiling
Min Li, Wen Du, Maoge Zhou, Li Zheng, Eli Song, Junjie Hou
Biophysics Reports    DOI: 10.1007/s41048-018-0061-3
Abstract   PDF (1545KB)
Insulin secretory granules (ISGs), a group of distinguishing organelles in pancreatic β cells, are responsible for the storage and secretion of insulin to maintain blood glucose homeostasis. The molecular mechanisms of ISG biogenesis, maturation, transportation, and exocytosis are still largely unknown because the proteins involved in these distinct steps have not been fully identified. Subcellular fractionation by density gradient centrifugation has been successfully employed to analyze the proteomes of numerous organelles. However, use of this method to elucidate the ISG proteome is limited by co-fractionated contaminants because ISGs are very dynamic and have abundant exchanges or contacts with other organelles, such as the Golgi apparatus, lysosomes, and endosomes. In this study, we developed a new strategy for identifying ISG proteins by protein correlation profiling (PCP)-based proteomics, which included ISG purification by OptiPrep density gradient centrifugation, label-free quantitative proteome, and identification of ISG proteins by correlating fractionation profiles between candidates and known ISG markers. Using this approach, we were able to identify 81 ISG proteins. Among them, TM9SF3, a nine-transmembrane protein, was considered a high confidence ISG candidate protein highlighted in the PCP network. Further biochemical and immunofluorescence assays indicated that TM9SF3 localized in ISGs, suggesting that it is a potential new ISG marker.
Reference | Related Articles | Metrics
Electron microscopy combined with spatial analysis: quantitative mapping of the nano-assemblies of plasma membrane-associating proteins and lipids
Yong Zhou, John F. Hancock
Biophysics Reports    DOI: 10.1007/s41048-018-0060-4
Abstract   PDF (697KB)
The plasma membrane (PM) is a complex environment consisting of[700 species of lipids and many different types of membrane-associating proteins.These lipids and membrane proteins are distributed heterogeneously into nanometer-sized domains,called nanoclusters.The lateral spatial segregation in the PM gives rise to different curvature and lipid composition,which determines the efficiency of effector binding and signal transmission.Here,we describe an electron microscopy (EM)-spatial mapping technique to quantify the extent of nanoclusters formation in the PM.The nano-assemblies in the PM are quantified via expressing the GFP-tagged proteins or lipid-binding domains in the cells, which are then immunolabeled with the gold nanoparticles pre-coupled to the anti-GFP antibody.The gold nanoparticles are visualized via the transmission EM at high magnification.The statistical analysis of the Ripley's K-function calculates the spatial distribution of the gold nanoparticles.Important spatial parameters,such as the extent of nanoclustering,the clustered fraction,the number of proteins per cluster,the optimal size of a nanocluster,and the number of proteins localized to the PM,can be calculated.Further detailed aggregation pattern,such as the populations of monomers,dimers,trimers, and higher ordered oligomers,can also be extracted from the spatial analysis.The EM-bivariate analysis quantifies the extent of co-localization between two different components in the PM and provides key information on the protein-protein and the protein-lipid interactions over a long-distance scale from 8 to 240 nm.
Reference | Related Articles | Metrics
First page | Prev page | Next page | Last page Page 1 of 1, 3 articles found  
CN 10-1302/Q
ISSN 2364-3439
eISSN 2364-3420
Home
About the Journal
Editorial Board
Author Guidelines
Archive
Submission
Subscription
Biophysics Reports Editorial Office
Institute of Biophysics, CAS 15 Datun Road, Chaoyang District Beijing 100101, China Tel: (86-10) 64888458
Fax: (86-10) 64889892
E-mail: biophysics-reports@ibp.ac.cn
Copyright © 2015 Biophysics Reports