Assessing protein–surface interactions with a series of multi-labeled BSA using fluorescence lifetime microscopy and Förster Energy Resonance Transfer

Abstract

Please cite this article as: Denisio M. Togashi, Alan G. Ryder, Assessing proteinsurface interactions with a series of multi-labeled BSA using Fluorescence Lifetime Microscopy and Förster Energy Resonance Transfer, Biophysical Chemistry (2010), doi: 10.1016/j.bpc.2010 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

Reevaluation of ANS Binding to Human and Bovine Serum Albumins: Key Role of Equilibrium Microdialysis in Ligand – Receptor Binding Characterization

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“…Correct determination of ligand-receptor binding stoichiometry and binding constants is very important both for fundamental investigations and practical aspects of molecule medicine, pharmaceutics and at the development of biosensor systems of high social significance [1], [2], [3], [4], [5], [6]. The determination of binding parameters significantly enriches tried-and-true method based on fluorescence of extrinsic dyes which is widely used in molecular and cellular biology for investigation of protein’s folding, structural changes induced by different agents, interaction with each other, aggregation, amyloid fibril formation etc.…”

Functional Polymers in Protein Detection Platforms: Optical, Electrochemical, Electrical, Mass-Sensitive, and Magnetic Biosensors

“…More recently, various sophisticated analytical techniques have been developed not only to quantify the amount of particular proteins but also to analyze interactions between multiple proteins. Examples of these analytical techniques include fluorescence resonance energy transfer (FRET) [25], fluorescence liftetime imaging microscopy (FLIM) [26–28], fluorescence correlation spectroscopy (FCS), and fluorescence recovery after photobleaching (FRAP). FRET is used for important applications such as determining localized structures of interacting proteins, protein folding behavior, conformational dynamics, and reaction mechanisms [29–31].…”

The Cysteine S‐Alkylation Reaction as a Synthetic Method to Covalently Modify Peptide Sequences

“…This approach allows effective improvement of the bioavailability and resistance to metabolic breakdown of peptide molecules with therapeutic potential . Moreover, naturally occurring post‐translational modifications can also be introduced, in order to thoroughly understand biomolecular mechanisms, as well as fluorophores or radiolabels for bioimaging and structural analysis, glycosylation for synthetic vaccines, and drug development …”