The spontaneous formation of a protein corona on a nanoparticle surface influences the physiological success or failure of the synthetic nanoparticle as a drug carrier or imaging agent used in vivo. A quantitative understanding of protein-nanoparticle interactions is therefore critical for the development of nanoparticle-based therapeutics. In this perspective, we briefly discuss the challenges and limitations of current approaches used for studying protein-nanoparticle binding in a realistic...
[NMR paper] Probing the Binding Modes of a Multi-Domain Protein to Lipid-Based Nanoparticles by Relaxation-Based NMR.
Probing the Binding Modes of a Multi-Domain Protein to Lipid-Based Nanoparticles by Relaxation-Based NMR.
Related Articles Probing the Binding Modes of a Multi-Domain Protein to Lipid-Based Nanoparticles by Relaxation-Based NMR.
J Phys Chem Lett. 2017 May 22;:
Authors: Ceccon A, Tugarinov V, Boughton AJ, Fushman D, Clore GM
Abstract
The interactions of two model multi-domain proteins - covalently linked di-ubiquitins, Ub2 - with lipid-based nanoparticles have been quantitatively probed by the measurements of NMR lifetime...
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05-23-2017 04:45 PM
[NMR paper] Unravelling and quantifying the "NMR-invisible" metabolites interacting with human serum albumin by binding competition and T2 relaxation-based decomposition analysis.
Unravelling and quantifying the "NMR-invisible" metabolites interacting with human serum albumin by binding competition and T2 relaxation-based decomposition analysis.
Related Articles Unravelling and quantifying the "NMR-invisible" metabolites interacting with human serum albumin by binding competition and T2 relaxation-based decomposition analysis.
J Proteome Res. 2017 Mar 27;:
Authors: Barrilero R, Ramirez N, Vallvé JC, Taverner D, Fuertes R, Amigó N, Correig X
Abstract
Quantitative profiling of low-molecular-weight...
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03-28-2017 03:06 PM
GlobalDynamics and Exchange Kinetics of a Proteinon the Surface of Nanoparticles Revealed by Relaxation-Based SolutionNMR Spectroscopy
GlobalDynamics and Exchange Kinetics of a Proteinon the Surface of Nanoparticles Revealed by Relaxation-Based SolutionNMR Spectroscopy
Alberto Ceccon, Vitali Tugarinov, Ad Bax and G. Marius Clore
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.6b02654/20160427/images/medium/ja-2016-02654c_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.6b02654
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/edns7WqH1Ts
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04-28-2016 02:04 AM
[NMR paper] Global Dynamics and Exchange Kinetics of a Protein on the Surface of Nanoparticles Revealed by Relaxation-Based Solution NMR Spectroscopy.
Global Dynamics and Exchange Kinetics of a Protein on the Surface of Nanoparticles Revealed by Relaxation-Based Solution NMR Spectroscopy.
Global Dynamics and Exchange Kinetics of a Protein on the Surface of Nanoparticles Revealed by Relaxation-Based Solution NMR Spectroscopy.
J Am Chem Soc. 2016 Apr 25;
Authors: Ceccon A, Tugarinov V, Bax A, Clore GM
Abstract
The global motions and exchange kinetics of a model protein, ubiquitin, bound to the surface of negatively charged lipid-based nano-particles (liposomes) are derived from...
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04-26-2016 12:14 PM
Pairwise binding competition experiments for sorting hub-protein/effector interaction hierarchy and simultaneous equilibria
Pairwise binding competition experiments for sorting hub-protein/effector interaction hierarchy and simultaneous equilibria
Abstract
NMR experiments on proteins in simultaneous equilibria with multiple binding partners can provide a tool to understand complex biological interaction networks. Competition among proteins for binding to signaling hubs is often at the basis of the information transmission across signaling networks in every organism. Changes in affinity towards one or more partners, as well as changes of the relative concentration of the...
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07-12-2014 06:07 PM
Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP
Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP
Abstract CD2 associated protein (CD2AP) is an adaptor protein that plays an important role in cell to cell union needed for the kidney function. It contains three N-terminal SH3 domains that are able to interact among others with CD2, ALIX, c-Cbl and Ubiquitin. To understand the role of the individual SH3 domains of this adaptor protein we have performed a complete structural, thermodynamic and dynamic characterization of the separate domains using NMR and DSC. The energetic contributions to the stability...
[NMR paper] The mitochondrial precursor protein apocytochrome c strongly influences the order of
The mitochondrial precursor protein apocytochrome c strongly influences the order of the headgroup and acyl chains of phosphatidylserine dispersions. A 2H and 31P NMR study.
Related Articles The mitochondrial precursor protein apocytochrome c strongly influences the order of the headgroup and acyl chains of phosphatidylserine dispersions. A 2H and 31P NMR study.
Biochemistry. 1990 Mar 6;29(9):2312-21
Authors: Jordi W, de Kroon AI, Killian JA, de Kruijff B
Deuterium and phosphorus nuclear magnetic resonance techniques were used to study the...
Solution NMR of Nanoparticles in Serum: Protein Competition Influences Binding Thermodynamics and Kinetics
Linear Mode
