Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2017 Jul 19;8:15902. doi: 10.1038/ncomms15902

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2017, The Author(s)

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

PMC Copyright notice

(a) Encapsulation efficiency studies for the C4scFv single chain Fv domain in spheres, cylinders, short, thin and thick fibres. The indicated error bars are the s.d. of the average of three different repeats, each one measure 10 times. Insert: schematic representation of the encapsulation and release of antibiody domains by NSF micrococoons: step (1) encapsulation, step (2) release. (b) Release kinetics for C4scFv from different NSF micrococoon shapes. The indicated error bars are the s.d. of the average of three different repeats, each one measure 10 times. (c) Biacore sensorgrams of the binding of NbSyn86 to immobilized α-synuclein: (i) a control sample of monomeric NbSyn86, (ii) NbSyn86 after encapsulation and release treatment in the absence of NSF, (iii) NbSyn86 released from gelled NSF micrococoons (which contain ca. 2% of aggregated NSF), (iv) NbSyn86 released from gelled micrococoons which contain ca. 60% of aggregated NSF. (d) Graph of the equilibrium binding values for the different released NbSyn86 samples (as shown in c) versus the initial (pre-encapsulation) concentration of NbSyn86. The data were fitted to a 1:1 bimolecular binding model to estimate the affinity constant of NbSyn86 for α-synuclein, and were also used to estimate the loss of activity between samples. The indicated error bars are the s.d. of the average of three different repeats, each one measure five times.