Quantification of silk protein using phage nanofibers with high binding specificity

2020 ◽  
Vol 8 (24) ◽  
pp. 5189-5194 ◽  
Author(s):  
Lu Ma ◽  
Tao Yang ◽  
Mengmeng Zhai ◽  
Mingying Yang ◽  
Chuanbin Mao

An ultrasensitive detection strategy for silk sericin (SS) is established by using phage nanofibers displaying SS-binding peptides derived from biopanning. SS concentration is determined by counting the plaques developed from the SS-binding phages.

2016 ◽  
Vol 113 (27) ◽  
pp. E3862-E3871 ◽  
Author(s):  
Abdellali Kelil ◽  
Emmanuel D. Levy ◽  
Stephen W. Michnick

Evolution of complexity in eukaryotic proteomes has arisen, in part, through emergence of modular independently folded domains mediating protein interactions via binding to short linear peptides in proteins. Over 30 years, structural properties and sequence preferences of these peptides have been extensively characterized. Less successful, however, were efforts to establish relationships between physicochemical properties and functions of domain–peptide interactions. To our knowledge, we have devised the first strategy to exhaustively explore the binding specificity of protein domain–peptide interactions. We applied the strategy to SH3 domains to determine the properties of their binding peptides starting from various experimental data. The strategy identified the majority (∼70%) of experimentally determined SH3 binding sites. We discovered mutual relationships among binding specificity, binding affinity, and structural properties and evolution of linear peptides. Remarkably, we found that these properties are also related to functional diversity, defined by depth of proteins within hierarchies of gene ontologies. Our results revealed that linear peptides evolved to coadapt specificity and affinity to functional diversity of domain–peptide interactions. Thus, domain–peptide interactions follow human-constructed gene ontologies, which suggest that our understanding of biological process hierarchies reflect the way chemical and thermodynamic properties of linear peptides and their interaction networks, in general, have evolved.


Viruses ◽  
2015 ◽  
Vol 7 (6) ◽  
pp. 2771-2793 ◽  
Author(s):  
Jens Hammerl ◽  
Nicole Roschanski ◽  
Rudi Lurz ◽  
Reimar Johne ◽  
Erich Lanka ◽  
...  

2016 ◽  
Vol 4 (2) ◽  
pp. 340-347 ◽  
Author(s):  
Wenhua Li ◽  
Yurong Cai ◽  
Qiwei Zhong ◽  
Ying Yang ◽  
Subhas C. Kundu ◽  
...  

Silk protein sericin based organic–inorganic hybrid microcapsules are fabricated by incubating sericin microcapsules with a supersaturated calcium phosphate solution containing citric acid.


2015 ◽  
Vol 6 (11) ◽  
pp. 6213-6218 ◽  
Author(s):  
Xiaobo Zhang ◽  
Chenghui Liu ◽  
Lingbo Sun ◽  
Xinrui Duan ◽  
Zhengping Li

A single microbead-based sensing platform has been developed, which enables the detection of microRNA at the single-molecule level.


2012 ◽  
Author(s):  
Christopher Weaver ◽  
Avanti Jangalapalli ◽  
Kimberly Yano ◽  
Charles Ramskov ◽  
Paul Marcille

1970 ◽  
Vol 65 (1_Suppl) ◽  
pp. S104-S121 ◽  
Author(s):  
E. E. Baulieu ◽  
J. P. Raynaud ◽  
E. Milgrom

ABSTRACT A brief review of the characteristics of steroid binding proteins found in the plasma and in some target organs is presented, followed by some general remarks on binding »specificity« and binding parameters. Useful techniques for measuring binding parameters at equilibrium are reported, both those which keep the equilibrium intact and those which implicate its disruption. A concept is developed according to which the determination of a specific steroid binding protein is based on the »differential dissociation« of the several steroid binding complexes present in most biological mixtures. Methods which allow determination of the kinetic parameters of the binding systems are also presented. Various representations of the binding and therefore different modes of graphic representation and calculation are discussed, including the recent »proportion graph« method.


Sign in / Sign up

Export Citation Format

Share Document