Towards Peptide and Protein Recognition by Antibody Mimicking Synthetic Polymers – Background, State of the Art, and Future Outlook

2020 ◽  
Vol 73 (4) ◽  
pp. 300
Author(s):  
Ian A. Nicholls ◽  
Jesper G. Wiklander
Keyword(s):  
Protein Interactions ◽  
Structural Integrity ◽  
State Of The Art ◽  
Synthetic Polymers ◽  
Protein Recognition ◽  
Imprinted Polymer ◽  
Molecularly Imprinted ◽  
Biochemical Research ◽  
And Function ◽  
Background State

Antibody–peptide/protein interactions are instrumental for many processes in the pharmaceutical and biotechnology industries and as tools for biomedical and biochemical research. The recent development of molecularly imprinted polymer nanoparticles displaying antibody-like recognition of peptides and proteins offers the possibility for substituting antibodies with these robust materials for applications where the structural integrity and function of antibodies is compromised by temperature, pH, solvent, etc. The background to the development of this class of antibody-mimicking material and the state-of-the-art in their synthesis and application is presented in this review.

Preparation and Characterize of Konjac Glucomannan-Based Protein Molecularly Imprinted Polymer

2011 ◽  
Vol 366 ◽  
pp. 460-463
Author(s):  
Zhi Yuan Mi ◽  
Zhuo Ma ◽  
Xiao Li Li ◽  
Pan Wang ◽  
Ying Qing Zhang
Keyword(s):  
Bovine Serum Albumin ◽  
Molecularly Imprinted Polymer ◽  
Room Temperature ◽  
Konjac Glucomannan ◽  
Protein Recognition ◽  
Imprinted Polymer ◽  
Molecularly Imprinted ◽  
Recognition Experiment ◽  
Template Protein ◽  
Imprinted Membrane

Objective: To prepare a novel molecularly imprinted materials for protein recognition. Methods: Konjac glucomannan was used as fundamental materials, after swollen, added 3-Chloro-1,2- epoxypropane and glycerol cross-linked for 3 h at 40 °C. Then added bovine serum albumin (BSA) solution, agitated 1 h at room temperature. Natural dried. Results: After eluted, the imprinted efficiency of the imprinted membrane were (59.27±3.53) % (n=6) with blank membrane as control. The adsorption rate increased from 2 h to 20 h, and reached saturation at 22 to 24 h. The selectively recognition experiment indicated the BSA imprinted membrane have significant selectively recognition abilities for the template protein. Conclusions: konjac glucomannan-based imprinted membrane shows great possibilities to be a promising material for protein molecularly imprinted recognition.

Mussel-inspired molecularly imprinted polymer coating superparamagnetic nanoparticles for protein recognition

2010 ◽  
Vol 20 (5) ◽  
pp. 880-883 ◽  
Author(s):  
Wen-Hui Zhou ◽  
Chun-Hua Lu ◽  
Xiu-Chun Guo ◽  
Fa-Rong Chen ◽  
Huang-Hao Yang ◽  
...  
Keyword(s):  
Molecularly Imprinted Polymer ◽  
Polymer Coating ◽  
Superparamagnetic Nanoparticles ◽  
Protein Recognition ◽  
Imprinted Polymer ◽  
Molecularly Imprinted

scholarly journals Hybrid Aptamer‐Molecularly Imprinted Polymer (aptaMIP) Nanoparticles from Protein Recognition—A Trypsin Model

2021 ◽  
pp. 2100002
Author(s):  
Mark V. Sullivan ◽  
Oliver Clay ◽  
Michael P. Moazami ◽  
Jonathan K. Watts ◽  
Nicholas W. Turner
Keyword(s):  
Molecularly Imprinted Polymer ◽  
Protein Recognition ◽  
Imprinted Polymer ◽  
Molecularly Imprinted

Electrochemical protein recognition based on macromolecular self-assembly of molecularly imprinted polymer: a new strategy to mimic antibody for label-free biosensing

2019 ◽  
Vol 7 (14) ◽  
pp. 2311-2319 ◽  
Author(s):  
Wei Zhao ◽  
Bing Li ◽  
Sheng Xu ◽  
Xuewen Huang ◽  
Jing Luo ◽  
...  
Keyword(s):  
Molecularly Imprinted Polymer ◽  
Self Assembly ◽  
Amphiphilic Copolymer ◽  
Protein Recognition ◽  
Label Free ◽  
Imprinted Polymer ◽  
Molecularly Imprinted ◽  
New Strategy ◽  
Mip Sensor

A versatile strategy, based on the use of an amphiphilic copolymer as a macromonomer, was developed for the preparation of a fully synthetic MIP sensor for protein recognition

The organization and function of water in protein crystals

1977 ◽  
Vol 278 (959) ◽  
pp. 3-32 ◽  
Keyword(s):  
Protein Interactions ◽  
Active Sites ◽  
Structural Integrity ◽  
Bound Water ◽  
Structural Data ◽  
Protein Molecule ◽  
Biologically Active ◽  
Complex Nature ◽  
Water Molecules ◽  
And Function

Dry proteins are dead, or at best asleep. Substitution of D 2 O can drastically alter biological activity. Water is thus essential in maintaining the structural integrity of biologically active macromolecules, and is implicated in their functioning. Such water may occupy a range of dynamical states, from being strongly bound and localized, to more labile and ‘liquid-like’. Spatially ordering the macromolecules aids the search for the more localized water molecules. For example, diffraction experiments on single crystals can resolve ‘bound’ water molecules within a protein molecule - often at active sites, coordinated to metals or ions. Less precise information is obtained on the partially occupied external water sites, which are of importance to the folding and the dynamics of the biomolecule. Orientation of fibrous molecules increases the information obtainable from n.m.r. experiments. Combination of other experimental results on disordered aggregates (e.g. in solution) with chemical and structural data on the macromolecule and water itself yields useful, if circumstantial, information. Statistical and computer techniques may help to elucidate the complex nature of water-protein interactions, and to interpret the results of more complex experiments.

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