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Related Concept Videos

Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
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Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.

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A Facile and Efficient Approach for the Production of Reversible Disulfide Cross-linked Micelles
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A Facile and Efficient Approach for the Production of Reversible Disulfide Cross-linked Micelles

Published on: December 23, 2016

Functional disulfide-stabilized polymer-protein particles.

Zhongfan Jia1, Jingquan Liu, Cyrille Boyer

  • 1Centre for Advanced Macromolecular Design (CAMD), School of Chemical Sciences and Engineering, The University of New South Wales (UNSW), Sydney, NSW 2052, Australia.

Biomacromolecules
|October 1, 2009
PubMed
Summary
This summary is machine-generated.

We developed versatile polymer-protein hybrid particles (PPHPs) for drug delivery and imaging. These disulfide cross-linked, poly(ethylene glycol)-streptavidin particles offer tunable sizes and functional surfaces for targeted applications.

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Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Polymer Chemistry

Background:

  • Polymer-protein hybrid particles (PPHPs) show promise in drug delivery, diagnostics, and biomedical imaging.
  • Existing PPHPs often require complex synthesis or lack tunable properties for specific applications.

Purpose of the Study:

  • To develop a straightforward method for creating disulfide cross-linked, poly(ethylene glycol)-streptavidin hybrid particles with controllable dimensions.
  • To engineer PPHPs with accessible biotin-binding sites for versatile bioconjugation and functional core for drug/label attachment.

Main Methods:

  • Synthesis of alpha-biotin PEG-b-poly(pyridyldisulfide ethylmethacrylate) block copolymers via RAFT polymerization.
  • One-pot micellization, disulfide cross-linking, and core functionalization using a thiol-reactive maleimide fluorophore.
  • Characterization of particle morphology, size, biotin availability (streptavidin/HABA assay), and streptavidin decoration via TEM and confocal microscopy.

Main Results:

  • Spherical micelles with a diameter of 54 ± 4 nm were formed, featuring a biotinylated poly(ethylene glycol) corona and a disulfide cross-linked core.
  • High biotin availability (75 mol %) on the micelle surface was confirmed, enabling efficient streptavidin conjugation.
  • Streptavidin-decorated PPHPs formed aggregates with tunable sizes ranging from 350 nm to 2 µm, with streptavidin localized on the particle periphery.

Conclusions:

  • A facile method for producing tunable, disulfide cross-linked polymer-protein hybrid particles with accessible streptavidin-binding sites was established.
  • These PPHPs offer significant versatility for applications in drug delivery, diagnostics, and imaging due to their functionalizable surface and core.
  • The tunable dimensions and controlled surface functionalization of these hybrid particles make them promising candidates for advanced biomedical applications.