Limits...
Overview of the main methods used to combine proteins with nanosystems: absorption, bioconjugation, and encapsulation.

Di Marco M, Shamsuddin S, Razak KA, Aziz AA, Devaux C, Borghi E, Levy L, Sadun C - Int J Nanomedicine (2010)

Bottom Line: Interactions of nanoparticles with biomolecules and caveats related to protein denaturation are also pointed out.A clear understanding of nanoparticle-protein interactions could make possible the design of precise and versatile hybrid nanosystems.This could further allow control of their pharmacokinetics as well as activity, and safety.

View Article: PubMed Central - PubMed

Affiliation: Nanobiotix, 60 rue de Wattignies, Paris, France. maria.dimarco@nanobiotix.com

ABSTRACT
The latest development of protein engineering allows the production of proteins having desired properties and large potential markets, but the clinical advances of therapeutical proteins are still limited by their fragility. Nanotechnology could provide optimal vectors able to protect from degradation therapeutical biomolecules such as proteins, enzymes or specific polypeptides. On the other hand, some proteins can be also used as active ligands to help nanoparticles loaded with chemotherapeutic or other drugs to reach particular sites in the body. The aim of this review is to provide an overall picture of the general aspects of the most successful approaches used to combine proteins with nanosystems. This combination is mainly achieved by absorption, bioconjugation and encapsulation. Interactions of nanoparticles with biomolecules and caveats related to protein denaturation are also pointed out. A clear understanding of nanoparticle-protein interactions could make possible the design of precise and versatile hybrid nanosystems. This could further allow control of their pharmacokinetics as well as activity, and safety.

Show MeSH
The introduction of sulfhydryl groups by: 3) Quenching of reactive protein aldehyde residues with cystaminiumdichloride reagents or 4) coupling of cystaminiumdichloride to carboxyl groups via 1-ethyl-3-(3-dimethyl-aminopropyl)carbodiimide (EDC); both cases followed by the disulfide bonds reduction with DTT.
© Copyright Policy
Related In: Results  -  Collection


getmorefigures.php?uid=PMC2819905&req=5

f1b-ijn-5-037: The introduction of sulfhydryl groups by: 3) Quenching of reactive protein aldehyde residues with cystaminiumdichloride reagents or 4) coupling of cystaminiumdichloride to carboxyl groups via 1-ethyl-3-(3-dimethyl-aminopropyl)carbodiimide (EDC); both cases followed by the disulfide bonds reduction with DTT.

Mentions: When protein does not have the suitable residue necessary for the specific conjugation, the most common way to get it is the chemical introduction of sulfhydryl groups. This process (Figures 1a and 1b) can be mainly made by the following four methods: 1) reduction of protein disulfide bonds using reductive agents such as dithiotreitol (DTT = Clelands reagent). 2) Coupling of protein primary amino groups with 2-iminothiolane (Trauts reagent). 3) Quenching of reactive protein aldehyde residues with cystaminiumdichloride reagents or 4) coupling of cystaminiumdichloride to carboxyl groups via 1-ethyl-3-(3-dimethyl-aminopropyl)carbodiimide (EDC); both cases followed by the disulfide bonds reduction with DTT as outlined above.112,120–123


Overview of the main methods used to combine proteins with nanosystems: absorption, bioconjugation, and encapsulation.

Di Marco M, Shamsuddin S, Razak KA, Aziz AA, Devaux C, Borghi E, Levy L, Sadun C - Int J Nanomedicine (2010)

The introduction of sulfhydryl groups by: 3) Quenching of reactive protein aldehyde residues with cystaminiumdichloride reagents or 4) coupling of cystaminiumdichloride to carboxyl groups via 1-ethyl-3-(3-dimethyl-aminopropyl)carbodiimide (EDC); both cases followed by the disulfide bonds reduction with DTT.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2819905&req=5

f1b-ijn-5-037: The introduction of sulfhydryl groups by: 3) Quenching of reactive protein aldehyde residues with cystaminiumdichloride reagents or 4) coupling of cystaminiumdichloride to carboxyl groups via 1-ethyl-3-(3-dimethyl-aminopropyl)carbodiimide (EDC); both cases followed by the disulfide bonds reduction with DTT.
Mentions: When protein does not have the suitable residue necessary for the specific conjugation, the most common way to get it is the chemical introduction of sulfhydryl groups. This process (Figures 1a and 1b) can be mainly made by the following four methods: 1) reduction of protein disulfide bonds using reductive agents such as dithiotreitol (DTT = Clelands reagent). 2) Coupling of protein primary amino groups with 2-iminothiolane (Trauts reagent). 3) Quenching of reactive protein aldehyde residues with cystaminiumdichloride reagents or 4) coupling of cystaminiumdichloride to carboxyl groups via 1-ethyl-3-(3-dimethyl-aminopropyl)carbodiimide (EDC); both cases followed by the disulfide bonds reduction with DTT as outlined above.112,120–123

Bottom Line: Interactions of nanoparticles with biomolecules and caveats related to protein denaturation are also pointed out.A clear understanding of nanoparticle-protein interactions could make possible the design of precise and versatile hybrid nanosystems.This could further allow control of their pharmacokinetics as well as activity, and safety.

View Article: PubMed Central - PubMed

Affiliation: Nanobiotix, 60 rue de Wattignies, Paris, France. maria.dimarco@nanobiotix.com

ABSTRACT
The latest development of protein engineering allows the production of proteins having desired properties and large potential markets, but the clinical advances of therapeutical proteins are still limited by their fragility. Nanotechnology could provide optimal vectors able to protect from degradation therapeutical biomolecules such as proteins, enzymes or specific polypeptides. On the other hand, some proteins can be also used as active ligands to help nanoparticles loaded with chemotherapeutic or other drugs to reach particular sites in the body. The aim of this review is to provide an overall picture of the general aspects of the most successful approaches used to combine proteins with nanosystems. This combination is mainly achieved by absorption, bioconjugation and encapsulation. Interactions of nanoparticles with biomolecules and caveats related to protein denaturation are also pointed out. A clear understanding of nanoparticle-protein interactions could make possible the design of precise and versatile hybrid nanosystems. This could further allow control of their pharmacokinetics as well as activity, and safety.

Show MeSH