Methoxypoly(ethylene glycol)-conjugated carboxypeptidase A for solid tumor targeting

Ton, Giangthy N.; Weichert, Jamey P.; Longino, Marc A.; Fine, Jason P.; Kwon, Glen S.

doi:10.1016/j.jconrel.2005.01.015

Cited by 7 publications

(1 citation statement)

References 21 publications

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“…PEGylation is known to extend the circulation times of therapeutically important species in the blood stream (24). Additionally, PEGylated proteins with low levels of PEGylation are very useful as homing signals on drug-loaded liposomes (25). In this context, it may be highly desirable to mono-PEGylate proteins as over PEGylation could interfere with intercalation into the liposome.…”

Section: Discussionmentioning

confidence: 99%

Sortase A as a Novel Molecular “Stapler” for Sequence-Specific Protein Conjugation

2007

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The Sortase family of transpeptidase enzymes catalyzes sequence-specific ligation of proteins to the cell wall of Gram-positive bacteria. Here, we describe the application of recombinant Staphylococcus aureus Sortase A to attach a tagged model protein substrate (green fluorescent protein) to polystyrene beads chemically modified with either alkylamine or the in vivo Sortase A ligand, Gly-Gly-Gly, on their surfaces. Furthermore, we show that Sortase A can be used to sequence-specifically ligate eGFP to amino-terminated poly(ethylene glycol) and to generate protein oligomers and cyclized monomers using suitably tagged eGFP. We find that an alkylamine can substitute for the natural Gly3 substrate, which suggests the possibility of using the enzyme in materials applications. The highly specific and mild Sortase A-catalyzed reaction, based on small recognition tags unlikely to interfere with protein expression, thus represents a useful addition to the protein immobilization and modification tool kit.

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Section: Discussionmentioning

confidence: 99%

Sortase A as a Novel Molecular “Stapler” for Sequence-Specific Protein Conjugation

2007

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Modulation of protein biophysical properties by chemical glycosylation: biochemical insights and biomedical implications

Solá

Rodríguez‐Martínez

Griebenow

2007

Cell. Mol. Life Sci.

115

135

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Glycosylation constitutes one of the most important posttranslational modifications employed by biological systems to modulate protein biophysical properties. Due to the direct biochemical and biomedical implications of achieving control over protein stability and function by chemical means, there has been great interest in recent years towards the development of chemical strategies for protein glycosylation. Since current knowledge about glycoprotein biophysics has been mainly derived from the study of naturally glycosylated proteins, chemical glycosylation provides novel insights into its mechanistic understanding by affording control over glycosylation parameters. This review presents a survey of the effects that natural and chemical glycosylation have on the fundamental biophysical properties of proteins (structure, dynamics, stability, and function). This is complemented by a mechanistic discussion of how glycans achieve such effects and discussion of the implications of employing chemical glycosylation as a tool to exert control over protein biophysical properties within biochemical and biomedical applications.

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Single enzyme nanoparticle, an effective tool for enzyme replacement therapy

et al. 2020

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Methoxypoly(ethylene glycol)-conjugated carboxypeptidase A for solid tumor targeting

Cited by 7 publications

References 21 publications

Sortase A as a Novel Molecular “Stapler” for Sequence-Specific Protein Conjugation

Sortase A as a Novel Molecular “Stapler” for Sequence-Specific Protein Conjugation

Modulation of protein biophysical properties by chemical glycosylation: biochemical insights and biomedical implications

Single enzyme nanoparticle, an effective tool for enzyme replacement therapy

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