Associative diblock copolymers of poly(ethylene glycol) and coiled-coil peptides

Pechar, Michal; Kopečková, Pavla; Joss, Lisa; Kopeček, Jindřich

doi:10.1002/1616-5195(200206)2:5<199::aid-mabi199>3.0.co;2-2

Cited by 110 publications

(132 citation statements)

References 27 publications

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“…35 Although PEG-ylation was found to proceed quantitatively for the lowest molar mass PEG-ylating agent, only approximately 40% of the peptide segments were modified when the PEG-ylation was carried out with the high-molar-mass PEG derivative. Kopeček et al 36 followed a slightly different approach. In this case, peptide synthesis was performed on a 2-chlorotrityl resin.…”

Section: Methodssupporting

confidence: 41%

“…Recently, we 35 and others 36 have prepared block copolymers of coiled-coil peptide sequences and PEG with procedures based on the strategies developed by Felix and Lu. In our own work, the Fmoc solid-phase synthesis of the desired peptide sequence on a Rink amide resin was followed by on-bead benzotriazole-1-yloxytris(pyrrolidino)phosphosium hexafluorophosphate mediated acylation of the N-terminal glycine residue with carboxylic acid functionalized mPEG derivatives with molecular weights of 750 and 2000 g/mol.…”

Section: Methodsmentioning

confidence: 48%

“…62,63 Recently, we and others have explored the coiled-coil motif to direct the self-assembly of PEGbased hybrid block copolymers. 35,36 Circular dichroism and analytical ultracentrifugation experiments have indicated that the coiled-coil sequences mediate the formation of essentially uniform nanoobjects, in which a core composed of a discrete number of ␣-helical peptides is closely encapsulated in a PEG shell. 64 A particularly interesting feature of these hybrid block copolymers is that the aggregation number and pH sensitivity of the nanoobjects can be controlled via directed single and double mutations of the peptide primary structure.…”

Section: Self-assembly and Supramolecular Architecturesmentioning

confidence: 44%

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Biological–synthetic hybrid block copolymers: Combining the best from two worlds

Klok

2004

J. Polym. Sci. A Polym. Chem.

276

142

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ABSTRACT:Although biopolymers and synthetic polymers share many common features, each of these two classes of materials is also characterized by a distinct and very specific set of advantages and disadvantages. Combining biopolymer elements with synthetic polymers into a single macromolecular conjugate is an interesting strategy for synergetically merging the properties of the individual components and overcoming some of their limitations. This article focuses on a special class of biological-synthetic hybrids that are obtained by site-selective conjugation of a protein or peptide and a synthetic polymer. The first part of the article gives an overview of the different liquid-phase and solidphase techniques that have been developed for the synthesis of well-defined, that is, site-selectively conjugated, synthetic polymer-protein hybrids. In the second part, the properties and potential applications of these materials are discussed. The conjugation of biological and synthetic macromolecules allows the modulation of protein binding and recognition properties and is a powerful strategy for mediating the self-assembly of synthetic polymers. Synthetic polymer-protein hybrids are already used as medicines and show significant promise for bioanalytical applications and bioseparations.

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Section: Methodssupporting

confidence: 41%

Section: Methodsmentioning

confidence: 48%

Section: Self-assembly and Supramolecular Architecturesmentioning

confidence: 44%

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Biological–synthetic hybrid block copolymers: Combining the best from two worlds

Klok

2004

J. Polym. Sci. A Polym. Chem.

276

142

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“…Such an increase was also observed for other peptide/synthetic block copolymers because of the aggregation of polypeptide segments in micelles [10][11][12][13] and in microphase-segregated structures. 6,7 In PS n -C-PBLG m , however, there was a decrease in the helical content of the PBLG segment in 0.7-3.6 vol% TFA after attachment of a PS segment to the C terminus.…”

Section: Resultsmentioning

confidence: 50%

“…Similar observations have been reported for block copolymers composed of a-helical polypeptide and PEO segments in water or hydrophobic solvents. [10][11][12][13] In bulk, Lecommendoux et al 6,7 reported that the attachment of an oligomeric polystyrene (PS) to an oligomeric poly(g-benzyl-L-glutamate) (PBLG) resulted in a significant stabilization of the helical structure. In contrast, Kugo et al 14 reported that the helical content of PBLG in solid-state PBLG/ PEO/PBLG triblock copolymers decreased gradually as the polymers swelled in the presence of water.…”

Section: Introductionmentioning

confidence: 46%

Helix–coil transformation of poly(γ-benzyl-L-glutamate) with polystyrene attached to the N or C terminus in trifluoroacetic acid–chloroform mixtures

Itoh

Hatanaka

Ihara

et al. 2011

Polym J

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The helix-coil transformations of block copolymers composed of poly(c-benzyl-L-glutamate) (PBLG) and polystyrene (PS), in which PS was attached to either the N terminus (PBLG n -N-PS m ) or the C terminus (PS n -C-PBLG m ) of PBLG, were investigated in trifluoroacetic acid (TFA)-chloroform mixtures with TFA concentrations in the range of 0.7-10 vol%. The helical content (f H ) estimated from 1 H nuclear magnetic resonance measurements indicated that the PBLG segment in PBLG 55 -N-PS 160 underwent a gradual helix-coil transformation from f H ¼1 to f H ¼0.75 over the range of 3.6-5.7 vol% TFA and then a drastic transformation to f H ¼0 at 9.5 vol% TFA, in a manner similar to that of the PBLG 55 homopolymer. In PS 120 -C-PBLG 55 , the helical deformation of the PBLG segment was observed by adding a very small amount of TFA (0.7-3.6 vol%), followed by gradual and drastic transformations at higher TFA concentrations. The results indicate that the conformational stability of the C terminus in a PBLG chain differs from that of the N terminus. Transformations of PBLG/PS block copolymers with various molecular weights and compositions were also studied.

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Protein‐Polymer Conjugates

Briand¹,

Kumar²,

Kasi³

2011

Encyclopedia of Polymer Science and Technology

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This chapter focuses on the design and applications of protein‐polymer conjugates. Protein‐polymer conjugates are synthesized by conjugating a polymer chain or many polymer chains onto a protein. The site of conjugation, protein, polymer, and stoichiometry are important criteria when designing a protein‐polymer conjugate. The important structural aspects and functions of proteins, such as hierarchical structure and activity, are discussed. The various methods of site‐specific conjugation, “grafting to”, “grafting from” and cofactor reconstitution, are included along the pros and cons of each method. Conjugates synthesized by random conjugation are also discussed. The specific reactions used for protein attachment are not included, as numerous synthetic reviews exist; however, a broad overview of the field is presented. Novel conjugate structures can be synthesized by attaching synthetic peptide sequences onto polymers. In addition to design considerations, the range of applications from drug delivery systems to biosensors are discussed. This chapter aims to aid in furthering the knowledge and growth of the synergistic combination of proteins and polymers.

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Associative diblock copolymers of poly(ethylene glycol) and coiled-coil peptides

Cited by 110 publications

References 27 publications

Biological–synthetic hybrid block copolymers: Combining the best from two worlds

Biological–synthetic hybrid block copolymers: Combining the best from two worlds

Helix–coil transformation of poly(γ-benzyl-L-glutamate) with polystyrene attached to the N or C terminus in trifluoroacetic acid–chloroform mixtures

Protein‐Polymer Conjugates

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