Relationship between conformation and physicochemical properties of polypeptides. II. GPC as a tool for the detection of conformational transitions of PEG‐bound peptides

Schmitt, Johannes; Mutter, Manfred

doi:10.1002/bip.360220803

Cited by 9 publications

(1 citation statement)

References 4 publications

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“…Self‐assembly in these biomimetic copolymers is a result of the hydrophobic/hydrophilic balance in addition to secondary structure interactions 19, 20. For example, valine sequences that are covalently attached to polymers can self‐assemble to form β‐sheet structures 21, 22…”

Section: Introductionmentioning

confidence: 99%

Self‐assembly of di‐ and triblock PEG‐pentavaline amphiphiles

Hwang

Wilson-Hill

Ahn

et al. 2010

J. Polym. Sci. A Polym. Chem.

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Nanoparticles formed from amphiphilic block copolymers can be used as drug delivery vehicles for hydrophilic therapeutics. Poly(ethylene glycol) (PEG)-peptide copolymers were investigated for their self-assembling properties and as consequent potential delivery systems. Mono-and dihydroxy PEGs were functionalized with a pentavaline sequence bearing Fmoc end groups. The molecular weight of the PEG component was varied to evaluate copolymer size and block number. These di-and tri-block copolymers readily self-assemble in aqueous solution with critical aggregation concentrations (CACs) of 0.46-16.29 lM. At concentrations above the CAC, copolymer solutions form spherical assemblies. Dynamic light scattering studies indicate these aggregates have a broad size distribution, with average diameters between 33 and 127 nm. The copolymers are comprised b-conformations that are stable up to 80 C, as observed by circular dichroism. This peptide secondary structure is retained in solutions up to 50% MeOH as well. The triblock copolymers proved to be the most stable, with copolymers synthesized from 10 kDa PEG having the most stable particles. Loading of carboxyfluorescein at 2-5 mol % shows that these copolymers have the potential to encapsulate hydrophilic drugs for delivery applications. V C 2010 Wiley Periodicals, Inc. J Polym Sci Part A: Polym Chem 49: 871-878, 2011

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Section: Introductionmentioning

confidence: 99%

Self‐assembly of di‐ and triblock PEG‐pentavaline amphiphiles

Hwang

Wilson-Hill

Ahn

et al. 2010

J. Polym. Sci. A Polym. Chem.

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Die Konstruktion von neuen Proteinen und Enzymen - eine Zukunftsperspektive?

Mutter

1985

Angew. Chem.

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The Construction of New Proteins and Enzymes‐a Prospect for the Future?

Mutter

1985

Angew. Chem. Int. Ed. Engl.

101

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Dedicated to Professor Paul J. FIory on the occasion of his 75th birthday Only a vanishingly small proportion of the almost infinite number of possible proteins occur in nature. Can this remaining potential of structural and functional diversity be used in the construction of new proteins? Is a "second evolution" of proteins and enzymes about to occur? These questions have suddenly become of interest because the recombinant DNA technique allows the synthesis of any given amino acid sequence. Examples of enzyme models demonstrate clearly that the unusual catalytic properties of enzymes are associated with the presence of a specifically folded polypeptide chain which has a complex three-dimensional form. The critical hurdle in the path of artificial proteins is thus the design of amino acid sequences which are able to fold into tertiary structures.-Recent studies on the topology and the mechanism of folding have provided considerable insight into the occurrence of, and the rules governing the three-dimensional architecture of proteins. Secondary structures apparently play a key role in the folding process; helices and "b-structures" act as nucleation centers directing folding and account for the surprisingly small number of different folding topologies. The problem of secondary structure formation can be investigated directly by means of conformational studies on model peptides. Oligopeptides with tailormade physicochemical, structural and conformational properties can already be designed. The theoretical and experimental basis for the construction of polypeptides with stable tertiary structures is therefore established. The path to macromolecules with an immense variety of novel properties lays before us.

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Relationship between conformation and physicochemical properties of polypeptides. II. GPC as a tool for the detection of conformational transitions of PEG‐bound peptides

Cited by 9 publications

References 4 publications

Self‐assembly of di‐ and triblock PEG‐pentavaline amphiphiles

Self‐assembly of di‐ and triblock PEG‐pentavaline amphiphiles

Die Konstruktion von neuen Proteinen und Enzymen - eine Zukunftsperspektive?

The Construction of New Proteins and Enzymes‐a Prospect for the Future?

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