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  Exploiting oligo(amido amine) backbones for the multivalent presentation of coiled-coil peptides

Gerling-Driessen, U. I. M., Mujkic-Ninnemann, N., Ponader, D., Schöne, D., Hartmann, L., & Koksch, B. (2015). Exploiting oligo(amido amine) backbones for the multivalent presentation of coiled-coil peptides. Biomacromolecules, 16(8), 2394-2402. doi:10.1021/acs.biomac.5b00634.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0027-BD6F-7 Version Permalink: https://hdl.handle.net/21.11116/0000-0007-E286-2
Genre: Journal Article

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 Creators:
Gerling-Driessen, Ulla I. M., Author
Mujkic-Ninnemann, Nina1, Author           
Ponader, Daniela1, Author           
Schöne, Daniel, Author
Hartmann, Laura1, Author           
Koksch, Beate, Author
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1Laura Hartmann, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863305              

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 Abstract: The investigation of coiled coil formation for one mono- and two divalent peptide-polymer conjugates is presented. Through the assembly of the full conjugates on solid support, monodisperse sequence-defined conjugates are obtained with defined positions and distances between the peptide side chains along the polymeric backbone. A heteromeric peptide design was chosen, where peptide K is attached to the polymer backbone and coiled coil formation is only expected through complexation with the complementary peptide E. Indeed, the monovalent peptide K-polymer conjugate displays rapid coiled coil formation when mixed with the complementary peptide E sequence. The divalent systems show intramolecular homomeric coiled coil formation on the polymer backbone despite the peptide design. Interestingly, this intramolecular assembly undergoes a conformational rearrangement by the addition of the complementary peptide E leading to the formation of heteromeric coiled coil-polymer aggregates. The polymer backbone acts as a template bringing the covalently bound peptide strands in close proximity to each other, increasing the local concentration and inducing the otherwise non-favorable formation of intramolecular helical assemblies.

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 Dates: 2015-06-262015
 Publication Status: Issued
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 Identifiers: DOI: 10.1021/acs.biomac.5b00634
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Title: Biomacromolecules
  Other : Biomacromolecules
Source Genre: Journal
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Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 16 (8) Sequence Number: - Start / End Page: 2394 - 2402 Identifier: ISSN: 1525-7797