Noncovalent template-assisted mimicry of multiloop protein surfaces

Assembling discontinuous and functional domains

Partha S. Ghosh, Andrew Hamilton

Research output: Contribution to journalArticle

Abstract

We report here a novel noncovalent synthetic strategy for template-assembled de novo protein design. In this approach, a peptide was first conjugated with two oligoguanosine strands via click chemistry and the conjugates were then self-assembled in the presence of metal ions. G-quadruplex formation directs two peptide strands to assemble on one face of the scaffold and form an adjacent two loop surface. This approach can be used to rapidly prepare multiple two-loop structures with both homo- and heterosequences.

Original languageEnglish (US)
Pages (from-to)13208-13211
Number of pages4
JournalJournal of the American Chemical Society
Volume134
Issue number32
DOIs
StatePublished - Aug 15 2012

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Peptides
Membrane Proteins
Click Chemistry
G-Quadruplexes
Proteins
Forms (concrete)
Scaffolds
Metal ions
Metals
Ions

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Noncovalent template-assisted mimicry of multiloop protein surfaces : Assembling discontinuous and functional domains. / Ghosh, Partha S.; Hamilton, Andrew.

In: Journal of the American Chemical Society, Vol. 134, No. 32, 15.08.2012, p. 13208-13211.

Research output: Contribution to journalArticle

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