Synthetic mimetics of protein secondary structure domains

Nathan T. Ross, William P. Katt, Andrew Hamilton

Research output: Contribution to journalArticle

Abstract

Proteins modulate the majority of all biological functions and are primarily composed of highly organized secondary structural elements such as helices, turns and sheets. Many of these functions are affected by a small number of key protein-protein contacts, often involving one or more of these well-defined structural elements. Given the ubiquitous nature of these protein recognition domains, their mimicry by peptidic and non-peptidic scaffolds has become a major focus of contemporary research. This review examines several key advances in secondary structure mimicry over the past several years, particularly focusing upon scaffolds that show not only promising projection of functional groups, but also a proven effect in biological systems.

Original languageEnglish (US)
Pages (from-to)989-1008
Number of pages20
JournalPhilosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences
Volume368
Issue number1914
DOIs
StatePublished - Mar 13 2010

Fingerprint

Protein Structure
Secondary Structure
proteins
Proteins
Protein
Scaffold
Scaffolds
Biological systems
Helix
Biological Systems
helices
Functional groups
Well-defined
projection
Projection
Contact

Keywords

  • α-helix mimetics
  • β-peptides
  • Protein mimetics
  • Stapled peptides
  • Terphenyl

ASJC Scopus subject areas

  • Engineering(all)
  • Mathematics(all)
  • Physics and Astronomy(all)

Cite this

Synthetic mimetics of protein secondary structure domains. / Ross, Nathan T.; Katt, William P.; Hamilton, Andrew.

In: Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences, Vol. 368, No. 1914, 13.03.2010, p. 989-1008.

Research output: Contribution to journalArticle

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