Preparation ofde NovoGlobular Proteins Based on Proline Dendrimers
The Journal of Organic Chemistry2005Vol. 70(16), pp. 6274–6281
Citations Over Time
Abstract
A synthetic method for the preparation of protein-like globular dendrimers derived from a combination of proline, glycine and imidazolidin ring as branching unit is described. The methodology allows the synthesis of novel peptide dendrimers up to fourth generation. Dendrimers were synthesized by a convergent solid-phase peptide synthesis approach. The conformational properties of branched polyproline peptides and proline dendrimers were studied by CD experiments. CD data suggest conformational plasticity of branched peptides for PPI and PPII, and a stable well-defined secondary structure of proline dendrimers for PPII.
Related Papers
- → Omnipresence of the polyproline II helix in fibrous and globular proteins(2016)15 cited
- → Solid-phase dendrimer synthesis(1998)72 cited
- → Solid‐phase synthesis of second‐generation polyproline dendrimers(2004)28 cited
- [Left-handed helix conformation of poly-L-proline II type in globular proteins. Statistics of incidence and a role of sequence].(2001)
- [Left-helical (PPII-PPII) type of globular protein structure: the level of the left helical type of poly-L-proline II in Kunitz trypsin inhibitor is no less than 43%. Experimental Reper spectrum of the extended left helix].(1995)