Literature DB >> 19053200

Alpha-helix stabilization within a peptide dendrimer.

Sacha Javor1, Antonino Natalello, Silvia Maria Doglia, Jean-Louis Reymond.   

Abstract

The alpha-helical second generation peptide dendrimer of sequence (AcAMEA)(4)(KKLME)(2)KMKLA is more stable than the corresponding linear peptide AcAMEAAKLMEAMKLA toward pH-induced unfolding and temperature-induced intermolecular aggregation. The effect is interpreted in terms of an alpha-helix spanning across two successive branching points of the dendrimer. This stabilization effect is unprecedented and opens the way to folded dendritic analogues of proteins using natural amino acids only.

Mesh:

Substances:

Year:  2008        PMID: 19053200     DOI: 10.1021/ja8076236

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN: 0002-7863            Impact factor:   15.419


  2 in total

1.  Rational development of a strategy for modifying the aggregatibility of proteins.

Authors:  Zhongping Tan; Shiying Shang; Samuel J Danishefsky
Journal:  Proc Natl Acad Sci U S A       Date:  2011-02-28       Impact factor: 11.205

2.  Glycine-spacers influence functional motifs exposure and self-assembling propensity of functionalized substrates tailored for neural stem cell cultures.

Authors:  Francesca Taraballi; Antonino Natalello; Marcello Campione; Omar Villa; Silvia M Doglia; Alberto Paleari; Fabrizio Gelain
Journal:  Front Neuroeng       Date:  2010-02-08
  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.