Work

Water-Soluble Polypeptides with Elongated, Charged Side Chains Adopt Ultrastable Helical Conformations

Year: 2011

Type: article

Abstract: Water-soluble polypeptides adopting α-helical conformations with unprecedented high helicities were obtained by elongating the charge-containing side chains of the constituent amino acids to allow the terminal charges to be situated distally from the peptide backbone. Poly(γ-(4-aminoethylthiopropoxyl)-benzyl-(L)-glutamate) (PAOBLG-AET) with a charge-peptide backbone distance of 17 σ-bonds exhibited a remarkably high helical content (81%) at a degree of polymerization as low as 10. The helical conformations of these short polypeptides were very stable against various harsh, protein-denaturing conditions, such as extreme pH, high temperature, and high salt or urea concentrations.

Source: Macromolecules

DOI: 10.1021/ma201678r

Authors: Yanfeng Zhang, Hua Lu, Yao Lin, Jianjun Cheng

Institutions: University of Illinois Urbana-Champaign, University of Connecticut

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of Biomedical Imaging and Bioengineering

Awards: Developing Clinically Applicable, Cancer-Targeting Polymeric Nanoconjugates, Development of Functional Poly(alpha-hydroxy acids) for Drug Delivery Application