Jump to main content
Jump to site search

Issue 13, 2012
Previous Article Next Article

Determination of the persistence length of helical and non-helical polypeptoids in solution

Author affiliations

Abstract

Control over the shape of a polymer chain is desirable from a materials perspective because polymer stiffness is directly related to chain characteristics such as liquid crystallinity and entanglement, which in turn are related to mechanical properties. However, the relationship between main chain helicity in novel biologically derived and inspired polymers and chain stiffness (persistence length) is relatively poorly understood. Polypeptoids, or poly(N-substituted glycines), constitute a modular, biomimetic system that enables precise tuning of chain sequence and are therefore a good model system for understanding the interrelationship between monomer structure, helicity, and persistence length. The incorporation of bulky chiral monomers is known to cause main chain helicity in polypeptoids. Here, we show that helical polypeptoid chains have a flexibility nearly identical to an analogous random coil polypeptoid as observed via small angle neutron scattering (SANS). Additionally, our findings show that polypeptoids with aromatic phenyl side chains are inherently flexible with persistence lengths ranging from 0.5 to 1 nm.

Graphical abstract: Determination of the persistence length of helical and non-helical polypeptoids in solution

Back to tab navigation

Supplementary files

Publication details

The article was received on 02 Nov 2011, accepted on 23 Jan 2012 and first published on 20 Feb 2012


Article type: Paper
DOI: 10.1039/C2SM07092H
Citation: Soft Matter, 2012,8, 3673-3680
  •   Request permissions

    Determination of the persistence length of helical and non-helical polypeptoids in solution

    A. M. Rosales, H. K. Murnen, S. R. Kline, R. N. Zuckermann and R. A. Segalman, Soft Matter, 2012, 8, 3673
    DOI: 10.1039/C2SM07092H

Search articles by author

Spotlight

Advertisements