Structure of asymmetrical peptide dendrimers: Insights given by self-consistent field theory

B.M. Okrugin, I.M. Neelov, F.A.M. Leermakers, Oleg V. Borisov*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

36 Citations (Scopus)

Abstract

Structural properties of asymmetric peptide dendrimers up to the 11th generation are studied on the basis of the self-consistent field Scheutjens-Fleer numerical approach. It is demonstrated that large scale properties such as, e.g., the gyration radius, are relatively weakly affected by the asymmetry that is, by difference in the length of short and long spacers. However, the asymmetry has strong influence on the internal structure of the dendrimers and on the radial distribution of polymer density and terminal segments. In particular, symmetrical and weakly asymmetrical dendimers are characterized by quasi-uniform intramolecular concentration profiles of monomer units whereas strongly asymmetric dendrimers are characterized by sharply decreasing in a radial direction polymer density profile reminiscent to that in star-shaped polymers. This finding may have important implication for the use of peptide dendrimers as carriers for biologically active molecules.
Original languageEnglish
Pages (from-to)292-302
JournalPolymer
Volume125
DOIs
Publication statusPublished - 2017

Keywords

  • Dendrimers
  • Poly(l)-lysine
  • Self-consistent field theory

Fingerprint

Dive into the research topics of 'Structure of asymmetrical peptide dendrimers: Insights given by self-consistent field theory'. Together they form a unique fingerprint.

Cite this