5 years ago

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

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

Publisher URL: www.sciencedirect.com/science

DOI: S0032386117307280

You might also like
Discover & Discuss Important Research

Keeping up-to-date with research can feel impossible, with papers being published faster than you'll ever be able to read them. That's where Researcher comes in: we're simplifying discovery and making important discussions happen. With over 19,000 sources, including peer-reviewed journals, preprints, blogs, universities, podcasts and Live events across 10 research areas, you'll never miss what's important to you. It's like social media, but better. Oh, and we should mention - it's free.

  • Download from Google Play
  • Download from App Store
  • Download from AppInChina

Researcher displays publicly available abstracts and doesn’t host any full article content. If the content is open access, we will direct clicks from the abstracts to the publisher website and display the PDF copy on our platform. Clicks to view the full text will be directed to the publisher website, where only users with subscriptions or access through their institution are able to view the full article.