Jump to main content
Jump to site search

Issue 20, 2011
Previous Article Next Article

Structural properties of soluble peptide amphiphile micelles

Author affiliations


Peptide amphiphiles (PAs) self-assemble into dynamic micellar structures that provide a multivalent display of functional peptides and are currently being developed for use in a wide range of therapeutic and diagnostic applications. This review focuses on the physical properties of PA assemblies that remain soluble under physiological conditions, termed protein analogous micelles. The relationship between PA monomer design, secondary structure, and the resulting micelle size and shape is examined, highlighting the complex balance of forces between the hydrophobic tail and the peptide headgroup. Micelle stability is also discussed, as stability is an important factor which will dictate the circulation behavior of micelles and their interaction with various tissues and cells. Analysis of different PA systems reveals methods for controlling micelle structure and stability, demonstrating how the physical properties of PA micelles can be tailored for specific applications.

Graphical abstract: Structural properties of soluble peptide amphiphile micelles

Back to tab navigation

Publication details

The article was received on 10 May 2011, accepted on 01 Aug 2011 and first published on 05 Sep 2011

Article type: Review Article
DOI: 10.1039/C1SM05862B
Citation: Soft Matter, 2011,7, 9572-9582
  •   Request permissions

    Structural properties of soluble peptide amphiphile micelles

    A. Trent, R. Marullo, B. Lin, M. Black and M. Tirrell, Soft Matter, 2011, 7, 9572
    DOI: 10.1039/C1SM05862B

Search articles by author