Self-assembly of α-helical polypeptides driven by complex coacervation.
Reported is the ability of α-helical polypeptides to self-assemble with oppositely-charged polypeptides to form liquid complexes while maintaining their α-helical secondary structure. Coupling the α-helical polypeptide to a neutral, hydrophilic polymer and subsequent complexation enables the formation of nanoscale coacervate-core micelles. While previous reports on polypeptide complexation demonstrated a critical dependence of the nature of the complex (liquid versus solid) on chirality, the α-helical structure of the positively charged polypeptide prevents the formation of β-sheets, which would otherwise drive the assembly into a solid state, thereby, enabling coacervate formation between two chiral components. The higher charge density of the assembly, a result of the folding of the α-helical polypeptide, provides enhanced resistance to salts known to inhibit polypeptide complexation. The unique combination of properties of these materials can enhance the known potential of fluid polypeptide complexes for delivery of biologically relevant molecules.
Institute for Molecular Engineering, University of Chicago, Chicago, IL 60637 (USA).
Dimitrios
D
Priftis
Institute for Molecular Engineering, University of Chicago, Chicago, IL 60637 (USA).
Lorraine
L
Leon
Department of Materials Science and Engineering, University of Illinois at Urbana-Champaign, Urbana, IL 61801 (USA).
Ziyuan
Z
Song
Institute for Molecular Engineering, University of Chicago, Chicago, IL 60637 (USA).
Sarah L
SL
Perry
Institute for Molecular Engineering, University of Chicago, Chicago, IL 60637 (USA).
Khatcher O
KO
Margossian
Institute for Molecular Engineering, University of Chicago, Chicago, IL 60637 (USA).
Anna
A
Tropnikova
Department of Materials Science and Engineering, University of Illinois at Urbana-Champaign, Urbana, IL 61801 (USA).
Jianjun
J
Cheng
Institute for Molecular Engineering, University of Chicago, Chicago, IL 60637 (USA). mtirrell@uchicago.edu.
Matthew
M
Tirrell
D002942:Circular Dichroism; D046529:Microscopy, Electron, Transmission; D010455:Peptides / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry; D011487:Protein Conformation
D010455:Peptides; D011108:Polymers
chirality; helical structures; micelles; peptides; self-assembly