Pathway Dependent Self-Assembly of Amphiphilic Diblock Copolypeptides

Content Provider	Semantic Scholar
Author	Pakstis, Lisa Nowak, Andrew Holowka, Eric P. Thompson, Jeffery M. Timothy J. Pochan, Darrin J.
Copyright Year	2005
Abstract	Submitted for the MAR05 Meeting of The American Physical Society Pathway Dependent Self-Assembly of Amphiphilic Diblock Copolypeptides LISA PAKSTIS, University of Delaware, ANDREW NOWAK, ERIC HOLOWKA, JEFFERY THOMPSON, TIMOTHY DEMING, University of California Los Angeles, DARRIN POCHAN, University of Delaware — Diblock copolypeptides consisting of a hydrophilic lysine (K) block and a hydrophobic leucine (L) block were designed to selfassemble due to their amphiphilic nature and the defined secondary structure of the hydrophobic block. In aqueous solution, these amphiphilic copolypeptides assemble into stiff, porous hydrogels at low volume fractions of polymer (vol. fraction polypeptide ( > 0.5 wt %). However, different selfassembly pathways (e.g. dissolution of the polypeptide into an organic solvent with subsequent addition of water followed by evaporation of the organic component) produce drastically different materials, spanning weak hydrogels, vesicles, twisted fibrils or hexagonal single crystals. Characterization of these disparate materials indicates that assembly is intrinsically controlled on the nanoscale by the interaction of the ahelical hydrophobic block into membranes. Hierarchical, microscale assembly is controlled through the pathway, i.e. kinetics, of assembly. Lisa Pakstis University of Delaware Date submitted: 24 Nov 2004 Electronic form version 1.4
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://absimage.aps.org/image/MAR05/MWS_MAR05-2004-000798.pdf
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article