NDLI: Tuning colloidal association with specific peptide interactions

Content Provider	Royal Society of Chemistry (RSC)
Author	Schoen, Alia P. Hommersom, Bob Leunissen, Mirjam E. Heilshorn, Sarah C.
Copyright Year	2013
Abstract	Coiled-coil leucine zipper domains are well-studied molecular recognition motifs that are attractive candidates for incorporation into engineered self-assembly systems due to their modular nature and wide range of binding affinities. Here, we investigate the ability of this peptide family to induce and control the specific association of micron-sized building blocks. Individual microparticles are functionalized with multiple copies of one particular leucine zipper motif which is capable of self-assembling through dimerization. We find that the dissociation temperature of the peptide-functionalized microparticles is considerably higher than the melting temperature of free peptide dimers in solution, which is a signature of the multivalent nature of the peptide-mediated particle interactions. We further demonstrate that titrating in freely soluble peptides to the peptide-coated bead suspensions can tune the particle association at constant temperature, pH, and ionic strength. While the high dissociation temperature of peptide-functionalized micro-objects may make global temperature control challenging, this ‘competition control’ with freely soluble peptides offers an attractive alternative to fine-tune the colloidal self-assembly with additional particle-specificity.
Starting Page	6781
Ending Page	6785
Page Count	5
File Format	HTM / HTML PDF
ISSN	1744683X
Volume Number	9
Issue Number	29
Journal	Soft Matter
DOI	10.1039/c3sm50230a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Self-assembly Ionic strength Leucine zipper Bead Dissociative Base pair Peptide
Content Type	Text
Resource Type	Article
Subject	Chemistry Condensed Matter Physics

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