Tuning colloidal association with specific peptide interactions

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 selfassembling through dimerization. We find that the dissociation temperature of the peptidefunctionalized 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.

Solid Colloids with Surface-Mobile DNA Linkers

“…Many of these binding groups are biologically inspired molecular recognition motifs, for instance taking the form of naturally occurring peptides [1][2][3][4] or synthetic DNA sticky ends. Many of these binding groups are biologically inspired molecular recognition motifs, for instance taking the form of naturally occurring peptides [1][2][3][4] or synthetic DNA sticky ends.…”

Mimicking Adhesion in Minimal Synthetic Cells

“…Moreover, it offers a large variety of possible binding motifs and adjustable melting temperatures depending on the design of the single-stranded DNA to form different colloidal amorphous and crystal structures. [62] Light is an attractive trigger to control the self-assembly process with high spatiotemporal resolution, as it is straightforward to illuminate a precise area at any desired time. [46,53,57,60,61] Likewise, the surfaces of oil in water droplets and lipid vesicles have also been decorated with DNA strands to specifically and reversibly assemble them into higher order structures.…”

“…[60,61] Nonetheless, the use of temperature as an external trigger is still not ideal to achieve high spatial and temporal control over cell-cell adhesion and is limited by the mostly high transition temperatures rendering it not biocompatible. [62] Light is an attractive trigger to control the self-assembly process with high spatiotemporal resolution, as it is straightforward to illuminate a precise area at any desired time. Further, light provides high tunability by altering the light intensity or pulse durations.…”

Protein-Mediated Colloidal Assembly

“…Schoen and co-workers used self-associating coiled-coil peptides to drive formation of small (~ 20 particles) clusters. 15 They were able to reverse cluster formation by addition of excess soluble peptide. Deyev and co-workers have used the barnase-barstar interaction to form complex structures that span multiple length scales.…”