Amanda B. Marciel

Ultrafast Redistribution of E. coli SSB along Long Single-Stranded DNA via Intersegment Transfer

Single-stranded DNA binding proteins (SSBs) selectively bind single-stranded DNA (ssDNA) and facilitate recruitment of additional proteins and enzymes to their sites of action on DNA. SSB can also locally diffuse on ssDNA, which allows it to quickly reposition itself while remaining bound to ssDNA. In this work, we used a hybrid instrument that combines single-molecule fluorescence and force spectroscopy to directly visualize the movement of Escherichia coli SSB on long polymeric ssDNA. Long ssDNA was synthesized without secondary structure that can hinder quantitative analysis of SSB movement. The apparent diffusion coefficient of E. coli SSB thus determined ranged from 70,000 to 170,000nt(2)/s, which is at least 600 times higher than that determined from SSB diffusion on short ssDNA oligomers, and is within the range of values reported for protein diffusion on double-stranded DNA. Our work suggests that SSB can also migrate via a long-range intersegment transfer on long ssDNA. The force dependence of SSB movement on ssDNA further supports this interpretation.

Fluidic‐Directed Assembly of Aligned Oligopeptides with π‐Conjugated Cores

A microfluidic-based directed assembly strategy is employed to form highly aligned supramolecular structures. Formation of aligned synthetic oligopeptide nanostructures is accomplished using planar extensional flow, which induces alignment of underlying material suprastructures. Fluidic-directed assembly of supramolecular structures allows for unprecedented manipulation at the nano- and mesoscales, which has the potential to provide rapid and efficient control of functional material properties.

Bulk and nanoscale polypeptide based polyelectrolyte complexes.

Polyelectrolyte complexes (PECs) formed using polypeptides have great potential for developing new self-assembled materials, in particular for the development of drug and gene delivery vehicles. This review discusses the latest advancements in PECs formed using polypeptides as the polyanion and/or the polycation in both polyelectrolyte complexes that form bulk materials and block copolymer complexes that form nanoscale assemblies such as PEC micelles and other self-assembled structures. We highlight the importance of secondary structure formation between homogeneous polypeptide complexes, which, unlike PECs formed using other polymers, introduces additional intermolecular interactions in the form of hydrogen bonding, which may influence precipitation over coacervation. However, we still include heterogeneous complexes consisting of polypeptides and other polymers such as nucleic acids, sugars, and other synthetic polyelectrolytes. Special attention is given to complexes formed using nucleic acids as polyanions and polypeptides as polycations and their potential for delivery applications.

Scale-Dependent Stiffness and Internal Tension of a Model Brush Polymer

Bottle-brush polymers exhibit closely grafted side chains that interact by steric repulsion, thereby causing stiffening of the main polymer chain. We use single-molecule elasticity measurements of model brush polymers to quantify this effect. We find that stiffening is only significant on long length scales, with the main chain retaining flexibility on short scales. From the elasticity data, we extract an estimate of the internal tension generated by side-chain repulsion; this estimate is consistent with the predictions of blob-based scaling theories.