Complex Protein Patterns in Drying Droplets
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Complex Protein Patterns in Drying Droplets Ronald G. Larson,1,2,3 Marc Alumnà López,1 Dong W. Lim,1,4 and Joerg Lahann1,2,* 1
Department of Chemical Engineering, University of Michigan, Ann Arbor Michigan, 48109, U.S.A. 2 Department of Biomedical Engineering, University of Michigan, Ann Arbor Michigan, 48109, U.S.A. 3 Department of Mechanical Engineering, University of Michigan, Ann Arbor Michigan, 48109, U.S.A. 4
present address: Department of BioNano Engineering, Hanyang University, Ansan, Kyeonggido, 425-791, Korea * corresponding author ABSTRACT We demonstrate that deposition patterns formed during drying droplets of aqueous protein solutions are complex, characteristic, and highly reproducible. Substrate, buffer as well as protein type are important factors largely influencing the patterned structure. Specifically, multiple growth zones in what we refer to as “soccer ball pattern” are formed when a droplet of albumin solution in sodium bicarbonate buffer is dried. Each growth zone has periodically patterned, concentric ringed structures surrounding a core at the center. Different macroscopic patterns are also found for streptavidin, fibrinogen, IgG antibody as well as rhodamine B base and polystyrene beads when droplets of their aqueous solutions are dried on the substrates with different degrees of hydrophilicity/hydrophobicity. Furthermore, distinguishable deposition patterns are formed in drying droplets of aqueous protein solutions containing albumin and fibrinogen at different ratios, suggesting that even the relative abundance of multiple proteins influences the deposition patterns. Since the protein pattern is reproducible for a given protein and variable among different proteins, the protein patterns from drying droplets might be useful to potentially identify a given protein under specific conditions. INTRODUCTION A wealth of hierarchically organized, highly functional, material architectures play important structural roles in biological systems as diverse as bone, dentine, shells, scales, spines, mollusks, and coccoliths [1-10]. Nature’s complex patterns are the result of highly orchestrated interactions between inorganic salts and unique biomolecules with specialized secondary, tertiary, and quaternary structures. While the exact mechanisms leading to these complex patterns are not fully understood, a series of distinguishable processes have been identified, including supramolecular self-organization of extended protein and polysaccharide networks, interfacial recognition, and directed crystallization.17 Precise molecular orientation of biomolecules with diverse structural properties, such as proteins, peptides, lipids, polysaccharides or glycoproteins, plays a pivotal role in regulating the formation of crystallization patterns [1-11]. In an attempt to mimic this behaviour in synthetic microenvironments, crystal patterns have been prepared using micro-structured surfaces as blueprints for directed crystallization [1,2,4].
More recently, self-assembly of aromatic compounds into ext
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