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1.
J Phys Chem B ; 122(38): 8972-8984, 2018 09 27.
Artigo em Inglês | MEDLINE | ID: mdl-30185036

RESUMO

Pattern formation during evaporation of biofluids has numerous biomedical applications, e.g., in disease identification. The drying of a bidisperse colloidal droplet involves formation of coffee ring patterns owing to the deposition of constituent particles. In the present study, we examine the distinctly different pattern formations during the drying of a colloidal solution depending on the nature of the constituent proteins. The pattern formations of two oppositely charged proteins, namely HSA and lysozyme, have been studied in the presence of fluorescence polystyrene beads of two different sizes (providing better image contrast for further analysis). The variation of pattern formation has been studied by varying the concentrations of the proteins as well as the particles. Furthermore, using image analysis, the patterns are segmented into different regions for quantification. To explain the variations in the patterns, we delve into the interplay of the interactions, especially the capillary and the DLVO forces (between the particles and the substrate). The developed methodology based on the coffee ring effect may be used to identify individual proteins.


Assuntos
Coloides/química , Dessecação , Muramidase/química , Nanopartículas/química , Albumina Sérica Humana/química , Algoritmos , Humanos , Processamento de Imagem Assistida por Computador , Microscopia Confocal , Microscopia Eletrônica de Varredura/métodos , Microscopia de Fluorescência , Poliestirenos/química , Eletricidade Estática , Tensão Superficial
2.
Int J Biol Macromol ; 79: 344-52, 2015 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-25964177

RESUMO

Pattern formation during evaporation of biofluids finds significant applications in the biomedical field for disease identification. Aß (25-35) is the smallest peptide in the amyloid peptide family that retains the toxicity of a full length peptide responsible for Alzheimer's disease and is chosen here as the model solute. Drying experiments on substrates of varying wettability exhibit unique drying patterns of Aß (25-35) fibrils visualized through fluorescence microscopy and transmission electron microscopy. The unique pattern formations can be interpreted as manifestations of the changes in the self-pinning mechanism with changes in wettability, which in some cases resembles the well-known coffee ring effect. Additionally, the delicate balance between the drag and capillary forces has been perturbed by initiating controlled rates of evaporation and probing their effects on the fibril patterning.


Assuntos
Peptídeos beta-Amiloides/ultraestrutura , Amiloide/ultraestrutura , Fragmentos de Peptídeos/ultraestrutura , Amiloide/química , Peptídeos beta-Amiloides/química , Benzotiazóis , Dessecação , Corantes Fluorescentes , Humanos , Microscopia Eletrônica de Transmissão , Microscopia de Fluorescência , Fragmentos de Peptídeos/química , Tiazóis , Molhabilidade
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