![]() ![]() Prominent structures containing randomly distributed voids can be detected when the bilayer of liposomes transforms from an ordered gel phase to a disordered fluid phase. On the other side, fern-like patterns formed by dried droplets of cervical mucus detect the preterm premature rupture of membranes and/or the onset of labor due to the presence of NaCl in mucus under estrogen effect. This occurs because of the number of red blood cells decreasing in anemia, while high levels of triglycerides and cholesterol in the blood appear in hyperlipidemia. ![]() ![]() The changes in the size and spatial distribution of crack and plaque patterns in stains of whole blood help to correlate anemia and hyperlipidemia in patients. In addition, the length of the large cracks is related to the level of bilirubin in the blood of infants with jaundice. For example, a reduction in radial crack lengths in dried droplets of whole blood helps to detect Thalassaemia, a blood disorder where hemoglobin (Hb) is abnormal. Pattern analysis of dried droplets of biofluids is useful for obtaining information about the existence and the structural state of the components of a solution. Therefore, developing techniques for the detection of conformational changes in proteins contributes to the understanding of pathologies and improves their care. Protein aggregation diseases, which affect and are toxic to the central nervous system, are Huntington’s disease, Parkinson’s disease, prion diseases, and Alzheimer’s disease. Moreover, type 2 diabetes may be due to pancreatic accumulation of islet amyloid polypeptide, affecting a single organ. For example, the accumulation of amyloids deposit on different parts of the body are related to systemic amyloidosis, such as AL amyloidosis (accumulation of immunoglobulin light chain amyloid fibrils), amyloid A (deposits of catabolic products of the SSA protein), and ATTR (transthyretin accumulation). Moreover, the aggregation and accumulation of proteins in the form of amyloids and plaques are distinctive elements of over 20 degenerative diseases, which affect diverse peripheral tissues and the central nervous system. Some diseases derived from an “incorrect” folding of a specific protein or protein complex are cystic fibrosis, Marfan syndrome, and amyotonic lateral sclerosis. Unfolded proteins interact inappropriately with other molecules and are often aggregated. In this process, the affected protein can lose its biological function, develop resistance to degradation, and may acquire toxicity. However, in certain circumstances, the protein concentration, complex interaction with other proteins, and the cellular environment can lead to misfolding or the formations of aggregates of proteins. The specific three-dimensional structure of proteins is necessary to maintain their biological function in the cell. Proteins are the principal component in all living systems, responsible for diverse molecular functions in biological systems. We prove that it is possible to achieve 100% accuracy in identifying 4% of unfolded BSA contained in a protein solution. The radial intensity profile, the mean pixel intensity, and the entropy make it possible to characterize the patterns in dried droplets. At a low relative concentration of unfolded proteins (above 2%), small amorphous aggregates emerge in the deposits, while at high concentrations (above 16%), the “eye-like pattern”, a large aggregate surrounded by a uniform coating, is produced. Optical microscopy reveals that the relative concentration of unfolded proteins determines the morphological characteristics of deposits. Depending on the NaCl concentration, the crystals can be small, large, elongated, entangled, or dense. Folded proteins produce a well-defined coffee ring and crystal patterns all over the dry droplet. To address this problem, we present an experimental study on pattern formation in dried droplets of bovine serum albumin (BSA), in folded and unfolded conformational states, in saline solution (NaCl). However, the effectiveness of this method to reveal the coexistence of macromolecules of the same species, but different conformational states, is still unknown. The morphological analysis of patterns in dried droplets has allowed the generation of efficient techniques for the detection of molecules of medical interest. ![]()
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