Publications by authors named "Edyta Mikula"

Background: Biomarkers are characteristic molecules that can serve as indicators of biological process status or condition; here, they are being studied with special relevance to Parkinson's Disease (PD). This disease is a chronic neurodegenerative disorder very difficult to study given the site of pathology and due to a clinical phenotype that fluctuates over time. Currently, there is no definitive diagnostic test for Parkinson's Disease; thus, clinicians hope that the detection of crucial biomarkers will help in the symptomatic and presymptomatic diagnostics and provide surrogate endpoints to demonstrate the clinical efficacy of new treatments.

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Improved outcomes for many types of cancer achieved during recent years is due, among other factors, to the earlier detection of tumours and the greater availability of screening tests. With this, non-invasive, fast and accurate diagnostic devices for cancer diagnosis strongly improve the quality of healthcare by delivering screening results in the most cost-effective and safe way. Biosensors for cancer diagnostics exploiting aptamers offer several important advantages over traditional antibodies-based assays, such as the in-vitro aptamer production, their inexpensive and easy chemical synthesis and modification, and excellent thermal stability.

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Background: It is estimated that the average time between the diagnosis of Alzheimer's disease (AD) and the patient's death is 5-9 years. Therefore, both the initial phase of the disease and the preclinical state can be included in the critical period in disease diagnosis. Accordingly, huge progress has recently been observed in biomarker research to identify risk factors for dementia in older people with normal cognitive functions and mild cognitive impairments.

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Background: In this work, we report an electrochemical biosensor for the detection of anti-hemagglutinin antibodies against the swine virus H1N1 present in mice sera immunized with mixture of His-H1 HA in monomeric and oligomeric form. The oriented immobilization of the recombinant His-tagged hemagglutinin (His-H1 HA) consists of: (i) formation of a mixed layer of 4-mercaptobutanol (MBT) and the thiol derivative of dipyrromethene (DPM); (ii) complexation of Cu (II) by DPM; (iii) immobilization of His-H1 HA via coordination bonds between Cu (II) sites from DPM-Cu (II) complex and imidazole nitrogen atoms of a histidine tag; (iv) filling free spaces with bovine serum albumin. The interactions between recombinant His- H1 HA covalently attached to the electrode surface and the anti-hemagglutinin H1 antibodies present in mice sera were explored with Osteryoung square-wave voltammetry.

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Background: Alzheimer's disease (AD) is the most common form of dementia. The process of AD can begin 20 years before any symptom of cognitive loss. Thus, the development of systems for early diagnosis and prevention is very important.

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In this work we report on an electrochemical biosensor for the determination of the S100B protein. The His-tagged VC1 domains of Receptors for Advanced Glycation End (RAGE) products used as analytically active molecules were covalently immobilized on a monolayer of a thiol derivative of pentetic acid (DPTA) complex with Cu(II) deposited on a gold electrode surface. The recognition processes between the RAGE VC1 domain and the S100B protein results in changes in the redox activity of the DPTA-Cu(II) centres which were measured by Osteryoung square-wave voltammetry (OSWV).

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This paper concerns the development of an electrochemical biosensor for the determination of Aβ(16-23') and A(β1-40) peptides. The His-tagged V and VC1 domains of Receptor for Advanced Glycation end Products (RAGE) immobilized on a gold electrode surface were used as analytically active molecules. The immobilization of His6-RAGE domains consists of: (i) formation of a mixed layer of N-acetylcysteamine (NAC) and the thiol derivative of pentetic acid (DPTA); (ii) complexation of Cu(II) by DPTA; (iii) oriented immobilization of His6-RAGE domains via coordination bonds between Cu(II) sites from DPTA-Cu(II) complex and imidazole nitrogen atoms of a histidine tag.

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