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  1. Aliyu AW, Mohd Nazri MN, Mohd Zaidi NF, Mohd Fadzli Mustaffa K
    Heliyon, 2023 Aug;9(8):e18861.
    PMID: 37609428 DOI: 10.1016/j.heliyon.2023.e18861
    Recent advancement in molecular medicine has seen applications of advanced biotechnology tools such as aptamer technology in therapeutics and diagnostics. Aptamer technology has witnessed various approaches including "Click-Chemistry" towards modifying aptamer structure to improve its potentials, but limited studies have reported the influence of such alteration on aptamer's specificity and affinity for their targets. Here, we utilized square wave voltammetry (SWV) electrochemical sensing based on heme to show the effects of cholesterol-triethylene-glycol (COL-TEG) modification of protoporphyrin-IX DNA-aptamers (OKA_24 and OKA_26) on their affinity for heme. Binding was evaluated by immobilizing 5 μM of heme onto cysteamine-glutaraldehyde-coated gold-electrode to construct electrochemical biosensor. Sensing of native/modified-aptamer was achieved by incubating their varying concentrations (9.76 nM - 10 μM) with heme-coated gold-electrode in HKSCM buffer pH 5, for 15 min. Chloroquine (2.5 μM) and non-binding HPIX-aptamer (2.5 μM) served as controls. Ferrocene was the redox solution used for SWV analysis. Protoporphyrin-IX DNA-aptamers specificity for heme was not tarnish by lipid conjugation. Selective binding of 2.5 μM of COL-TEG-OKA_24 and COL-TEG-OKA_26 to heme induced peak-current reduction by 30.68% and 24% respectively. Incubation of OKA_24 and OKA_26 aptamers produced resistance to current flow through the heme-coated gold-electrode by 23.21% and 14.4 8% respectively. Affinity SWV reveals that cholesterol conjugation decreases the affinity of COL-TEG-OKA_24 (KD = 4 7.13 ± 3.767 nM) and COL-TEG-OKA_24 (KD = 84.6 ± 8.7 nM) by 3- fold. There is a need to check the impact of such alteration on inhibition of heme to hemozoin polymerization, a process mediated by Plasmodium falciparum.
  2. Amira Khairil Anwar N, Najmi Mohd Nazri M, Rosliza Mohd Adzemi E, Amilda Anthony A, Mohd Azlan M, Balakrishnan V, et al.
    Cytokine, 2024 Jul 22;182:156698.
    PMID: 39042994 DOI: 10.1016/j.cyto.2024.156698
    BACKGROUND: Elevated serum levels of soluble PD-L1 (sPD-L1) have been reported in many cancers; however, there is limited data of sPD-L1 in breast cancer, especially those representing Asian (Malay) women. The purpose of this study was to evaluate sPD-L1 serum levels and analyze its correlation with clinical characteristics in breast cancer patients at Hospital Universiti Sains Malaysia (HUSM).

    METHODS: Blood specimens were obtained from 92 malignant, 16 benign breast cancer patients and 23 healthy controls. The serum concentrations of sPD-L1 were assessed by enzyme-linked immunosorbent assay (ELISA).

    RESULTS: The median serum sPD-L1 concentration of malignant and benign breast cancer patients was significantly elevated compared to the healthy cohorts (12.50 ng/mL vs 13.97 ng/mL vs 8.75 ng/mL, p 

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