Publications by authors named "Olawole Ayinuola"
Organochlorine pesticides in therapeutic teas and human health risk assessment.
Food Addit Contam Part B Surveill
December 2022
Article Synopsis
- - This study assessed the levels of organochlorine pesticide (OCP) residues in commercially available therapeutic teas to understand the health risks of long-term consumption.
- - The researchers used a specialized extraction method and analyzed the samples with Gas Chromatography to detect pesticide levels, finding many exceeded EU safety limits.
- - Notable findings included widespread detection of aldrin in all samples, with methoxychlor and p,p'-DDT found in most, while the health risk assessment highlighted aldron as a significant cancer risk.
The proteolytic activity of human plasmin (hPm) is utilized by various cells to provide a surface protease that increases the potential of cells to migrate and disseminate. Skin-trophic Pattern D strains of (GAS), e.g.
View Article and Find Full Text PDFThe direct binding of human plasminogen (hPg), via its kringle-2 domain (K2 ), to streptococcal M-protein (PAM), largely contributes to the pathogenesis of Pattern D Group A Streptococcus pyogenes (GAS). However, the mechanism of complex formation is unknown. In a system consisting of a Class II PAM from Pattern D GAS isolate NS88.
View Article and Find Full Text PDFVirulent strains of Streptococcus pyogenes (gram-positive group A Streptococcus pyogenes [GAS]) recruit host single-chain human plasminogen (hPg) to the cell surface-where in the case of Pattern D strains of GAS, hPg binds directly to the cells through a surface receptor, plasminogen-binding group A streptococcal M-protein (PAM). The coinherited Pattern D GAS-secreted streptokinase (SK2b) then accelerates cleavage of hPg at the R-V peptide bond, resulting in the disulfide-linked two-chain protease, human plasmin (hPm). hPm localizes on the bacterial surface, assisting bacterial dissemination via proteolysis of host defense proteins.
View Article and Find Full Text PDFVEK50 is a truncated peptide from a Streptococcal pyogenes surface human plasminogen (hPg) binding M-protein (PAM). VEK50 contains the full A-domain of PAM, which is responsible for its low nanomolar binding to hPg. The interaction of VEK50 with kringle 2, the PAM-binding domain in hPg (K2), has been studied by high-resolution NMR spectroscopy.
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