The Curli Accessory Protein CsgF of Salmonella Typhimurium Influences the in vitro Aggregation of Human Islet Amyloid Polypeptide
Year: 2025
Type: article
Abstract: . Herein we describe the ability of CsgF to influence the in-vitro aggregation of human islet amyloid polypeptide (hIAPP), an amyloidogenic polypeptide that is unrelated to Curli. In the presence of CsgF no increase in Thioflavin T fluorescence was observed for freshly solubilized hIAPP monitored as a function of time, suggesting that CsgF prevents the aggregation of hIAPP during the period of observation. A variant of CsgF lacking the first 65 residues in the N-terminus of CsgF retained the ability to inhibit the aggregation of hIAPP suggesting that the ability of CsgF to inhibit the aggregation of hIAPP is mediated by the C-terminal half of the protein.
Source: PubMed
Authors: Osmar Meza-Barajas, Clayton Connelly, Alejandra Lopez, Isamar Aranda, Ashwag Binmahfooz, Allison Newell, Sajith Jayasinghe
Institution: California State University, San Marcos
Language: English
Subfield: Physiology
Field: Medicine
Domain: Health Sciences
Open Access status: green
OpenAlex ID: W4411045310