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Full-Text Articles in Biology
Identification Of Plant Extracts That Inhibit The Formation Of Diabetes-Linked Iapp Amyloid, Ana Lucia Fuentes, Kathleen Hennessy, Jacob Pascual, Nicole Pepe, In Wang, Cynthia Chaggan, Jessica Martinez, Evelyn Rivera, Paola Cota, Christina Cunha, Luiza A. Nogaj, David A. Moffet
Identification Of Plant Extracts That Inhibit The Formation Of Diabetes-Linked Iapp Amyloid, Ana Lucia Fuentes, Kathleen Hennessy, Jacob Pascual, Nicole Pepe, In Wang, Cynthia Chaggan, Jessica Martinez, Evelyn Rivera, Paola Cota, Christina Cunha, Luiza A. Nogaj, David A. Moffet
Chemistry and Biochemistry Faculty Works
The extracts of 27 vegetables, spices and herbs were screened for their functional ability to inhibit the aggregation of islet amyloid polypeptide (IAPP, amylin) into toxic amyloid aggregates. The aggregation of IAPP has been directly linked to the death of pancreatic β-islet cells in type 2 diabetes. Inhibiting the aggregation of IAPP is believed to have the potential to slow, if not prevent entirely, the progression of this disease. As vegetables, spices and herbs are known to possess many different positive health effects, the extracts of 27 plants (abundant within the United States and spanning several plant families) were screened …
Myricetin Inhibits Islet Amyloid Polypeptide (Iapp) Aggregation And Rescues Living Mammalian Cells From Iapp Toxicity, Casey Zelus, Ayano Fox, Anastasia Calciano, Bianca S. Faridian, Luiza A. Nogaj, David A. Moffet
Myricetin Inhibits Islet Amyloid Polypeptide (Iapp) Aggregation And Rescues Living Mammalian Cells From Iapp Toxicity, Casey Zelus, Ayano Fox, Anastasia Calciano, Bianca S. Faridian, Luiza A. Nogaj, David A. Moffet
Chemistry and Biochemistry Faculty Works
The aggregation of the amyloidogenic polypeptide IAPP (Islet Amyloid Polypeptide, amylin) is believed to play a direct role in the death of pancreatic β-islet cells in type II diabetes. Preventing the initial aggregation event of IAPP is one strategy for slowing, and possibly preventing, the progression of this disease. Here, we investigate myricetin’s potential as an inhibitor of IAPP aggregation. We show that myricetin prevented thioflavin T binding in a concentration dependent manner. Atomic force microscopy revealed that myricetin prevented fiber formation under rigorous conditions conducive to forming IAPP aggregates. Using an IAPP-EGFP (Enhanced Green Fluorescent Protein) protein construct, we …
Short Peptides As Inhibitors Of Amyloid Aggregation, Bradley Neddenriep, Anastasia Calciano, Daniel Conti, Erin Sauve, Marissa Paterson, Edward Bruno, David A. Moffet
Short Peptides As Inhibitors Of Amyloid Aggregation, Bradley Neddenriep, Anastasia Calciano, Daniel Conti, Erin Sauve, Marissa Paterson, Edward Bruno, David A. Moffet
Chemistry and Biochemistry Faculty Works
The misfolding and aggregation of proteins into amyloid has been linked to a variety of age-related diseases. Aggregation of proteins, such as Aβ in Alzheimer's disease and Islet Amyloid Polypeptide (IAPP, amylin) in type 2 diabetes, appears to lead to the formation of toxic assemblies. These assemblies range in size from small oligomers (2-8 proteins) to large fibrils (thousands of proteins). It remains unclear how these amyloidogenic proteins misfold and form toxic species, but growing evidence suggests that inhibiting the aggregation of these proteins could slow, if not prevent altogether, the progression of these diseases. We describe the use of …
Selection For Non-Amyloidogenic Mutants Of Islet Amyloid Polypeptide (Iapp) Identifies An Extended Region For Amyloidogenicity, Ayano Fox, Thibaut Snollaerts, Camille Errecart Casanova, Anastasia Calciano, Luiza A. Nogaj, David A. Moffet
Selection For Non-Amyloidogenic Mutants Of Islet Amyloid Polypeptide (Iapp) Identifies An Extended Region For Amyloidogenicity, Ayano Fox, Thibaut Snollaerts, Camille Errecart Casanova, Anastasia Calciano, Luiza A. Nogaj, David A. Moffet
Chemistry and Biochemistry Faculty Works
The aggregation of the 37-residue polypeptide IAPP, as either insoluble amyloid or as small oligomers, appears to play a direct role in the death of pancreatic β-islet cells in type II diabetes. While IAPP has been known to be the primary component of type II diabetes amyloid, the molecular interactions responsible for this aggregation have not been identified. To identify the aggregation-prone region(s), we constructed a library of randomly generated point mutants of IAPP. This mutant IAPP library was expressed in E. coli as genetic fusions to the reporter protein enhanced green fluorescent protein (EGFP). Because IAPP aggregates rapidly, both …
Inhibition Of Aβ42 Aggregation Using Peptides Selected From Combinatorial Libraries, Michael Baine, Daniel S. Georgie, Elelta Z. Shiferraw, Theresa P. T. Nguyen, Luiza A. Nogaj, David A. Moffet
Inhibition Of Aβ42 Aggregation Using Peptides Selected From Combinatorial Libraries, Michael Baine, Daniel S. Georgie, Elelta Z. Shiferraw, Theresa P. T. Nguyen, Luiza A. Nogaj, David A. Moffet
Chemistry and Biochemistry Faculty Works
Increasing evidence suggests that the aggregation of the small peptide Aβ42 plays an important role in the development of Alzheimer’s disease. Inhibiting the initial aggregation of Aβ42 may be an effective treatment for preventing, or slowing, the onset of the disease. Using an in vivo screen based on the enzyme EGFP, we have searched through two combinatorially diverse peptide libraries to identify peptides capable of inhibiting Aβ42 aggregation. From this initial screen, three candidate peptides were selected and characterized. ThT studies indicated that the selected peptides were capable of inhibiting amyloid aggregation. Additional ThT studies showed that one of the …