期刊
PROTEIN JOURNAL
卷 39, 期 1, 页码 10-20出版社
SPRINGER
DOI: 10.1007/s10930-019-09877-w
关键词
Amylin; Islet amyloid polypeptide; Amyloid; Diabetes; Oligomer
资金
- Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES) [001]
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq) [PQ-309330/2014-9]
- Fundacao de Amparo a Pesquisa do Estado do Rio de Janeiro Carlos Chagas Filho (FAPERJ) [E-26/201.320/2014-BOLSA]
Control of amylin agglomeration is of interest for both the study of pathophysiology and the design of amylin-based pharmaceutical products. Here we report the effects of a large set of common buffering agents, aminoacids and nucleoside phosphates over the amylin amyloid aggregation. Circular dichroism showed no apparent effects of the co-solutes over the secondary-structure of soluble amylin. Instead, we found a large dependence of the fibrillation process on the total amount of co-solute charged groups. The amyloid nature of the aggregates was confirmed by transmission electron microscopy, X-ray diffraction and infrared spectroscopy. While acidic pH and low-ionic co-solutes shows the largest size effect in hampering aggregation, no further effect was observed that could identify a single compound as a major direct heterotropic determinants of the amyloid process. These data suggest a more physico-chemical effect of co-solutes over the modulation of amylin instead of a chemical entity-related causal factor.
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