Porcine Islet amyloid polypeptide,IAPP ELISA Kit
- Known as:
- Porcine Islet amyloid multipeptide,IAPP Enzyme-linked immunosorbent assay test Kit
- Catalog number:
- E0331Po
- Product Quantity:
- 48T
- Category:
- Elisa Kits
- Supplier:
- Btlab
- Gene target:
- Porcine Islet amyloid polypeptide IAPP ELISA Kit
Related genes to: Porcine Islet amyloid polypeptide,IAPP ELISA Kit
- Gene:
- IAPP NIH gene
- Name:
- islet amyloid polypeptide
- Previous symbol:
- -
- Synonyms:
- AMYLIN, DAP, IAP
- Chromosome:
- 12p12.1
- Locus Type:
- gene with protein product
- Date approved:
- 1989-05-24
- Date modifiied:
- 2014-11-19
Related products to: Porcine Islet amyloid polypeptide,IAPP ELISA Kit
Related articles to: Porcine Islet amyloid polypeptide,IAPP ELISA Kit
- Aggregation of human islet amyloid polypeptide (hIAPP, amylin) into amyloid fibrils is a hallmark of β-cell dysfunction in type 2 diabetes, yet the molecular determinants governing its aggregation pathways remain incompletely understood. Here, we investigate how systematic fluorination of Phe23a key aromatic residue within the amyloidogenic coremodulates intra- and intermolecular interactions and thereby probes hIAPP self-assembly under physiologically relevant acidic and neutral pH conditions. Using a combination of Thioflavin T kinetics, scaling-exponent analysis, pyrene fluorescence, ion mobility-mass spectrometry, circular dichroism, F NMR spectroscopy, and molecular dynamics simulations, we show that fluorination of Phe23 reshapes aggregation behavior in a highly nonadditive manner. While wild-type and minimally fluorinated variants, at neutral pH, follow the surface-catalyzed secondary nucleation mechanism discussed well in the literature, higher degrees of fluorination progressively reduce monomer dependence and give rise to pronounced concentration-dependent, self-inhibiting aggregation behavior. Under acidic conditions, protonation of His18 leads to a divergent concentration dependence, with reduced monomer dependence for wild-type and minimally fluorinated peptides and enhanced concentration sensitivity for tetra- and penta-fluorinated variants. These concentration dependencies reflect differences in the conformational accessibility, flexibility, and oligomerization efficiency required for productive fibril formation under each pH condition. Together, these results identify Phe23 as a molecular switch that couples local interactions to global aggregation pathways and demonstrate how subtle chemical and environmental perturbations can modulate the productivity of hIAPP fibril formation. - Source: PubMed
Publication date: 2026/05/05
Pavlov ArtemBatebi HosseinÖsterlund NicklasPagel KevinSchade BorisSchubert MarioNetz Roland RKoksch Beate - Hybrid insulin peptides (HIPs) are neoepitopes involved in type 1 diabetes (T1D), but their complete repertoire remains unknown. The vast combinatorial space makes experimental screening unfeasible and requires bioinformatics-based prioritization. We developed a multi-level machine learning pipeline for ranking HIP candidates. First, 36 physicochemical and junction-specific features were computed for a reference library of 240 HIPs with known enzyme-linked immunospot (ELISPOT) reactivity, and a baseline Ridge regression model was trained. Next, all possible HIP candidates with 7-9 amino acid residues per fragment were generated from eight pancreatic β-cell secretory granule source proteins, including insulin chains and C-peptide, islet amyloid polypeptide, chromogranin A, neuropeptide Y, and two secretogranins, yielding 1,057,374 candidates. For each source protein, a local weighted XGBoost (Extreme Gradient Boosting) model was trained using Ridge-score-derived pseudo-labels together with weighted ELISPOT-derived and literature-derived reference HIPs. Finally, anchor-calibrated re-ranking was performed in the global model using cosine similarity to positive anchors (n = 46) and negative anchors (n = 210). The Ridge model achieved 5-fold out-of-fold R² = 0.711 and an area under the receiver operating characteristic curve (AUC) of 0.967. The global model produced a prioritized list of 40 HIP candidates, five per source protein. The highest ranks were observed for candidates with right fragments from neuropeptide Y, secretogranins 1 and 2, islet amyloid polypeptide, and chromogranin A. Candidates carrying the insulin fragment on the right side were systematically down-ranked, suggesting asymmetry in HIP formation. The proposed pipeline reduces the HIP search space from more than one million sequences to a limited set of candidates for experimental validation and provides a framework adaptable to other chimeric neoepitopes in autoimmunity. - Source: PubMed
Publication date: 2026/08/07
Kandinov IlyaTrukhin DmitryGryadunov DmitrySavvateeva Elena - Aggregation of islet amyloid polypeptide (IAPP) to form amyloid contributes to β-cell dysfunction in type 2 diabetes, yet the identity and temporal persistence of the toxic species is unresolved. Competing models attribute toxicity to mature fibrils, fibril growth, or transient prefibrillar intermediates formed during the lag phase or via secondary nucleation. Here, we directly test these models by combining time-resolved β-cell functional assays with concurrent biophysical measurements of IAPP aggregation across multiple perturbations and sequence variants. Across 22 independent experiments spanning more than a 450-fold range in lag times, we find that maximal toxicity occurs during the lag phase and declines as fibrils accumulate. The duration of β-cell dysfunction scales linearly with lag phase length, establishing aggregation kinetics as a quantitative predictor of the onset, peak, and termination of toxicity. Perturbations that alter aggregation kinetics, including concentration, temperature, and sequence, predictably shift the temporal window of toxicity. The diabetes-associated S20G variant produces higher peak toxicity over a compressed time window, whereas the slower-aggregating variants examined prolong toxicity without increasing its magnitude. These results resolve competing models by demonstrating that transient lag-phase intermediates, rather than growth phase processes or mature fibrils, dominate β-cell dysfunction, and establish aggregation kinetics as a predictor of the timing and duration of cellular exposure to toxic intermediates. - Source: PubMed
Publication date: 2026/08/06
Plesner AnnetteCao PingRaleigh Daniel PAbedini Andisheh - The distribution of amylin-like substances was investigated by immunohistochemistry in the pancreas of the Japanese eel (Anguilla japonica). Amylin-immunoreactive cells were observed in pancreatic islets. These immunostaining profiles were not observed by the preabsorption of the anti-amylin serum with synthetic amylin, indicating that the serum specifically recognized eel amylin-like peptide. Almost all amylin-immunoreactive cells were immunopositive for peptide YY, suggesting that amylin and peptide YY co-secreted from the islet cells might participate in the modulation of insulin and glucagon secretion in the pancreatic islets. In addition, weakly glucagon-immunopositive cells, but not densely glucagon-immunopositive cells, also corresponded to amylin-immunoreactive cells. The subpopulation of glucagon-immunoreactive and glucagon-like peptide-1-immunoreactive cells was also immunopositive for peptide YY. These results suggest that amylin and peptide YY, and also presumably glucagon-like peptide-1, are co-secreted from the amylin/peptide YY cells, and these three peptides modulate food intake through the central nervous system in addition to intrainsular functions. - Source: PubMed
Suzuki HirohumiYamamoto Toshiharu - Amylin is a pancreatic beta-cell hormone that sits at a systems hub connecting key aspects of energy metabolism. Amylin physiologically controls satiation, slows gastric emptying and limits postprandial glucagon release, while its actions also link homeostatic eating controls with reward driven behaviours via defined central nervous system pathways. Further, at least under certain conditions, aggregating amylin exerts a strong pathophysiological impact on the destruction of pancreatic beta-cells in Type 2 diabetes mellitus (T2D), providing a plausible explanation for why a T2D-like disease entity is only observed in a few mammalian species. This review will provide a brief summary of selected aspects of our current understanding of the biology of amylin and outlines how this knowledge has recently been translated into effective pharmacotherapy for obesity and diabetes, including long-acting analogs combination approaches with other peptide hormones. - Source: PubMed
Publication date: 2026/08/05
Le Foll ChristelleLutz Thomas A