A potential anti-amyloidogenic therapy for type 2 diabetes based on the QBP1 peptide
Posted on: 1 April 2026
Preprint posted on 10 May 2025
Prospecting and characterization of a peptide (QBP1) with potential to inhibit amyloid aggregation of proteins associated with type 2 diabetes
Selected by Joao Gabriel, Marcus Oliveira
Categories: bioinformatics, biophysics, cell biology
Graphical abstract
Schematic illustration of the development of type 2 diabetes mellitus through the amyloid aggregation process of hIAPP (islet amyloid polypeptide), from the preprint: https://www.biorxiv.org/content/10.1101/2025.05.06.652241v1
Background
Type 2 diabetes (T2D) is a metabolic disease with amyloid characteristics, whose development, among other factors, depends on the relationship between the individual and their environment and/or their lifestyle.
Insulin resistance is the starting point in the development of T2D, as it is directly related to the increased expression of insulin (reaching up to 10 times more than a normal organism) in an attempt to regulate glycemic homeostasis [5]. Dysregulation of proteostasis at the tissue level (pancreas) leads to the overexpression of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic potential, resulting in a reduction of pancreatic beta cells [6].
Most insulin expression follows the fluctuations of blood glucose during feeding and fasting cycles; this “cycle” involves the regulation of a series of physiological processes within energy metabolism [7]. The regulation of this system is also carried out by peptides produced during the process, such as Amylin (also known as IAPP), a peptide co-produced with insulin [8]. In specific situations can form soluble and insoluble aggregates with amyloid or amorphous morphology.
The phenomenon of protein aggregation is complex and widely studied, constituting a heterogeneous process. The proteoforms generated during the aggregation process of the same protein can differ from each other in terms of size, morphology, secondary structures, cytotoxicity, aggregation speed, etc. [9]. The overexpression of Amylin, within the context of T2D, is crucial for the reduction of β-pancreatic cells, as the aggregation of this peptide leads to cytotoxic proteoforms that impact the loss of cell viability in the islets of Langerhans [10].
Key Results
QBP1 strongly inhibits hIAPP amyloid fibril formation from the start of the aggregation process
Aggregation kinetics assessed by the ThT assay demonstrated that the incubation of hIAPP in the presence of QBP1 (1:5) drastically reduces amyloid fiber intensity. Moreover, the research group showed that the primary sequence of the peptide is crucial for its anti-amyloidogenic effect. Their results demonstrate that scrambled sequences of QBP1 (SC-M8 and SC-M11) reduce the maximum Thioflavin emission intensity, but not to the same order of magnitude (10x) as QBP1.
QBP1 directs amylin to a different aggregation pathway, altering its morphology
The morphology of the aggregates formed under both conditions (hIAPP-QBP1, hIAPP-SC-M8, and hIAPP-SC-M11) was analyzed by fluorescence microscopy (Thioflavin-Stained, ThS). While hIAPP alone showed dense ThS-positive material with uniform characteristics, hIAPP incubated with QBP1 displayed smaller and more diffuse aggregates with lower ThS intensity.
To determine at which stage of the aggregation pathway QBP1 interferes, the authors used two antibodies: A11 for prefibrillar oligomers and OC for mature amyloid fibrils. The aggregation process of hIAPP was analyzed at three incubation points (0, 16, and 48 h). hIAPP alone showed A11 positivity at 16 hours and OC positivity at 48 hours of incubation. Furthermore, hIAPP incubated with QBP1 showed no reaction to A11 or OC during the 48-hour period. Aggregate morphology was analyzed by TEM, where hIAPP alone presented characteristic amyloid fibers, while hIAPP incubated with QBP1 exhibited amorphous aggregates.
QBP1 reduces cellular damage caused by amylin overexpression and by the presence of exogenous amylin aggregates
By fusing penetratin (a peptide capable of crossing the plasma membrane without causing damage) to QBP1, the researchers were able to analyze its effect in INS-E1 cells modified to overexpress amylin (INS-E1-Amylin). Under these conditions, the authors showed that 10 µM of QBP1-penetratin ensures the survival of INS-E1-Amylin cells. Furthermore, the authors also demonstrated that QBP1 provides protection against exogenous amylin aggregates (in a 1:1 ratio).
Molecular insights into the QBP1-hIAPP interaction through MD simulations
To analyze possible interactions between QBP1 and amylin, the authors conducted in silico molecular dynamics simulations. It turned out this interaction occurs mainly through the hydrophobic region (tryptophan, phenylalanine, proline), which can interact with the hydrophobic domain of amylin. QBP1 exhibited a more favorable binding energy when compared with the scrambled sequences (SC), highlighting the importance of peptide identity. From this, the group concluded that the molecular interaction between amylin and QBP1—dependent on the peptide sequence and conformation—occurs through hydrophobic interactions, specifically involving the residues responsible for enabling the structural transition of amylin to β-sheet-rich conformations.
Questions and Suggestions
Main questions
Q1 – When showing that QBP1 drastically reduces the maximum ThT intensity, the authors still demonstrate an increase (up to 1000 A.U.) in ThT fluorescence. However, fluorescence spectroscopy results and antibody analyses alone cannot confirm that there is no secondary structure transition in the Amylin-QBP1 case. In the discussion (page 22, line 5), the authors state:
“…QBP1 appears to prevent misfolding and reduce the formation of toxic oligomers and fibrils…”
Fluorescence microscopy and TEM images show Amylin-QBP1 aggregates—how can we be sure that, within this aggregated structure, QBP1 does not interfere with antibody (OC or A11) binding? The same question applies to Thioflavin binding within this aggregate complex.
Q2 – The experimental design with cells is very interesting, especially the approach used to mimic T2DM. Some studies employ another murine insulinoma lineage, RIM-m5F. Is there a specific experimental reason for choosing the INS-E1 lineage?
Q3 – For the aggregation kinetics assay, wouldn’t it be interesting to analyze QBP1 alone with ThT? This could help demonstrate whether QBP1 by itself interferes with the increase in ThT intensity.
Q4 – Why was ATP concentration analysis used as the sole viability marker?
Main suggestions
S1 – In the Materials and Methods section (ThT Fluorescence Assay), the description of the kinetic protocol in the plate reader is missing, such as agitation, agitation intervals, frequency, and plate type. The cited literature “Abedini et al., 2016; Gade Malmos et al., 2017” does not use plate readers to conduct kinetics but rather to analyze as an end-point.
S2 – The result related to the graph in Figure 1B is unclear, as neither the legend nor the Materials and Methods specify which hIAPP concentration was used for that assay.
S3 – In the introductory text, the authors address a point from the literature at the end of page 2, where they discuss that murine amylin, due to having three prolines at positions 25, 28, and 29 (unlike the human sequence), prevents pathological amyloid aggregation and disrupts the transition to β-sheet-rich fibrillar structures. However, some studies show that murine amylin aggregates in amyloid form, including the drug designed not to aggregate (Pramlintide). Some studies [1,2,3,4], for example, demonstrate that murine amylin may form aggregates with biophysical characteristics very similar to those of human amylin, including β-sheet formation.
S4 – The graph corresponding to Figure 4A in the preprint is not clear, as the X-axis indicates the molar concentration of exogenous hIAPP in solution with cells, which suggests that even the control cells received exogenous IAPP. The image legend also does not clearly define the conditions for the control cells.
S5 – Including a negative control in the kinetics assays would be important, as it would allow the authors to demonstrate whether the increase in ThT intensity in Figure 1B of the preprint is noise or truly reflects amyloid fiber formation for Amylin-QBP1.
Reference:
1 – Dayana Cabral da Silva, Giselle N. Fontes, Luiza C.S. Erthal, Luís Maurício T.R. Lima, Amyloidogenesis of the amylin analogue pramlintide, Biophysical Chemistry, Volume 219, 2016, Pages 1-8, SSN 0301-4622, https://doi.org/10.1016/j.bpc.2016.09.007.
2 – Alghrably M, Bennici G, Szczupaj G, Alasmael N, Qutub S, Maatouk B, Chandra K, Nowakowski M, Emwas AH, Jaremko M. Exploring the central region of amylin and its analogs aggregation: the influence of metal ions and residue substitutions. Front Chem. 2024 Jul 8;12:1419019. doi: 10.3389/fchem.2024.1419019. PMID: 39072260; PMCID: PMC11272978.
3 – Brunzell E, Sigfridsson K, Gedda L, Edwards K, Bergström LM. Investigation of supramolecular structures in various aqueous solutions of an amyloid forming peptide using small-angle X-ray scattering. Soft Matter. 2024;20: doi:10.1039/D3SM01172K.
4 – Leonardo C. Palmieri, Bruno Melo-Ferreira, Carolina A. Braga, Giselle N. Fontes, Luana Jotha Mattos, Luís Maurício T.R. Lima,Stepwise oligomerization of murine amylin and assembly of amyloid fibrils, Biophysical Chemistry, Volumes 180–181, 2013, ages 135-144, ISSN 0301-4622, https://doi.org/10.1016/j.bpc.2013.07.013.
5 – Zheng, Y., Ley, S. & Hu, F. Global aetiology and epidemiology of type 2 diabetes mellitus and its complications. Nat Rev Endocrinol 14, 88–98 (2018). https://doi.org/10.1038/nrendo.2017.151
6 – Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus Per Westermark, Arne Andersson, and Gunilla T. Westermark Physiological Reviews 2011 91:3, 795-826
7 – Sun X, Liu B, Yuan Y, Rong Y, Pang R, Li Q. Neural and hormonal mechanisms of appetite regulation during eating. Front Nutr. 2025 Mar 24;12:1484827. doi: 10.3389/fnut.2025.1484827. PMID: 40201582; PMCID: PMC11977392.
8 – Ludvik B. Amylin/IAPP (Islet Amyloid Polypeptide)–Physiologie und klinische Bedeutung [Amylin/IAPP (islet amyloid polypeptide)–physiology and clinical significance]. Wien Klin Wochenschr. 1997 Jun 6;109(11):379-83. German. PMID: 9281227.
9 – Meisl G, Yang X, Hellstrand E, Frohm B, Kirkegaard JB, Cohen SI, Dobson CM, Linse S, Knowles TP. Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides. Proc Natl Acad Sci U S A. 2014 Jul 1;111(26):9384-9. doi: 10.1073/pnas.1401564111. Epub 2014 Jun 17. PMID: 24938782; PMCID: PMC4084462.
10 – Leena Haataja, Tatyana Gurlo, Chang J. Huang, Peter C. Butler, Islet Amyloid in Type 2 Diabetes, and the Toxic Oligomer Hypothesis, Endocrine Reviews, Volume 29, Issue 3, 1 May 2008, Pages 303–316, https://doi.org/10.1210/er.2007-0037
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