In Situ Preparation of Tannic Acid-Modified Poly(-isopropylacrylamide) Hydrogel Coatings for Boosting Cell Response.

The improvement of the capability of poly(-isopropylacrylamide) (PNIPAAm) hydrogel coating in cell adhesion and detachment is critical to efficiently prepare cell sheets applied in cellular therapies and tissue engineering. To enhance cell response on the surface, the amine group-modified PNIPAAm (PNIPAAm-APTES) nanohydrogels were synthesized and deposited spontaneously on tannic acid (TA)-modified polyethylene (PE) plates. Subsequently, TA was introduced onto PNIPAAm-APTES nanohydrogels to fabricate coatings composed of TA-modified PNIPAAm-APTES (PNIPAAm-APTES-TA).

Biflavones inhibit the fibrillation and cytotoxicity of the human islet amyloid polypeptide.

Biflavones are a kind of natural compound with a variety of biological activities, which have the capability of reversing diabetes and neurodegenerative diseases. The human islet amyloid polypeptide (hIAPP) is closely related to the pathological process of type II diabetes mellitus (T2DM). The development of new inhibitors is crucial to prevent hIAPP aggregation against T2DM.

Triterpenoids impede the fibrillation and cytotoxicity of human islet amyloid polypeptide.

The inhibition of human islet amyloid polypeptide (hIAPP) deposition to block its toxicity is an important strategy for the prevention and treatment of type II diabetes mellitus (T2DM).Natural compounds with pharmacological properties and low toxicity can serve as a good point to discover potential inhibitors of protein misfolding, which may be useful for the treatment of various amyloidosis-related diseases. Previous studies have reported that triterpenoids, such as maslinic acid (MA) and momordicin I (MI), can modulate glucose metabolism partially by reducing insulin resistance.

Procyanidine resists the fibril formation of human islet amyloid polypeptide.

Human islet amyloid polypeptide (hIAPP) is widely studied due to its close correlation with the pathogenic mechanism of type II diabetes mellitus (T2DM). Bioflavonoids have been used in the neurodegeneration and diabetes studies. However, the structure-activity relationship remains unclear in many of these compounds.

Resistance of nepetin and its analogs on the fibril formation of human islet amyloid polypeptide.

The self-aggregation of human islet amyloid polypeptide (hIAPP) into toxic oligomers and fibrils is closely linked to the pathogenesis of type II diabetes mellitus. Inhibitors can resist hIAPP misfolding, and the resistance can be considered an alternative therapeutic strategy for this disease. Flavones have been applied in the field of diabetes research, however, the inhibition mechanism of many compounds on the fibril formation of related pathogenic peptides remains unclear.

Tetracycline derivatives resist the assembly behavior of human islet amyloid polypeptide.

The misfolding of amyloid proteins is closely correlated with the pathogenesis of protein conformation-related diseases, such as Alzheimer's disease (AD), prion disease, and type 2 diabetes mellitus (T2DM). The deposition of human islet amyloid polypeptide (hIAPP) and amyloid-β (Aβ) protein is entangled in AD and diabetes mellitus. The development of potential inhibitors is a feasible therapeutic strategy to treat these diseases by resisting peptide aggregation.

Regulation of Artemisinin and Its Derivatives on the Assembly Behavior and Cytotoxicity of Amyloid Polypeptides hIAPP and Aβ.

The misfolding and aggregation of human islet amyloid polypeptide (hIAPP) and amyloid-β (Aβ) protein are closely associated with type 2 diabetes mellitus (T2DM) and Alzheimer's disease, respectively. Inhibitors of amyloid peptides include short peptides, aromatic organic molecules, nanoparticles, and even metal compounds. Sesquiterpenoid artemisinins are widely used in anti-malaria treatments, and they may modulate glucose homeostasis against diabetes.

Assembly behavior of amylin fragment hIAPP19-37 regulated by Au(III) complexes.

Human islet amyloid polypeptide (hIAPP, amylin) may self-aggregate and rupture the membrane of β cells, which is closely correlated with the pathogenesis of type 2 diabetes mellitus (T2DM). Hence, suppressing amyloidogenic hIAPP may be beneficial for the treatment of diabetes. As an important part of hIAPP, the fragment hIAPP19-37 was studied in this work to explore their disaggregation and cellular behavior regulation by some selected Au complexes, as follows: dichloro diethyl dithiocarbamate Au complex [AuCl(DDTC)] (1), dichloro pyrrolidine dithiocarbamate Au complex [AuCl(PDT)] (2), dichloro 4-4'-dimethyl-2,2'-bipyridyl Au(III) chloride [AuCl(Me)bpy]Cl (3), and dichloro 4-4-di-tert-butyl-2,2'-bipyridyl Au(III) chloride [AuCl(t-Bu)bpy]Cl (4).

Inhibitory effects of oxidovanadium complexes on the aggregation of human islet amyloid polypeptide and its fragments.

Human islet amyloid polypeptide (hIAPP) is synthesized by pancreatic β-cells and co-secreted with insulin. Misfolding and amyloidosis of hIAPP induce β-cell dysfunction in type II diabetes mellitus. Numerous small organic molecules and metal complexes act as inhibitors against amyloid-related diseases, justifying the need to explore the inhibitory mechanism of these compounds.

Influence of methionine-ruthenium complex on the fibril formation of human islet amyloid polypeptide.

The abnormal aggregation and deposition of human islet amyloid polypeptide (hIAPP) are implicated in the pathogeny of type 2 diabetes mellitus (T2DM). Many aromatic ring-containing Ru complexes inhibit the aggregation of hIAPP. A new Ru complex Ru(bipy)(met)·3HO (1), where bipy is 2,2'-bipyridine and met is methionine, was synthesized and employed to resist the fibril formation of hIAPP and to promote the biocompatibility of metal complexes.

Regulation of heteronuclear Pt-Ru complexes on the fibril formation and cytotoxicity of human islet amyloid polypeptide.

The deposition of human islet amyloid polypeptide (hIAPP) is considered as a causative factor of type 2 diabetes mellitus (T2DM). Developing effective inhibitors against the fibril formation of hIAPP is a potential way to treat T2DM. Recent studies indicate that various metal complexes including homo-binuclear Ru complexes can inhibit hIAPP aggregation.

Schiff base oxovanadium complexes resist the assembly behavior of human islet amyloid polypeptide.

The misfolding and fibrillation of human islet amyloid polypeptide (hIAPP) is related to the pathologic process of type II diabetes mellitus (T2DM). The inhibitors of hIAPP aggregation include aromatic organic molecules, short peptides, and metal complexes. Vanadium complexes have been applied for the treatment of diabetes since the 19th century.

Regulation of the aggregation behavior of human islet amyloid polypeptide fragment by titanocene complexes.

The aggregation of human islet amyloid polypeptide (hIAPP) is associated with type II diabetes. The misfolding of hIAPP induces amyloid deposition and causes β-cell dysfunction. Metal complexes are potential metallodrugs that may reverse the aggregation of amyloid peptides.