Hexamerin and allergen are required for female reproduction in the American cockroach, Periplaneta americana.

Reproduction is of great importance for the continuation of the species. In insects, the fat body is the major tissue for nutrient storage and involved in vitellogenesis, which is essential for female reproduction. Here, 2 proteins, hexamerin and allergen, were separated from the fat bodies of adult female American cockroaches (Periplaneta americana) and identified as storage proteins, encoding for 733 amino acids with molecular weight of 87.88 kDa and 686 amino acids with molecular weight of 82.18 kDa, respectively. The encoding genes of these 2 storage proteins are mainly expressed in the fat body. RNA interference-mediated knockdown of Hexamerin and Allergen in the early stage of the first reproductive cycle in females suppressed vitellogenesis and ovarian maturation, indicating that these storage proteins are involved in controlling reproduction. Importantly, the expression of Hexamerin and Allergen was repressed by knockdown of the juvenile hormone (JH) receptor gene Met and the primary response gene Kr-h1, and was induced by methoprene, a JH analog, in both in vivo and in vitro experiments. Altogether, we have determined that hexamerin and allergen are identified as storage proteins and play an important role in promoting female reproduction in the American cockroach. The expression of their encoding genes is induced by JH signaling. Our data reveal a novel mechanism by which hexamerin and allergen are necessary for JH-stimulated female reproduction.

Inhibitory potential of 4-hexylresorcinol against α-glucosidase and non-enzymatic glycation: Activity and mechanism.

Inhibition of α-glucosidase as well as non-enzymatic glycation is thought as an effective method for treating type-2 diabetes mellitus. In this study, we investigated the inhibitory potential and mechanism of 4-hexylresorcinol against α-glucosidase and non-enzymatic glycation by using multispectroscopic analyses and molecular docking. The results of enzyme kinetics showed that 4-hexylresorcinol reversibly inhibited α-glucosidase activity in a noncompetitive way. Fluorescence quenching then revealed that it increased the hydrophobicity of α-glucosidase and changed the conformation of the enzyme by forming the α-glucosidase-hexylresorcinol complex. Thermodynamic analysis and molecular docking further demonstrated that the inhibition of 4-hexylresorcinol on the α-glucosidase was mainly dependent on hydrogen bond and hydrophobic interaction. Moreover, the 4-hexylresorcinol moderately inhibited the formation of fructosamine, and strongly suppressed the generation of α-dicarbonyl compounds and advanced glycation end products (AGEs). The interaction between 4-hexylresorcinol and bovine serum albumin was mainly driven by hydrophobic interaction. This study showed a novel inhibitor of α-glucosidase as well as non-enzymatic glycation, and provided a drug candidate for the prevention and treatment of type-2 diabetes.