GEC1-kappa Opioid Receptor Binding Involves Hydrophobic Interactions GEC1 has Chaperone-Like Effect

We demonstrated previously that the protein GEC1 (glandular epithelial cell 1) bound to the human κ opioid receptor (hKOPR) and promoted cell surface expression of the receptor by facilitating its trafficking along the secretory pathway. Here we showed that three hKOPR residues (Phe345, Pro346, and Met350) and seven GEC1 residues (Tyr49, Val51, Leu55, Thr56, Val57, Phe60, and Ile64) are indispensable for the interaction. Modeling studies revealed that the interaction was mediated via direct contacts between the kinked hydrophobic fragment in hKOPR C-tail and the curved hydrophobic surface in GEC1 around the S2 β-strand. Intramolecular Leu44-Tyr109 interaction in GEC1 was important, likely by maintaining its structural integrity. Microtubule binding mediated by the GEC1 N-terminal domain was essential for the GEC1 effect. Expression of GEC1 also increased cell surface levels of the GluR1 subunit and the prostaglandin EP3.f receptor, which have FPXXM and FPXM sequences, respectively. With its widespread distribution in the nervous system and its predominantly hydrophobic interactions, GEC1 may have chaperone-like effects for many cell surface proteins along the biosynthesis pathway

In situ tailored strategy to remove capping agents from copper sulfide for building better lithium–sulfur batteries

Capping agents are frequently used in the chemical synthesis of materials, to precisely tailor the size, shape, and composition, with the expectation of high-performance catalysis. However, the adsorbed capping agents also serve as a physical barrier to restrict the interaction between reactants and catalytically active sites on the material surface. In this article, an in situ tailored interface strategy is introduced for effectively removing capping agents (long-chain oleylamine) from the surface of copper sulfide, to maximize the catalytic activity. The interface long-chain molecules of oleylamine are replaced by the inorganic S2- ion via a facile stirring approach without harsh processing conditions or the need for additional non-commercial materials. The as-cleaned copper sulfide shows greatly enhanced activity toward lithium-sulfur batteries, with an impressive current rate, excellent cycling stability, and great rate capability. These "clean surface"strategies using interface engineering provide a significant insight into the structure-activity relationships to support advancements in electrocatalysis technology in lithium-sulfur batteries. This journal i

GEC1-κ Opioid Receptor Binding Involves Hydrophobic Interactions: GEC1 HAS CHAPERONE-LIKE EFFECT*S⃞

We demonstrated previously that the protein GEC1 (glandular epithelial cell 1) bound to the human κ opioid receptor (hKOPR) and promoted cell surface expression of the receptor by facilitating its trafficking along the secretory pathway. Here we showed that three hKOPR residues (Phe345, Pro346, and Met350) and seven GEC1 residues (Tyr49, Val51, Leu55, Thr56, Val57, Phe60, and Ile64) are indispensable for the interaction. Modeling studies revealed that the interaction was mediated via direct contacts between the kinked hydrophobic fragment in hKOPR C-tail and the curved hydrophobic surface in GEC1 around the S2 β-strand. Intramolecular Leu44-Tyr109 interaction in GEC1 was important, likely by maintaining its structural integrity. Microtubule binding mediated by the GEC1 N-terminal domain was essential for the GEC1 effect. Expression of GEC1 also increased cell surface levels of the GluR1 subunit and the prostaglandin EP3.f receptor, which have FPXXM and FPXM sequences, respectively. With its widespread distribution in the nervous system and its predominantly hydrophobic interactions, GEC1 may have chaperone-like effects for many cell surface proteins along the biosynthesis pathway