Abstract In this study, we attempted to prepare novel angiotensin I-converting enzyme inhibitory (ACEI) peptides from Tie Guanyin tea residue protein (TTRP). Different proteases were used to hydrolyze TTRP to prepare ACEI peptides, neutral protease and alkaline protease hydrolysates exhibited higher ACEI activity and was chosen in further hydrolysis treatment. Response surface methodology (RSM) was used to optimize the enzymatic condition, and the results indicated that the optimal conditions of enzymatic hydrolysis were: 4% (w/v) of TTRP in water was hydrolyzed with 3500 U/g neutral protease at 50 °C and pH 6.5 for 2.5 h in the first step and then with 5000 U/g alkaline protease at 50 °C and pH 10.0 for 3 h in the second step. Under the optimum condition, the ACE inhibitory rate of the final products was 88.45% ± 0.45% at the concentration of 1.0 mg/mL. Moreover, ACEI peptides derived from TTRP showed good stability under different temperatures, pHs, metal ions and gastrointestinal digestion. These results indicated that the TTRP has potential to be used for preparing ACEI peptides.

PURPOSE: To systematically evaluate the clinical efficacy of reamed and nonreamed intramedullary nailing in treatment of closed tibial fractures with Cochrane systematic review methods. METHODS: According to the Cochrane systematic review methods, literatures were retrieved from Cochrane library, PubMed, EMbase and other database. Randomized controlled trials (RCTs) and quasi-randomized controlled clinical trials about reamed and nonreamed intramedullary nailing in the treatment of closed tibial fractures were collected and RevMan 5.0 was chosen for meta-analysis. RESULTS: A total of seven studies were included in this meta-analysis. Reamed intramedullary nailing was better than nonreamed intramedullary nailing in nonunion rate [P = 0.02, RR = 0.46, 95% CI: (0.24, 0.91)] and implant failure rate [P <0.0001, RR = 0.36, 95% CI: (0.22, 0.57)]. No statistically significant difference was observed in malunion rate, compartment syndrome rate, postoperative infection [P = 0.18, RR = 0.50, 95% CI: (0.18, 1.383); P = 0 43, RR = 0.77, 95% CI: (0.40, 1.48); P = 0.27, RR = 0.38, 95% CI: (0.01, 7.87)]. CONCLUSION: Compared with the nonreamed intramedullary nailing, reamed intramedullary nailing can lead to better outcome in the treatment of closed tibial fractures.

O campo emergente da engenharia molecular de metaloproteínas visa preparar proteínas artificiais, cujas propriedades podem imitar e talvez até mesmo melhorar várias características encontradas nas metaloenzimas naturais. Este artigo de revisão resume nossos esforços recentes na preparação de metaloproteínas sintéticas, construídas a partir de "coiled-coils" alfa-hélices, e na incorporação de grupos de transferência de elétrons nesses sistemas. Recentemente, concebemos uma cisteína contendo um peptídeo com hélice randômica, o qual forma uma estrutura "coiled-coil" alfa-helicoidal ao se ligar a vários metais. O aduto de CuI pode atuar como agente fotoindutor de transferência de elétrons para receptores exógenos, e transfere elétrons por colisão na região invertida de Marcus para várias aminas de rutênio, as quais atuam como receptores. Especula-se que este resultado inesperado advenha do posicionamento do cofator de CuI no interior da porção hidrofóbica da proteína, o qual proíbe a aproximação entre o doador e o receptor, diminuindo a velocidade de transferência eletrônica daquelas reações termodinamicamente muito favorecidas, para velocidades inferiores à do limite difusional.

The emerging field of metalloprotein design seeks to prepare artificial proteins whose properties can mimic, enhance, and perhaps improve upon many features found in natural metalloenzymes. This review summarizes our recent efforts to prepare synthetic metalloproteins built from alpha-helical coiled-coils and to incorporate electron-transfer functionality within these systems. We have recently designed a cysteine-containing random-coil peptide which forms a alpha-helical coiled-coil upon binding various metals. The CuI adduct can serve as photoinduced electron-transfer agent to exogenous acceptors and undergoes collisional electron-transfer in the inverted Marcus region to various ruthenium ammine acceptors. It is speculated that this unexpected result might be due to the positioning of the CuI cofactor within the hydrophobic core of the protein which prohibits close approach between the donor and acceptor to slow the high driving force reaction rates below the diffusion limit.