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Objective Obesity in the United States continues to increase. Time restricted feeding (TRF) is a dietary intervention that has potential to serve as an effective weight loss strategy, however more data is needed to establish the effectiveness of a TRF eating pattern on health outcomes related to obesity. To our knowledge, manipulation of macronutrient distribution during a TRF intervention and the effect of TRF on sleep and mood have not been studied. Therefore, the objective of this study was to determine the effect of protein supplementation during TRF on mood, sleep, and appetite in overweight and obese adults. Methods Overweight and obese men and women (36.6±7.3 years; BMI: 32.8±6.5) participated in this randomized, controlled 12‐week dietary intervention. Participants were allocated to one of two groups: 1) control, TRF (n=7) and 2) TRF with whey protein supplementation (25 g/d; n=9). Protein supplements were consumed at the breaking of the fasting period each day. Anthropometrics, sleep (via Pittsburgh Sleep Quality Index Global Sleeping Score; PSQI GSS), total mood disturbances (TMD; via Profile of Mood States (POMS) including six affect states of depression, fatigue, anger, tension, confusion, and vigor subscales), and appetite (using visual analog scales) were assessed at 0, 4, 8, and 12 weeks. Sleep was also measured at 0 and 12 weeks via wrist Actigraphy. Body composition was measured via DXA at 0 and 12 weeks. Data was analyzed using two‐way ANOVA to assess the relationship. Results Overall, both interventions improved total body fat percentage (p<0.05) over 12 weeks. There was a significant difference in mood between intervention groups (p<0.001) and the control group total mood disturbance was significantly different (p<0.05) between week 1 and 12. However, there was no change in mood with protein supplementation over the span of 12 weeks. Sleep, self‐reported via PSQI, did not change from week 1 and week 12 within or between each of the interventions. Appetite did not show a significant difference between interventions or time points. Conclusions This pilot study suggests that protein supplementation during TRF has the potential to improve body composition in overweight and obese individuals. However, additional research is needed to determine the long‐term effect of protein supplementation in combination with TRF on mood, sleep, and appetite.

The research-teaching nexus is the pinnacle of academic activity. As a scientist and educator, my overall objective is to give students access to cutting-edge research and help them develop high order inquiry skills. In addition, as research and thesis writing frequently involves the development of new complex reading skills associated with comprehension and synthesis of a tremendous volume of information, along with in-depth critical analysis, evaluation, and elegant academic writing style, I decided to assign this editorial to my 2020-Biochemical Nutrition graduate students. As my students have diverse educational and cultural backgrounds and have been exposed to a variety of tech-based learning, we decided to summarize here recent advances in omics research in avian species to facilitate the discussion by asking new questions, which may help open new vistas for future investigations. By following the “scaffolded” approach, my students highlighted progress in Transcriptomics (Komp M and Bowie R), Proteomics (Tabler T and Lee T), Kinomics (Hernandez RM and Zuo B), Epigenomics (Ferver A), Metabolomics (Maynard C and Mullenix G), and Microbiomics (Teyssier JR and Bodle B). I would like to thank my students for their motivation, dedication, determination, perseverance, connection, consistency, and support. I would also like to thank AFTNS-OJ for inviting me to write this editorial and I hope by getting my students involved would promote their curiosity, help them understand complex questions, explore more sources, stimulate their independent thinking, and create research- and question-mindsets.

Skeletal muscle (SM) is vital for both long term health and quality of life. Recent research suggests an increase in catabolic signals with age triggers pathologic conditions, such as sarcopenia. Although results from in vitro studies model how essential amino acids (EAA) can regulate muscle protein synthesis (MPS), the relevance of these models to muscle protein breakdown (MPB), and the presence of physiological plasma amino acid concentrations (PAA) remain to be established. Therefore, the objective of this study was to determine the effects of EAA with (0.2, 1.0, and 3.0 x PAA) in a young (passages 2‐10) and aging (passages 16‐24) C2C12 murine muscle cell model. We hypothesized that increased levels of EAA will increase MPS in aging cells and suppress MPB via the mTORC1 pathway when compared to young cells. Myoblasts were seeded (1x105) into 6‐well plates and differentiated into myotubes when they reached 80% confluency. Myotubes were serum and AA starved for 24 hours before receiving one of the following treatments: control (CON), 0.2 x PAA, 1.0 x PAA, 3.0 x PAA with or without rapamycin (100 nm; RAP) for 1, 6, and 24 hours. All treatments were performed in triplicate and then each experiment was repeated three times, yielding nine wells per treatment. Proteins related to sensing of AA and protein synthesis and degradation were assessed using Western Blot. Rapamycin inhibited phosphorylation of p70 S6 kinase 1 (p70S6K1) and 4E binding protein 1 (4E‐BP1), downstream targets of mTORC1, in both CON and AA‐treated young and aged cells. Phosphorylation of 4EBP1 and p70S6K1 was significantly increased (p<0.05) in both young and aged cells following all PAA treatments. However, there was no significance after 24 hours of AA supplementation in aged cells. Particularly, after 6 hours of treatment all doses significantly increased (p<0.0001) phosphorylation of p70S6K1 in both young and aged cells. 0.2 x PAA and 3.0 x PAA elicited a significantly greater response in 4EBP1 phosphorylation in young cells compared to the CON after 6 hours of treatment, whereas a dose of 3.0 x PAA induced a similar response in aged cells. In conclusion, in a C2C12 myotube model, increasing EAA concentrations downregulates the expression of translation initiation factors in young and aging cells. Specifically, it takes a 3.0 x PAA to elicit a response in aging cells, whereas young cells respond to lower physiological concentrations of 0.2 x PAA and 1.0 x PAA. Therefore, it can be proposed increasing EAA may be effective for adjusting the rate of MPS and MPB via the mTORC1 pathway in both young and aging muscle cells.