Freer Hall
Urbana, Illinois, 61801, United States
NCT Number: NCT03952884
Skeletal muscle quality is an important determinant of exercise performance and overall health. It is vital for not just movement, but also metabolizing nutrients. Protein from the diet can promote muscle protein synthesis for muscle recovery and growth. More importantly, doing so shifts net protein balance positively (e.g. protein synthesis is greater than protein breakdown) and promotes greater rates of muscle protein turnover. Leucine is an amino acid required to build muscle, but it also acts as a signaling molecule informing the muscle to start protein synthesis. Before reaching skeletal muscle, dietary protein is digested into small peptides and free amino acids. Rate of absorption from the intestine to the blood stream is significantly faster for peptides compared to amino acids. As amino acid availability in the blood is a precursor for muscle protein synthesis, our objective is to determine if the different absorption rates between free amino acid and peptides influence muscle protein synthetic and breakdown rates.
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Notify Me18 year–35 year
All sexes
Interventional
Not applicable
Urbana, Illinois, 61801, United States
Healthy volunteers accepted: Yes
Only the study team can determine whether someone qualifies for participation.
Inclusion criteria
Exclusion criteria
Prior to protein consumption participants will perform an acute bout of resistance exercise. They will warm up with two sets of 10 repetitions at 35-75% working load respectively, then perform four working sets of 10-12 repetitions at 65-70% of 1-RM. 1 min, 30 sec rest periods will be implemented between each set.
Participants allocated to this group will not perform exercise prior to the administration of the nutritional intervention. Participants will remain at rest throughout the trial.
Participants will be given 2g of leucine dissolved in 250mL of water. Drink will be consumed immediately after exercise or equivalent time point for non-exercise group.
Participants will be given 2g of dileucine dissolved in 250mL of water. Drink will be consumed immediately after exercise or equivalent time point for non-exercise group.
Time frame: Postabsorptive for 3.5 hours, Postprandial for 3 hours.
Mixed muscle protein synthesis rates will be assessed during the 3.5hr Postabsorptive period (e.g. non-fed state) and the 3hr postprandial period (e.g. fed state) for both experimental interventions (e.g. leucine and leucine peptide). This will allow us to assess the change in fractional synthetic rate from the Postabsorptive period to the postprandial period.
Time frame: Postabsorptive for 3.5 hours, Postprandial for 3 hours.
Myofibrillar muscle protein synthesis rates will be assessed during the 3.5hr Postabsorptive period (e.g. non-fed state) and the 3hr postprandial period (e.g. fed state) for both experimental interventions (e.g. leucine and leucine peptide). This will allow us to assess the change in fractional synthetic rate from the Postabsorptive period to the postprandial period.
Time frame: Postprandial for 1 hour
Mixed muscle protein breakdown rates will be assessed during the first hour of the postprandial period (e.g. fed state) for both experimental interventions (e.g. leucine and leucine peptide). This will allow us to assess the change in fractional breakdown rate for each respective experimental intervention.
Time frame: Baseline, immediately after ingestion of leucine/leucine peptides, and 3 hours after ingestion of leucine/leucine peptides
Phosphorylation of anabolic signaling pathways will be assessed in the fasted state and after the ingestion of the experimental interventions.
University of Illinois at Urbana-Champaign
Other
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