Leucine Structured Peptides

250% Greater Muscle Growth!

Structured Peptides are absorbed faster, utilized better, and produce 250 percent greater muscle growth than free-form amino acids.

BIOTEST® Leucine and BCAA Structured Peptides are produced from peptide enhanced whey-protein isolate, utilizing a three-step process:

1. Whey-protein isolate is hydrolyzed into very small peptide forms using a combination of selective enzymes (aminopeptidases and proteases) to break apart targeted leucine peptide and BCAA-peptide bonds.
2. Afterward, small peptide formations are extracted from the hydrolyzed whey by passing the mixture through a series of filters, ending with nanofiltration.
3. Next, the nano-mixture undergoes a final reaction phase to further enhance its total leucine and BCAA content.

The end result is a highly refined mixture of leucine and BCAA di- and tripeptides that provides the body with the greatest effects from leucine/ BCAA supplementation.

Di- and Tripeptide Science

• Unlike regular (free-form) amino acids, the uptake of di- and tripeptides is achieved through a very specific, high-capacity intestinal transporter (PEPT-1), which can lead to a larger and more rapid spike in blood levels of these crucial anabolic signals.

Leucine Science

• Most of the anabolic effects of protein are actually the result of a single amino acid – leucine. Only slight elevations in all of the other essential amino acids are necessary for leucine to spark (and maintain) increases in muscle protein synthesis.
• Leucine is the amino-acid "trigger" by which skeletal muscle accrues protein. Specifically, the muscle-building effects of leucine are due to a cascade of cellular reactions including the activation of the mammalian target of rapamycin (mTOR), upregulation of ribosomal protein S6 kinase (S6K1) activity, enhancement of eukaryotic initiation factor-4E binding protein (eIF4E-BP1) phosphorylation, and the association of eukaryotic initiation factor (eIF)4E with eIF4G. These effects have been shown to occur both in vitro and in humans.
• Estimates of dietary requirements for leucine range from 1 g to 12 g daily. The amount of leucine necessary to optimize performance and muscle growth is unknown, but recent research in humans points to a plateau effect (at least on muscle protein synthesis) occurring around 3.5 grams per meal.
• As we get older, muscles become less sensitive to the anabolic effects of insulin, protein, and amino acids (including leucine). As a result, peri-workout nutrition becomes more important to maximize our overall health and performance.
• Leucine oxidation by muscle can be reduced by co-ingesting a high-quality carbohydrate, an effect that in theory should increase the anabolic signal to muscle growth.
• Although theoretical at this point in time, key leucine di- and tripeptides may turn out to provide extraordinary muscle-building benefits.

Leucine References

Norton LE and Layman DK.

Leucine regulates translation initiation of protein synthesis in skeletal muscle after exercise. J Nutr. 2006; 136(2):533S-537S.

Frexes-Steed M, Lacy DB, Collins J & Abumrad NN (1992).

Role of leucine and other amino acids in regulating protein metabolism in vivo. Am J Physiol 262, E925–E935.

Katsanos CS, Kobayashi H, Sheffield-Moore M, Aarsland A & Wolfe RR (2005).

Aging is associated with diminished accretion of muscle proteins after the ingestion of a small bolus of essential amino acids. Am J Clin Nutr 82, 1065–1073.

Rieu I, Balage M, Sornet C, Giraudet C, Pujos E, Grizard J, Mosoni L, Dardevet D.

Leucine supplementation improves muscle protein synthesis in elderly men independently of hyperaminoacidaemia. J Physiol. 2006 Aug 15;575(Pt 1):305-15.

Tipton KD, Ferrando AA, Phillips SM, Doyle Jr, Wolfe RR.

Postexercise net protein synthesis in human muscle from orally administered amino acids. Am J Physiol. 1999 Apr;276(4 Pt 1):E628-34.