Leucine and BCAA 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:
- – 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.
- – Afterward, small peptide formations are
extracted from the hydrolyzed whey by passing the mixture through a series of
filters, ending with nanofiltration.
- – 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.
BCAA Science
- The branched-chain amino acids (BCAA) consist of the essential
amino acids leucine, isoleucine, and valine.
- BCAA account for approximately 35% of the essential amino acids
in muscle.
- In contrast to most essential amino acids that are metabolized in
the liver, BCAA are unique because they are metabolized primarily in
skeletal muscle. This fact also explains why BCAA are used to help patients with
liver failure retain their lean mass. BCAA are also used in
the management of tardive dyskinesia, amytrophic lateral sclerosis (ALS),
hepatic encephalopathy, and phenylketonuria.
- Numerous studies have demonstrated the anti-catabolic effects of
(free form) BCAA administration, i.e., a reduction in muscle protein
breakdown during clinical conditions of wasting (e.g., starvation,
post-surgery, burns, liver disease, etc.).
- BCAA have been theorized to act as a metabolic fuel during
exercise, particularly during intense and/or prolonged physical activity. This
effect "spares" muscle glycogen during training, at least when BCAA are taken
pre-exercise.
- BCAA also donate nitrogen (via transamination) to non-essential amino
acids. This phenomenon explains why not all amino acids are necessary to
stimulate protein synthesis.
- Proponents of BCAA supplementation maintain that BCAA may blunt the
increase in serotonin, thus reducing perceived effort and mental fatigue
during prolonged exercise, and here's why:
BCAA contribute to the synthesis of neurotransmitters. As such, supplementing with
BCAA during prolonged exercise could, in theory, increase the mental
effort necessary to maintain (or extend) higher performance levels. This
conclusion is based on the well-known "Central Fatigue Hypothesis," which
suggests that prolonged exercise decreases BCAA and increases fatty acids in
circulating blood, resulting in elevated tryptophan levels. And tryptophan is the
amino-acid precursor to serotonin, a neurotransmitter that causes feelings of
sleepiness and (in excess) depression.
- A few recent studies have shown that men and women who
ingest approximately 10 to 15 grams of BCAA per day (comprised of 5-7 g leucine,
3-4 g isoleucine, and 3-4 g valine) for at least four-weeks increase their lean
mass more than matched control subjects. This effect appears to be the result of
a BCAA-induced increased protein synthesis during the recovery period following
resistance exercise.
- Another interesting aspect of BCAA that has only recently been
explored is the potential effect on weight loss. During moderate protein intake
(1.5 grams/kg of body weight per day) and a lower carbohydrate (100-200
grams/day) diet, an increased intake of BCAA is thought to have positive
effects on muscle protein synthesis, insulin signaling, and sparing of
glucose use by stimulation of the glucose-alanine cycle. This may lead to more
fat loss and a greater sparing of lean tissue compared to a
calorically-matched, higher carbohydrate diet.
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.
BCAA References
Blomstrand E, Ek S, Newsholme EA. Influence of ingesting a solution of
branched chain amino acids on plasma and muscle concentrations of amino acids
during prolonged submaximal exercise. Nutrition 1996;12:485-490.
Blomstrand E, Hassmen P, Ek S, et al. Influence of ingesting a solution of
branched chain amino acids on perceived exertion during exercise. Acta
Physiol Scand. 1997;159:41-49.
Blomstrand E, Hassmen P., et al. Administration of branched chain amino acids
during sustained exercise-effects on performance and plasma concentration of
some amino acids. Eur J Appl Physiol 1991;63:83-88.
Blomstrand E, Saltin B. BCAA intake affects protein metabolism in
muscle after but not during exercise in humans. Am J Physiol
Endocrinol Metab. 2001 Aug;281(2):E365-74.
Candeloro N, Bertini I, Melchiorro G, DeLorenzo A. Effects of prolonged
administration of branched chain amino acids on body composition and physical
fitness. Minerva Endocrinol 1995;20(4):217-223.
Layman DK, Baum JI. Dietary protein impact on glycemic control
during weight loss. J Nutr. 2004 Apr;134(4):968S-73S.
Madsen K, Maclean DA. Et al. Effects of glucose, glucose plus branched chain
amino acids, or placebo on bike performance over 100 km. J Appl
Physiol. 1996;81:2644-2650.
Mourier A, Bigard AX, deKerviler E, et al. Combined effects of caloric
restriction and branched chain amino acid supplementation on body composition
and selected performance parameters in elite wrestlers. Int J Sports
Med. 1997;18:47-55.
Shimomura Y, Murakami T, Nakai N, Nagasaki M, Harris RA. Exercise
promotes BCAA catabolism: effects of BCAA supplementation on skeletal muscle
during exercise. J Nutr. 2004 Jun;134(6 Suppl):1583S-1587S.