Free Form Amino Acids should be taken with Hydrosylates or Whey ONLY or crap

[eryanb]

By the way I don't expect any of you to just take my word for it. I have a degree in Biochemistry and I just learned this recently myself! They can't teach you everything.

So I'm excited to share the info (here is the link):

http://www.frot.co.nz/dietnet/basics/protein_whey.htm.

The guy who wrote this article is Michael Colgan who is a former senior member of the Science Faculty of the University of Auckland. He is an author, lecturer and head of the Colgan Institute of Nutritional science in the United States.

Here is a direct quote from that site:

"The unique chemical shapes these bonds create, are information keys that fit the enzyme locks in your body to switch on protein functions. Without the keys to open the doors of the cells, you can throw all the denatured proteins you like at your muscles, but hardly any gets retained.

That's also why all those mixtures of pure singular free-form amino acids are virtually useless for building muscle, even those whose amino acid profile exactly matches that of ideal protein. Despite all the promotional hokum and untold millions in sales over the last 40 years, amino acid blends are virtually useless, because they lack the chemical keys that fit your body locks. The only way your body can use them is by piggybacking on any spare keys provided by the food proteins you eat.

To be fair to amino promoters, science revealed these protein mechanisms only in the last decade. I detail the research in my book Optimum Sports Nutrition but briefly, the unique chemical shapes created by di-peptide and tri-peptide bonds are the keys to optimum protein metabolism. Your body recognises and absorbs di-peptides and tri-peptides by a special pathway that cannot be used by single amino acids. Most aminos in your blood are in di-peptide and tri-peptide form. Peptide protein formulas that preserve the essential bonds, allow the body to retain twice the protein retained from whole protein foods, and up to seven times the protein retained from blends of singular amino acids.

Let's look at the di-sulphide bond in the tri-peptide formed by glutamine and two molecules of cysteine. This glutamine-cysteine key is crucial for both protein retention and immunity. Most common proteins don't contain these di-sulphide bonds. Unprocessed egg white has a small amount. Unprocessed whey protein contains a bundle. But they are completely destroyed by usual extraction methods that use heat and acids."

[Anssi Manninen]

Largely nonsense.

[eryanb]

Largely nonsense.

Is that an objective or subjective opinion my friend? I can list several solid references from peer reviewed journals as well as solid theory from my old biochemistry textbook.

I love to learn. You seem to have a definitive and strong position here. Could you please list a few of your favourite articles supporting the bioavailability of free form amino acids and the effect of dipeptides on this bioavailability?

[AphtaLyfe]

Very interesting read.

Seems pretty legit too... I read some of the articles and couldn't find 1 red flag.

The study makes sense to me.

It doesn't however say how much/many "keys" you need per amount of "bad" protein that is "piggybacking."

So the blend in ON 100% whey (the kind I use) could possibly be the best bang for your buck.

Since it has all 4 types (different ways whey can be processed) of protein along with digestive enzymes.

The article also explains why the huge amount of milk I used to drink... did not seem to positively effect my muscle growth at all..

I might be switching to a whey isolate in the near future though.... the article seems to have plenty of evidence to back it up.

-Thanks for posting

[Anssi Manninen]

[QUOTE=eryanb;56483511]Is that an objective or subjective opinion my friend? I can list several solid references from peer reviewed journals as well as solid theory from my old biochemistry textbook.

Objective. That Colgan article is largely nonsense.

[eryanb]

Objective. That Colgan article is largely nonsense.

OK. But unless you give at least one respectable reference I have to assume subjective.

I don't have my articles saved on my laptop. I'm going to login to SciFinder at my University this week and dig up the latest research.

But from the theoretical standpoint it makes perfect sense to me. I know for a fact that not even water passes though cell membranes without specific selective water transport channels. The same goes in spades for AA's. There is a mass of research demonstrating major bioavailabilty of peptides solutions. Like glutamine peptides are 10X more bioavailable than free form glutamine.

Anyway, you must have some pretty good articles yourself to be so sure....so please just share one or two with us.

Much thanks for your input.

[Anssi Manninen]

Peptides are indeed more bioavailable than free form aminos but the claim that free aminos are useless is simply ridiculous.

[DriverDan]

There is a LOT of research that shows free form aminos to be effective, especially in the presence of CHO.

[DriverDan]

Euglycemic hyperinsulinemia augments amino acid uptake by human leg tissues during hyperaminoacidemia
Timing of amino acid-carbohydrate ingestion alters anabolic response of muscle to resistance exercise

That's all I have bookmarked but I'm sure you can lookup a plethora of other studies.

[v4lu3s]

Interesting read, and i have read Colgan's work before (copy of Optimum Sports Nutrition sitting right here lol). I would want to know his sources for what he has to say. I noticed that he usually is pretty good at citing his sources, and I notice this article does not cite anything. Is that an oversight of the website or what?

[eryanb]

Hey thanks for the feedback everybody.

I think I'm in agreement that free-form amino acids are NOT CRAP in the strict sense implied by my title and the word "useless" in the quote. I realize I should have been more specific and not so dramatic!

However in the relative sense I consider taking free form amino acids by themselves crap in comparison to being taken with the correct amount of a quick absorbing protein sources such as whey or even better a good hydrosylate (AN/TN > 14% or better).

I mean I'm not at my lab computer right now for accessing articles but I remember figures as high as 10X increase in bioavailability off the top of my head.

Also slightly off topic but related:
Since we all at least take whey anyway it just makes sense to coordinate the supplementation. From a metabolic standpoint I don?t see the point in taking BCAA's without a complete protein source. By themselves they will supply gluconeogenesis needs instead of using your muscles as that supply. So that is good. But lecuine also plays a major regulatory role in protein synthesis. So why upregulate an anabolic state without simultaneously flushing your system with good high quality protein. Same goes for arginine and glutamine they just promote anabolic state in diff. ways.

Another example I found interesting is the study that showed 100% greater insulin response when phenylalanine was combined with hydrosylates and maltodextrin. They screened like 9 or more AA's and found phenylalanine to be most effective. But they needed to combine with whey hydrosylates to get the effect.

[dance2trance]

Also slightly off topic but related:
Since we all at least take whey anyway it just makes sense to coordinate the supplementation. From a metabolic standpoint I don?t see the point in taking BCAA's without a complete protein source. By themselves they will supply gluconeogenesis needs instead of using your muscles as that supply. So that is good. But lecuine also plays a major regulatory role in protein synthesis. So why upregulate an anabolic state without simultaneously flushing your system with good high quality protein. Same goes for arginine and glutamine they just promote anabolic state in diff. ways.

----------------------------------------------------------------
Int J Sport Nutr Exerc Metab. 2004 Jun;14(3):255-71.
Effect of an amino acid, protein, and carbohydrate mixture on net muscle protein balance after resistance exercise.
Borsheim E, Aarsland A, Wolfe RR.

This study tests the hypotheses that (a) a mixture of whey protein, amino acids (AA), and carbohydrates (CHO) stimulates net muscle protein synthesis to a greater extent than isoenergetic CHO alone after resistance exercise; and (b) that the stimulatory effect of a protein, AA, and CHO mixture will last beyond the 1st hour after intake. Eight subjects participated in 2 trials. In one (PAAC), they ingested 77.4 g CHO, 17.5 g whey protein, and 4.9 g AA 1 hr after resistance exercise. In the other (CON), 100 g CHO was ingested instead. They received a primed constant infusion of L-[2H5]-phenylalanine, and samples from femoral artery and vein, and biopsies from vastus lateralis were obtained. The area under the curve for net uptake of phenylalanine into muscle above pre-drink value was 128+/- 42 mg x leg(- 1) (PAAC) versus 32+/- 10 mg x leg (-1) (CON) for the 3 hr after the drink (p =.04). The net protein balance response to the mixture consisted of two components, one rapid immediate response, and a smaller delayed response about 90 min after drink, whereas in CON only a small delayed response was seen. We conclude that after resistance exercise, a mixture of whey protein, AA, and CHO stimulated muscle protein synthesis to a greater extent than isoenergetic CHO alone. Further, compared to previously reported findings, the addition of protein to an AA+ CHO mixture seems to extend the anabolic effect.
--------------------------------------------------------------------


If you're in the know this is nothing new...it is generally accepted that whey + BCAAs (or more importantly, L-Leucine) + carbs are conducive for muscle recovery and growth.

Glucose and L-Leucine are activators of mTOR. Whey protein provides complete profile of amino acids to support protein synthesis.

Not really any new knowledge here...but shows the money spent on NO and Trib supps etc may not be worth the money considering cost vs benefit.


-

[str8flexed]

By the way I don't expect any of you to just take my word for it. I have a degree in Biochemistry and I just learned this recently myself! They can't teach you everything.

So I'm excited to share the info (here is the link):

http://www.frot.co.nz/dietnet/basics/protein_whey.htm.

The guy who wrote this article is Michael Colgan who is a former senior member of the Science Faculty of the University of Auckland. He is an author, lecturer and head of the Colgan Institute of Nutritional science in the United States.

Here is a direct quote from that site:

"The unique chemical shapes these bonds create, are information keys that fit the enzyme locks in your body to switch on protein functions. Without the keys to open the doors of the cells, you can throw all the denatured proteins you like at your muscles, but hardly any gets retained.

That's also why all those mixtures of pure singular free-form amino acids are virtually useless for building muscle, even those whose amino acid profile exactly matches that of ideal protein. Despite all the promotional hokum and untold millions in sales over the last 40 years, amino acid blends are virtually useless, because they lack the chemical keys that fit your body locks. The only way your body can use them is by piggybacking on any spare keys provided by the food proteins you eat.

To be fair to amino promoters, science revealed these protein mechanisms only in the last decade. I detail the research in my book Optimum Sports Nutrition but briefly, the unique chemical shapes created by di-peptide and tri-peptide bonds are the keys to optimum protein metabolism. Your body recognises and absorbs di-peptides and tri-peptides by a special pathway that cannot be used by single amino acids. Most aminos in your blood are in di-peptide and tri-peptide form. Peptide protein formulas that preserve the essential bonds, allow the body to retain twice the protein retained from whole protein foods, and up to seven times the protein retained from blends of singular amino acids.

Let's look at the di-sulphide bond in the tri-peptide formed by glutamine and two molecules of cysteine. This glutamine-cysteine key is crucial for both protein retention and immunity. Most common proteins don't contain these di-sulphide bonds. Unprocessed egg white has a small amount. Unprocessed whey protein contains a bundle. But they are completely destroyed by usual extraction methods that use heat and acids."

i'm sorry but he's full of it

[eryanb]

i'm sorry but he's full of it

Colgan is full of it or me?

[str8flexed]

the guy who wrote the article. I just can't believe a person educated in nutrition would write that nonsense. I do believe free form BCAA have merit but the stuff this guy is spewing is downright nonesense

[dance2trance]

THat was written in 1997. Never in my biomedical undergraduate experience nor in my current biochem & exercise physiol postgrad research have i come across any such notion that di-peptides and tri-peptides are required for the uptake of amino acids.

From my knowledge, hydrolysis of proteins is not a stimulus and is not essential for amino acid uptake. Not saying i am right, but this is my understanding of this facet of amino acid metabolism

[eryanb]

THat was written in 1997. Never in my biomedical undergraduate experience nor in my current biochem & exercise physiol postgrad research have i come across any such notion that di-peptides and tri-peptides are required for the uptake of amino acids.

From my knowledge, hydrolysis of proteins is not a stimulus and is not essential for amino acid uptake. Not saying i am right, but this is my understanding of this facet of amino acid metabolism

Ya me neither. I pretty much memorized Lehninger's Principles of Biochemistry and when I came across this article it really surprised me because I'd never been taught that.

But when I saw it was written by a professor I guess my critical thinking was taken off guard.

I'm going to look for primary literature when I get to school but I definitely believe Layne and you.

Thanks guys....I'm glad I posted this.

[ATHLETIC EDGE NUTRITION]

Man, what has happened to colgan, he used to put out some pretty decent stuff.

[str8flexed]

THat was written in 1997. Never in my biomedical undergraduate experience nor in my current biochem & exercise physiol postgrad research have i come across any such notion that di-peptides and tri-peptides are required for the uptake of amino acids.

From my knowledge, hydrolysis of proteins is not a stimulus and is not essential for amino acid uptake. Not saying i am right, but this is my understanding of this facet of amino acid metabolism

di & tri peptides are normally absorbed faster than free form due to a greater abundance of the transporter for di & tri peptides however, the notion that you need di & tri peptides for uptake of free form is nonsense

[eryanb]

And actually if you look at this reference as well it indirectly supports the notion that peptides can enhance absorption of free form AA's. For instance as Layne pointed out there are more receptors for peptide absorption than free form AA absorption, which partly explains the much better absorptivity of peptides relative to free form AA's.

So why then does the research below conclude that free form arginine has EQUAL bioavailability to peptide bound arginine? My guess is that in both formulations they included casein-wheat gluten or casein-gelatin. So this strong peptide source (after rapid enzymatic hydrolysis in vivo) enhanced the absorption of free form arginine substantially enough that the bioavailability became actually equal to the peptide bound form.

However my more recent reference provides the direct evidence.

Bibliographic Information

Free- and peptide-based dietary arginine supplementation for the South American fish pacu (Piaractus mesopotamicus). Tesser, M. B.; Terjesen, B. F.; Zhang, Y.; Portella, M. C.; Dabrowski, K.. School of Natural Resources, The Ohio State University, Columbus, OH, USA. Aquaculture Nutrition (2005), 11(6), 443-453. Publisher: Blackwell Publishing Ltd., CODEN: AQNUF6 ISSN: 1353-5773. Journal written in English. CAN 144:467289 AN 2005:1336419 CAPLUS

Abstract

Arginine was hypothesized to be a model compd. in the present study on mol. forms of indispensable amino acid (IAA) dietary supplementation. Juvenile South American pacu (Piaractus mesopotamicus) were fed diets contg. arginine in a protein base (casein-wheat gluten or casein-gelatin), or the casein-wheat gluten base supplemented with dipeptide or free arginine at two levels (5 and 10 g kg-1). Growth and protein efficiency ratios were significantly affected by diets, but not by arginine mol. form. Three free dispensable amino acids (DAA) and four IAA in plasma were affected by diet, but plasma arginine concns. did not differ. Plasma urea concns., being very low in the pacu, and hepatic arginase activities, were not affected by diet (P = 0.10 - 0.11), but together with plasma ornithine, mirrored the growth data. Mol. form of arginine supplementation, free or dipeptide, significantly changed several free IAA (Phe, Leu, Ile, His) and urea, with a higher mean plasma concn. in dipeptide fed fish. The dietary treatments, or mol. form of the arginine supplementation, did not change proximate compn., except that calcium levels decreased with higher dietary arginine supplementation level. The present study indicates that dipeptides can provide IAA to pacu, and that arginine supplemented in this form is utilized as efficiently as in free form.

[eryanb]

di & tri peptides are normally absorbed faster than free form due to a greater abundance of the transporter for di & tri peptides however, the notion that you need di & tri peptides for uptake of free form is nonsense

So I agree with both of you that you don't NEED peptides to absorb free form AA's. This was a bad exaggeration on my part since I trusted Colgans credentials too readily.

However from the references I have found (two of them posted here). I conclude that taking peptides that are completely independent of your free form AA can substantially increase the absorption of the free form AA.

Short version. We are all right.

Colgans article was way to oversimplified and basically a spoonfeed it to the public piece which was very misleading and should be removed from the net.

I'm glad we've had this talk. I've learned a few things about exogenous protein transport.

[dance2trance]

Stick with Lehninger

[str8flexed]

everyone makes mistakes.

[NO HYPE]

di & tri peptides are normally absorbed faster than free form due to a greater abundance of the transporter for di & tri peptides however, the notion that you need di & tri peptides for uptake of free form is nonsense

Agreed.

Free-form amino's are indeed bioavailable.... however, glutamine (our favorite), is one that definitely needs some assistance. Do you agree Layne?

For example, free-form glutamine is unstable at physiological pH in liquid media. It (non-enzymatically) breaks down to ammonium and pyroglutamate, and the deamination rate is rapidly upregulated in the presence of phosphate or bicarbonate. However, glutamine's instability is not an issue, when delivered in the form of a protein hydrolysate or dipeptide.

[str8flexed]

it is more stable as a dipeptide however; it's still metabolized rapidly by the enterocyte & liver which remains an issue

[eryanb]

So I'm at work on SciFinder search engine and I determined that there IS indeed an interplay between peptide absorption and free form amino acid absorption.

So as I said earlier I agree both Colgan and I exaggerated calling free amino acids crap/useless since they are absorbed albeit much less efficiently than peptides. However, taking your free form AA's with peptides or fast absorbing protein can substantially increase the absorption of free form AA's taken concurrently.

So my final conclusion is that from the perspective of optimal anabolism AND optimal absorption free form BCAA should always be taken with some whey or best yet hydrosylates.

Bibliographic Information

PEPT1-mediated uptake of dipeptides enhances the intestinal absorption of amino acids via transport system b0,+. Wenzel, Uwe; Meissner, Barbara; Doring, Frank; Daniel, Hannelore. Institute of Nutritional Sciences, Molecular Nutrition Unit, Technical University of Munich, Freising-Weihenstephan, Germany. Journal of Cellular Physiology (2001), 186(2), 251-259. Publisher: Wiley-Liss, Inc., CODEN: JCLLAX ISSN: 0021-9541. Journal written in English. CAN 134:176091 AN 2001:40673 CAPLUS

Abstract

Free amino acids and short chain peptides are the main digestion products of dietary proteins in the small intestine. Whether there is a direct interference in transport of both groups of degrdn. products is not known. We used human intestinal Caco-2 cells to investigate whether the absorption of dipeptides by the peptide transporter PEPT1 alters the apical uptake of free cationic and neutral amino acids. Influx of L-[3H]Arg into Caco-2 cells was Na+-independent and mediated mainly by the b0,+ system recognizing both cationic and neutral amino acids. Preincubation of cells with 10 mM of selected neutral, mono- or dicationic dipeptides increased the influx of L-Arg up to fourfold. Preloading with equiv. concns. of the corresponding free amino acids also increased L-Arg influx but dipeptides always proved to be more efficient. The obsd. trans-stimulation was found to be specific for cationic amino acids since transport of L-[3H]Ala remained unaffected. We here demonstrate for the first time a direct interplay in amino acid and peptide transport in intestinal cells that may selectively alter the kinetics of amino acid absorption.

[Blackjackcat]

Layne, your thoughts on this?

[str8flexed]

well first off it may vary depending on which individual amino acid you are looking at; additionally, this is done in isolated cells so I have difficulty calling it definitive.

Also, the way bodybuilders eat every 3 hours or so you will always be absorptive so there will always be DI & tri peptides present from the food you've been eating

[eryanb]

Layne is right, in vivo results can be substantially different from in vitro so you have to take the information for what it is.

The paper simply tells us this for sure: Peptides can upregulate free AA transport processes on/in certain intestinal cells. Period. So there is a possibility that this research is artifact and in vivo the cells are not so saturated with the "signal" (peptides) or a number of other possibilities.

Theoretically if the upregulation does occur in vivo taking hydrosylates/whey with your free AA's would give better absorption than without even if you do eat every three hours because it's unlikely you would saturate the receptors with natural eating habits.

However, as Layne implies, this is just conjecture unless I can find a better reference.