I've been hoping to understand why b5 triggers hairloss in some. It's clear b5 increase Coenzyme A. You can find lots of literature to support this. I recently came across this artcile that shows Coenzyme A plays a big role in catalyzing biotin. Of course just adding more Biotin to your body probably won't do any good since the synthesis of biotin is being altered. I think this is as good an explanation as I have seen.

Also... while b5 seems to exit the body well CoA can be stored in the liver... No one talks about this but it's worth noting. This is likely why after stopping b5 you still have a good effect for some period of time and also why hairloss continues for some till all the CoA is worked out and the biotin synthesis is corrected.

Not that I recommend experimentation but if anyone has good literature on how to increase biotin synthesis that would likely counter CoA knocking it out.

Article on interest below:

Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing

Francis K Athappilly, 1 and Wayne A Hendrickson2

1 Francis K Athappilly (corresponding author) and Wayne A Hendrickson, Department of Biochemistry and Molecular Biophysics, College of Physicians and Surgeons of Columbia University, New York, NY 10032, USA

2 Wayne A Hendrickson, Howard Hughes Medical Institute, College of Physicians and Surgeons of Columbia University, New York, NY 10032, USA

Received 4 September 1995; Revised 26 October 1995; accepted 27 October 1995. Available online 22 July 2004.

Background: Acetyl-coenzyme A carboxylase catalyzes the first committed step of fatty acid biosynthesis. Universally, this reaction involves three functional components all related to a carboxybiotinyl intermediate. A biotinyl domain shuttles its covalently attached biotin prosthetic group between the active sites of a biotin carboxylase and a carboxyl transferase. In Escherichia coli, the three components reside in separate subunits; a biotinyl domain is the functional portion of one of these, biotin carboxyl carrier protein (BCCP).

Exceprt from text:

Biotinylation of apocarboxylases to form holoenzymes is important from a clinical perspective. Defects in either holocarboxylase synthetase or biotinidase resulting in impaired biotinylation are responsible for inherited biotin-responsive multiple carboxylase deficiency in humans [18, 19 and 20]. The symptoms of this disorder include skin rash, loss of hair, difficulty in feeding and breathing, developmental delay, seizures and coma. The biotinylation reaction is evolutionarily conserved such that synthetases function with various apocarboxylases across species boundaries. Thus, bacterial holocarboxylase synthetase can biotinylate rat apocarboxylases [21 and 22]. Only the biotinyl domain of apocarboxylase is necessary for biotinylation [23 and 24], although synthetases can biotinylate intact apocarboxylases [25, 26 and 27]. Thus, we expect that an analysis of biotinylation of BCCPsc by the E. coli holocarboxylase synthetase (BirA) [25 and 28], the structure of which is known [29], will enhance our understanding of biotinylation in man.