Dinavil Studies, much more just search on Pubmed.gov
Lignans from the roots of Urtica dioica and their metabolites bind to human sex hormone binding globulin (SHBG).
(Lignans from the roots of Urtica dioica and their ...[Planta Med. 1997] - PubMed Result
Sch??????¶ttner M, Gansser D, Spiteller G.
Lehrstuhl Organische Chemie I, Universit??????¤t Bayreuth, Germany.
Polar extracts of the stinging nettle (Urtica dioica L.) roots contain the ligans (+)-neoolivil, (-)-secoisolariciresinol, dehydrodiconiferyl alcohol, isolariciresinol, pinoresinol, and
3,4-divanillyltetrahydrofuran. These compounds were either isolated from Urtica roots, or obtained semisynthetically. Their affinity to human sex hormone binding globulin (SHBG) was tested in an in vitro assay. In addition, the main intestinal transformation products of plant lignans in humans, enterodiol and enterolactone, together with enterofuran were checked for their activity.
All lignans except (-)-pinoresinol developed a binding affinity to SHBG in the in vitro assay. The affinity of (-)-3,4-divanillyltetrahydrofuran was outstandingly high. These findings are discussed with respect to potential beneficial effects of plant lignans on benign prostatic hyperplasia (BPH).
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The Dinavil causes binding to the SHBG so you can "free up" total test. "Free test" is the bioavailable test that is usable.
Lignans interfering with 5 alpha-dihydrotestosterone binding to human sex hormone-binding globulin.
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Lignans interfering with 5 alpha-dihydrotestostero...[J Nat Prod. 1998] - PubMed Result)
Sch??????¶ttner M, Spiteller G, Gansser D.
Lehrstuhl f??????¼r organische Chemie, Universit??????¤t Bayreuth, Germany.
The natural lignans (-)-3,4-divanillyltetrahydrofuran (1), (-)-matairesinol (2), (-)-secoisolariciresinol (3), (+/-)-enterolactone (4), (+/-)-enterodiol (5), and nordihydroguaiaretic acid (NDGA) (6)
reduce the binding of 3H-labeled 5 alpha-dihydrotestosterone (DHT) to human sex hormone-binding globulin (SHBG). (-)-3,4-Divanillyltetrahydrofuran (1) has the highest binding affinity (Ka = 3.2 +/- 1.7 x 10(6)M-1) of all lignans investigated so far; the reversibility of its binding and a double reciprocal plot suggest a competitive inhibition of the SHBG-DHT interaction. Increasing hydrophobity in the aliphatic part of the lignans (butane-1,4-diol-butanolide-tetrahydrofuran structures) leads to higher binding affinity. In the aromatic part, a 3-methoxy-4-hydroxy substitution pattern is most effective for binding to SHBG.
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This study shows that when Dinavil (3,4-divanillytetrahydrofuran) is present it reduceds the binding of test to SHBG which causes an increase in bioavailable test (good for hypertrophy, strength, etc.)