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a lignan found in nettle for inhibition of shbg
Z Naturforsch [C]. 1997 Nov-Dec;52(11-12):834-43. Related Articles, Links
Interaction of lignans with human sex hormone binding globulin (SHBG).
Schottner M, Gansser D, Spiteller G.
Lehrstuhl Organische Chemie I, Universitat Bayreuth, Germany.
Lignans bind to sex hormone-binding globulin (SHBG). The lignan with the highest binding affinity is (+/-)-3,4-divanillyltetrahydrofuran. In a double Stobbe condensation--without use of protecting groups--a wide variety of lignans with different substitution pattern in the aromatic and aliphatic part of the molecule was synthesized. These lignans were tested in a SHBG-binding assay which allowed to deduce the following relationship between structure and activity: 1) (+/-)-diastereoisomers are more active than meso compounds 2.) the 4-hydroxy-3-methoxy (guajacyl) substitution pattern in the aromatic part is most effective 3.) the activity increases with the decline in polarity of the aliphatic part of the molecule.
PMID: 9463941 [PubMed - indexed for MEDLINE]
J Nat Prod. 1998 Jan;61(1):119-21. Related Articles, Links
Lignans interfering with 5 alpha-dihydrotestosterone binding to human sex hormone-binding globulin.
Schottner M, Spiteller G, Gansser D.
Lehrstuhl fur organische Chemie, Universitat 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.
PMID: 9461660 [PubMed - indexed for MEDLINE]
Planta Med. 1997 Dec;63(6):529-32. Related Articles, Links
Lignans from the roots of Urtica dioica and their metabolites bind to human sex hormone binding globulin (SHBG).
Schottner M, Gansser D, Spiteller G.
Lehrstuhl Organische Chemie I, Universitat 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).
PMID: 9434605 [PubMed - indexed for MEDLINE]
Z Naturforsch [C]. 1997 Nov-Dec;52(11-12):834-43. Related Articles, Links
Interaction of lignans with human sex hormone binding globulin (SHBG).
Schottner M, Gansser D, Spiteller G.
Lehrstuhl Organische Chemie I, Universitat Bayreuth, Germany.
Lignans bind to sex hormone-binding globulin (SHBG). The lignan with the highest binding affinity is (+/-)-3,4-divanillyltetrahydrofuran. In a double Stobbe condensation--without use of protecting groups--a wide variety of lignans with different substitution pattern in the aromatic and aliphatic part of the molecule was synthesized. These lignans were tested in a SHBG-binding assay which allowed to deduce the following relationship between structure and activity: 1) (+/-)-diastereoisomers are more active than meso compounds 2.) the 4-hydroxy-3-methoxy (guajacyl) substitution pattern in the aromatic part is most effective 3.) the activity increases with the decline in polarity of the aliphatic part of the molecule.
PMID: 9463941 [PubMed - indexed for MEDLINE]
J Nat Prod. 1998 Jan;61(1):119-21. Related Articles, Links
Lignans interfering with 5 alpha-dihydrotestosterone binding to human sex hormone-binding globulin.
Schottner M, Spiteller G, Gansser D.
Lehrstuhl fur organische Chemie, Universitat 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.
PMID: 9461660 [PubMed - indexed for MEDLINE]
Planta Med. 1997 Dec;63(6):529-32. Related Articles, Links
Lignans from the roots of Urtica dioica and their metabolites bind to human sex hormone binding globulin (SHBG).
Schottner M, Gansser D, Spiteller G.
Lehrstuhl Organische Chemie I, Universitat 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).
PMID: 9434605 [PubMed - indexed for MEDLINE]
