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On the side chain conformation of 1α,25-dihydroxyvitamin D3 responsible for binding to the receptor

✍ Scribed by Keiko Yamamoto; Masateru Ohta; Hector F. DeLuca; Sachiko Yamada


Publisher
Elsevier Science
Year
1995
Tongue
English
Weight
313 KB
Volume
5
Category
Article
ISSN
0960-894X

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✦ Synopsis


AbsWaet: Side chain mobility of 1,25(OH)2D3 (1) and its 20-epimer (2) was analyzed and shown in a threedimensional dot map that indicates the two distinct spatial regions accessible by the terminal 25-hydroxyl group for each vitamin. The biological activities of two analogs (3 and 4) of 1, which possess restricted side chain flexibility, were tested and the results suggest the spatial region of I responsible for binding to VDR and DBP.


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Five analogs of 1 alpha,25-dihydroxyvitamin D3 [1,25(OH)2D3] [1], 26,27-dimethyl-1 alpha,25-dihydroxyvitamin D3 [1,25(OH)2(Me)2D3] [2], 26,27-dimethyl-1 alpha,25-dihydroxyvitamin D3 [1,25(OH)2(Et)2D3] [3], 26,27-dipropyl-1 alpha,25-dihydroxyvitamin D3 [1,25(OH)2(Pr)2D3] [4], 26,27-dimethyl-24,24-dif