Conformation of Cyclic Heptapeptides : Conformational Analysis of Segetalins D and E by Distance Geometry Calculations

概要

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Three-dimensional structures in dimethyl sulfoxide-d_6 of two cyclic heptapeptides, segetalin D(1) : cyclo (-Gly-Leu-Ser-Phe-Ala-Phe-Pro-) and segetalin E (2) : cyclo (-Gly-Try-Val-Pro-Leu-Trp-Pro-), which have been isolated from the seeds of Vaccaria segetalis, were elucidated by computational and NMR methods. Distance geometry calculations using nuclear Overhauser effect (NOE) constraints resulted in uniquely determined backbone conformations of segetalins D and E : each had two β-turns, a βII turn at Pro^7-Gly^1 and a βI turn at phe^4-Ala^5 for segetalin D, and a βII turn at Pro^7-Gly^1 and a βVI turn at Val^3-Pro^4 for segetalin E, respectively. In addition, each had three intramolecular hydrogen bonds, which constructed a classical β-bulge conformation, as suggested by calculations and NMR studies.
社団法人日本薬学会の論文
1997-05-15