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1、Eur.J.Biochem.212,185-191(1993)0FEBS1993Conformationofdeltorphin-I1inmembraneenvironmentstudiedbytwo-dimensionalNMRspectroscopyandmoleculardynamicscalculationsYasunoriOHNO',MotozumiSEGAWA',HirofumiOHISHI',MitsunobuDOI',KunihiroKITAMURA',ToshimasaISHIDA',MasatoshiINOU
2、E'andTakashiIWASHITA'DepartmentofPhysicalChemistry,OsakaUniversityofPharmaceuticalSciences,Osaka,JapanSuntoryInstituteforBioorganicResearch,Osaka,Japan(ReceivedOctober22,1992)-EJB921488Two-dimensionalhomonuclearHartmann-HahnspectroscopyandNOESY(nuclearOverhausereffec
3、tandexchangespectroscopy)'H-NMRtechniqueshavebeenusedtoobtaincompleteprotonresonanceassignmentsandtoperformaconformationalinvestigationofdeltorphin-I1(Tyr-D-Ala-Phe-Glu-Val-Val-Gly-NH,),anaturallyoccurring&selectiveopioidpeptide,inthemembrane-mi-meticmicellesofperdeu
4、terateddodecylphosphocholine.Thiswasdoneinordertoexamineconfor-mationalcharacteristicsthatwouldbecloselyrelatedtotheselectivitytowardsthe8-opioidreceptor.Withtheuseoftheproton-protondistancesderivedfromNOESYmeasurements,50possiblethree-dimensionalstructuresweregenera
5、tedbymeansofdistance-geometrycalculations,and25ofthemweresubjectedtothemolecular-dynamicssimulationsof10ps,whichwereenergeticallycon-strainedfortheNOEinterprotondistances.Mostofthepossibleconformerssimulatedshowedacommonfeaturesuchthattheconformationofdeltorphin-I1is
6、characterizedbytheS-shapedback-bonestructureinwhichtheturnconformationoftheVal-Val-Gly-NH,sequenceislocatedunderthehelicallyfoldedconformationoftheN-terminalTyr-D-Ala-Phe-Glusequence.Thepossiblerelation-shipbetweenthisconformationalcharacteristicandthe6-opioid-recept
7、orselectivityhasbeendis-cussed.Sincethediscoveryoftwoendogeneousopioidpentapep-extendedone[7,81hasbeensuggested.Similarly,thesub-tides,i.e.,[Ldlenkephalinand[Met5]enkephalin[l],thestratespecificityofthe6-opioidreceptorhasbeendiscussedmolecularconformationsoftheir,and
8、related,opioidpep-intermsofwhetheritcorrespondstothefolded[9-111ortideshavebeenextensivelystudiedbyvariousphysico-extended[12]confo
