Weusecookiestoenhanceyourexperience.Bycontinuingtobrowsethissiteyouagreetoouruseofcookies.Moreinfo.AcceptCookieSettingsLugdunininthehumannosehasstrongantimicrobialpropertiesagainstS.aureusDownloadPDFCopyReviewedbyJamesIves,M.Psych.(Editor)May292019Antibiotic-resistantbacteriaareanincreasinghealththreat,makingnewantibioticsessential.Germanresearchershaverecentlyhadabreakthrough:theydiscoveredlugdunininthehumannose--anewkindofcyclicpeptidethatcomesfromthebacteriumStaphylococcuslugdunensisandhasstrongantimicrobialpropertiesagainstStaphylococcusaureus,amongothers.Theresearchershavebeenabletoclarifythemodeofactionbysynthesizingvariants.AstheyexplaininthejournalAngewandteChemie,protontransportacrossbacterialmembranesisinvolved.Aninterestingpartoflugdunin'sstructureisitsthiazolidinegroup(aringmadefromonenitrogen,onesulfur,andthreecarbonatoms),whichformsapartofitspeptidering.Thisfive-memberedringresemblesaclaspthat"adorns"thepeptidering.Forthisreason,theresearchersnamedtheirnewclassofmaterials"fibupeptides",fromtheLatinfibula,meaningclasp.Havingpreviouslysucceededinsynthesizinglugdunin,theteamfromtheUniversityofTübingenandtheUniversityofGöttingen(Germany)optimizedthesyntheticpathwaytomakemanydifferentderivativesofthisnaturalsubstance.Thisallowedforacomprehensivestudyofthemechanismbywhichlugduninworks.Theresearchersmadeaseriesofderivativesinwhichtheyreplacedeachoftheaminoacidsinthepeptideringwithalanine--oneinwhichtheyleftoffthe"ornamentclasp",andafibupeptidewithastructurethatisthemirrorimageoflugdunin.Theythenusedthesederivativestocarryoutactivitytests.Theteam,consistingofchemists,biochemists,andmicrobiologists,discoveredthatthecyclicstructureofthepeptide,thethiazolidine"clasp",andtwoaminoacids(tryptophanandleucin),arecriticaltotheantibioticactivityofthecompound.Inaddition,thepeptideringmustalwaysbemadeofalternatingD-andL-aminoacids.However,therewasnodifferenceintheactivityoftheoriginalmoleculeoritsmirrorimage."Thisindicatesalackofstereospecificreceptor-ligandinteraction,"s