Does the cis/trans configuration of peptide bonds in bioactive tripeptides play a role in ACE-1 enzyme inhibition?

References

• JäkäläPVapaataloHAntihypertensive peptides from milk proteinsPharmaceuticals201031251272
   Google Scholar
• TurpeinenAMJärvenpääSKautiainenHKorpelaRVapaataloHAntihypertensive effects of bioactive tripeptides – a random effects meta-analysisAnn Med2013451515623305234
   PubMed Web of Science ®Google Scholar
• LuhtalaSVaajanenAOksalaOValjakkaJVapaataloHActivities of angiotensin-converting enzymes 1 (ACE1) and 2 (ACE2) and inhibition by bioactive peptides in porcine ocular tissuesJ Ocul Pharmacol Ther2009251232819232015
   PubMed Web of Science ®Google Scholar
• SipolaMFinckenbergPSantistebanJKorpelaRVapaataloHNurminenMLLong-term intake of milk peptide attenuates development of hypertension in spontaneously hypertensive ratsJ Physiol Pharmacol2001524 Pt274575411785770
   PubMed Web of Science ®Google Scholar
• JäkäläPHakalaATurpeinenAMKorpelaRVapaataloHCasein-derived bioactive tripeptides Ile-Pro-Pro and Val-Pro-Pro attenuate the development of hypertension and improve endothelial function in salt-loaded Goto-Kakizaki ratsJ Funct Foods200914366374
   Web of Science ®Google Scholar
• NakamuraYYamamotoNSakaiKOkuboAYamazakiSTakanoTPurification and characterization of angiotensin I-converting enzyme inhibitors from sour milkJ Dairy Sci19957847777837790570
   PubMed Web of Science ®Google Scholar
• NakamuraYYamamotoNSakaiKTakanoTAntihypertensive effect of sour milk and peptides isolated from it that are inhibitors of angiotensin I-converting enzymeJ Dairy Sci1995786125312577673515
   PubMed Web of Science ®Google Scholar
• XuJYQinLQWangPYLiWChangCEffects of milk tripeptides on blood pressure: a meta-analysis of randomized controlled trialsNutrition2008241093394018562172
   PubMed Web of Science ®Google Scholar
• CiceroAFGGerocarniBLaghiLBorghiCBlood pressure lowering effects of lactotripeptides assumed as functional food: a meta-analysis of current available clinical trialsJ Hum Hypertens201125742543620811398
   PubMed Web of Science ®Google Scholar
• TurpeinenAMJärvenpääSKautiainenHKorpelaRVapaataloHAntihypertensive effects of bioactive tripeptides – a random effects meta-analysisAnn Med2013451515623305234
   PubMed Web of Science ®Google Scholar
• JäkäläPJauhiainenTKorpelaRVapaataloHMilk protein-derived bioactive tripeptides Ile-Pro-Pro and Val-Pro-Pro protect endothelial function in vitro in hypertensive ratsJ Funct Foods200913266273
   Web of Science ®Google Scholar
• JauhiainenTPilviTChengZJMilk products containing bioactive tripeptides have an antihypertensive effect in double transgenic rats (dTGR) harbouring human renin and human angiotensinogen genesJ Nutr Metab20102010 Article ID287030, 6 pages
   Google Scholar
• SipolaMFinckenbergPKorpelaRVapaataloHNurminenMLEffect on long-term intake of milk products on blood pressure in hypertensive ratsJ Dairy Res200269110311112047101
   PubMed Web of Science ®Google Scholar
• LehtinenRJauhiainenTKankuriEEffects of milk casein-derived tripeptides Ile-Pro-Pro, Val-Pro-Pro, and Leu-Pro-Pro on enzymes processing vasoactive precursors in vitroArzneimittelforschung201060418218520486467
   PubMed Web of Science ®Google Scholar
• JäkäläPPereELehtinenRTurpeinenAKorpelaRVapaataloHCardiovascular activity of milk-casein-derived tripeptides and plant sterols in spontaneously hypertensive ratsJ Phys Pharm20096041120
   Web of Science ®Google Scholar
• JauhiainenTCollinMNarvaMEffect of long-term intake of milk peptides and minerals on blood pressure and arterial function in spontaneously hypertensive ratsMilk Sci Int2005604358363
   Google Scholar
• SiltariAKivimäkiASEhlersPIKorpelaRVapaataloHEffects of milk casein derived tripeptides on endothelial enzymes in vitro; a study with synthetic tripeptidesArzneimittelforschung2012621047748122918858
   PubMed Web of Science ®Google Scholar
• EhlersPINurmiLTurpeinenAMKorpelaRVapaataloHCasein-derived tripeptide Ile-Pro-Pro improves angiotensin-(1-7)-and bradykinin-induced rat mesenteric artery relaxationLife Sci2011885–620621121056585
   PubMed Web of Science ®Google Scholar
• FernandesLFortesZBNigroDTostesRCASantosRASCatelli De CarvalhoMHPotentiation of bradykinin by angiotensin-(1-7) on arterioles of spontaneously hypertensive rats studied in vivoHypertension2001372 Pt 270370911230360
   PubMed Web of Science ®Google Scholar
• UedaSMasumori-MeamotoSWadaAIshiiMBrosnihanIBUmemuraSAngiotensin(1-7) potentiates bradykinin-induced vasodilatation in manJ Hypertens200119112001200911677365
   PubMed Web of Science ®Google Scholar
• EspínJCGarcía-RuizPATudelaJGarcía-CánovasFStudy of stereospecificity in mushroom tyrosinaseBiochem J1998331Pt 25475519531496
   PubMed Web of Science ®Google Scholar
• QuNIgnatenkoNAYamauchiPInhibition of human ornithine decarboxylase activity by enantiomers of difluoromethylornithineBiochem J2003375Pt 246547012859253
   PubMed Web of Science ®Google Scholar
• LondonREMatwiyoffNAStewartJMCannJR13C nuclear magnetic resonance study of the cis-trans isomerism in X-Pro-Pro tripeptidesBiochemistry197817122277228328142
   PubMed Web of Science ®Google Scholar
• BermanHMWestbrookJFengFThe Protein Data BankNucleic Acids Res200028123524210592235
   PubMed Web of Science ®Google Scholar
• MorrisGMHueyRLindstromWAutodock4 and AutoDock-Tools4: automated docking with selective receptor flexiblityJ Comput Chem200930162785279119399780
   PubMed Web of Science ®Google Scholar
• NateshRSchwagerSLSturrockEDAcharyaKRCrystal structure of the human angiotensin-converting enzyme-lisinopril complexNature2003421692255155412540854
   PubMed Web of Science ®Google Scholar
• GuexNPeitschMCSWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelingElectrophoresis19971815271427239504803
   PubMed Web of Science ®Google Scholar
• PhillipsJCBraunRWangWScalable molecular dynamics with NAMDJ Comput Chem200526161781180216222654
   PubMed Web of Science ®Google Scholar
• HornakVAbelROkurAStrockbineBRoitbergASimmerlingCComparision of multiple amber force fields and development of improved protein backbone parametersProteins200665371272516981200
   PubMed Web of Science ®Google Scholar
• WangJWolfRMCaldwellJWKollmanPACaseDADevelopment and testing of a general amber force fieldJ Comput Chem20042591157117415116359
   PubMed Web of Science ®Google Scholar
• PorterCTBartlettGJThorntonJMThe Catalytic Site Atlas: a resource of catalytic sites and residues identified in enzymes using structural dataNucl Acids Res200432Database issueD129D13314681376
   PubMed Web of Science ®Google Scholar
• SiowRCCulture of human endothelial cells from umbilical veinsMethods Mol Biol201280626527422057458
   PubMedGoogle Scholar
• MarinVKaplanskiGGresSFarnarierCBongrandPEndothelial cell culture: protocol to obtain and cultivate human umbilical endothelial cellsJ Immunol Methods20012541–218319011406163
   PubMed Web of Science ®Google Scholar
• SantosRAKriegerEMGreeneLJAn improved fluorometric assay of rat serum and plasma converting enzymeHypertension1985722442522984118
   PubMed Web of Science ®Google Scholar
• RubinBAntonaccioMJGoldbergMEChronic antihypertensive effects of captopril (SQ 14,225), an orally active angiotensin I-converting enzyme inhibitor, in conscious 2-kidney renal hypertensive ratsEur J Pharmacol1978514377388213296
   PubMed Web of Science ®Google Scholar
• VollmerRRBoccagnoJASteinbacherTEHorovitzZPMurthyVSAntihypertensive effects of captopril (SQ 14,225), an orally active inhibitor of angiotensin I-converting enzyme in conscious two kidney perinephritic hypertensive dogsJ Pharmacol Exp Ther198121622252316257882
   PubMed Web of Science ®Google Scholar
• MutterMWöhrTGioriaSKellerMPseudo-prolines: Induction of cis/trans-conformational interconversion by decreased transition state barriersBiopolymers199951212112810397796
   PubMed Web of Science ®Google Scholar
• SchmidFXGrafRWrbaBeintemaJJRole of proline peptide bond isomerization in unfolding and refolding of ribonucleaseProc Natl Acad Sci U S A19868348728763456571
   PubMed Web of Science ®Google Scholar
• EngberinkMFSchoutenEGKokFJvan MierloLABrouwerIAGeleijnseJMLactotripeptides show no effect on human blood pressure. Result on double-blinded randomiced controlled trialHypertension200851239940518086944
   PubMed Web of Science ®Google Scholar
• Van der ZanderKBotsMLBakAAKoningMMde LeeuwPWEnzymatically hydrolyzed lactotripeptides do not lower blood pressure in mildly hypertensive subjectsAmer J Clin Nutr20088861697170219064533
   PubMed Web of Science ®Google Scholar
• WuerznerGPeyrardSBlanchardALalanneFAziziMThe lactotripeptides isoleucine-proline-proline and valine-proline-proline do not inhibit the N-terminal or C-terminal angiotensin converting enzyme active sites in humansJ Hypertens20092771404140919506528
   PubMed Web of Science ®Google Scholar
• CountermannAClemmerDECis-Trans signatures of proline-containing tryptic peptides in the gas phaseAnal Chem20027491946195112033290
   PubMed Web of Science ®Google Scholar
• KorhonenHMilk-derived bioactive peptides: From science to applicationsJ Funct Foods200912177187
   Web of Science ®Google Scholar
• FoltzMvan BurenLKlaffkeWDuchateauGSModeling of the relationship between dipeptide structure and dipeptide stability, permeability, and ACE inhibition activityJ Food Sci2009747H243H25119895477
   PubMed Web of Science ®Google Scholar
• MeyerRFEssenburgADSmithRDKaplanHRAngiotensin converting enzyme inhibitors: modification of a tripeptide analogueJ Med Chem19822589969996288947
   PubMed Web of Science ®Google Scholar
• JäkäläPTurpeinenAMRajakariKKorpelaRVapaataloHBiological effects of casein-derived tripeptides powders are not affected by fermentation processInt Dairy J2010205366370
   Web of Science ®Google Scholar