id,collection,dc.contributor.author,dc.date.accessioned,dc.date.available,dc.date.issued,dc.description.abstract[en],dc.format.extent,dc.identifier.uri,dc.language,dc.rights.uri,dc.subject.ddc,dc.subject[en],dc.title,dc.type,dcterms.accessRights.openaire,dcterms.bibliographicCitation.articlenumber,dcterms.bibliographicCitation.doi,dcterms.bibliographicCitation.journaltitle,dcterms.bibliographicCitation.number,dcterms.bibliographicCitation.url,dcterms.bibliographicCitation.volume,dcterms.isPartOf.eissn,refubium.affiliation,refubium.affiliation.other,refubium.resourceType.isindependentpub,refubium.resourceType.provider "75a1ecf8-0272-4a18-8dbe-751e7c83ca25","fub188/16","Engelhardt, Pascal M.||Florez-Rueda, Sebastián||Drexelius, Marco||Neudörfl, Jörg-Martin||Lauster, Daniel||Hackenberger, Christian P. R.||Kühne, Ronald||Neundorf, Ines||Schmalz, Hans-Günther","2022-10-06T09:10:37Z","2022-10-06T09:10:37Z","2022","During viral cell entry, the spike protein of SARS-CoV-2 binds to the α1-helix motif of human angiotensin-converting enzyme 2 (ACE2). Thus, alpha-helical peptides mimicking this motif may serve as inhibitors of viral cell entry. For this purpose, we employed the rigidified diproline-derived module ProM-5 to induce α-helicity in short peptide sequences inspired by the ACE2 α1-helix. Starting with Ac-QAKTFLDKFNHEAEDLFYQ-NH2 as a relevant section of α1, a series of peptides, N-capped with either Ac-βHAsp-[ProM-5] or Ac-βHAsp-PP, were prepared and their α-helicities were investigated. While ProM-5 clearly showed a pronounced effect, an even increased degree of helicity (up to 63 %) was observed in sequences in which non-binding amino acids were replaced by alanine. The binding affinities of the peptides towards the spike protein, as determined by means of microscale thermophoresis (MST), revealed only a subtle influence of the α-helical content and, noteworthy, led to the identification of an Ac-βHAsp-PP-capped peptide displaying a very strong binding affinity (KD=62 nM).","6 Seiten","https://refubium.fu-berlin.de/handle/fub188/36098||http://dx.doi.org/10.17169/refubium-35814","eng","https://creativecommons.org/licenses/by/4.0/","500 Naturwissenschaften und Mathematik::540 Chemie::540 Chemie und zugeordnete Wissenschaften","CD spectroscopy||peptides||protein-protein interactions||SARS-CoV-2||secondary structures","Synthetic α-Helical Peptides as Potential Inhibitors of the ACE2 SARS-CoV-2 Interaction","Wissenschaftlicher Artikel","open access","e202200372","10.1002/cbic.202200372","ChemBioChem","17","https://doi.org/10.1002/cbic.202200372","23","1439-7633","Biologie, Chemie, Pharmazie","Institut für Chemie und Biochemie:::bdaf1c47-f341-464f-b012-0d24067d34b8:::600","no","WoS-Alert"