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Design and Synthesis of Oligopeptidic Parvulin Inhibitors

Title: Design and Synthesis of Oligopeptidic Parvulin Inhibitors
Authors: Relitti N.; Prasanth Saraswati A.; Carullo G.; Papa A.; Monti A.; Benedetti R.; Passaro E.; Brogi S.; Calderone V.; Butini S.; Gemma S.; Altucci L.; Campiani G.; Doti N.
Contributors: Relitti, N.; Prasanth Saraswati, A.; Carullo, G.; Papa, A.; Monti, A.; Benedetti, R.; Passaro, E.; Brogi, S.; Calderone, V.; Butini, S.; Gemma, S.; Altucci, L.; Campiani, G.; Doti, N.
Publication Year: 2022
Collection: Università degli Studi di Siena: USiena air
Subject Terms: biological activity; molecular modelling; peptide synthesi; Pin1/4; PPIase
Description: Pin1 catalyzes the cis-trans isomerization of pThr-Pro or pSer-Pro amide bonds of various proteins involved in several physio/pathological processes. In this framework, recent research activity is directed toward the identification of new selective Pin1 inhibitors. Here, we developed a set of peptide-based Pin1 inhibitors. Direct-binding experiments allowed the identification of the peptide-based inhibitor 5 k (methylacetyl-l-alanyl-l-histidyl-l-prolyl-l-phenylalaninate) as a potent ligand of Pin1. Notably, 5 k binds Pin1 with higher affinity than Pin4. The comparative analysis of molecular models of Pin1 and Pin4 with the selected compound gave a rational explanation of the biochemical activity and pinpointed the chemical elements that, if opportunely modified, may further improve inhibitory potency, pharmacological properties, and selectivity of future peptide-based parvulin inhibitors. Since 5 k showed limited cell penetration and no antiproliferative activity, it was conjugated to a polyarginine stretch (R8), known to promote cell penetration of peptides, to obtain the R8–5 k derivative, which displayed antiproliferative effects on cancer cell lines over non-tumor cells. The effect of R8 on cell proliferation was also investigated. This work warrants caution about applying the R8 strategy in the development of cell-penetrating antiproliferative peptides, as it is not inert. © 2022 The Authors.
Document Type: article in journal/newspaper
File Description: ELETTRONICO
Language: English
Relation: info:eu-repo/semantics/altIdentifier/pmid/35357776; info:eu-repo/semantics/altIdentifier/wos/WOS:000788050300001; volume:17; issue:11; journal:CHEMMEDCHEM; https://hdl.handle.net/11365/1208349; https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9321596/
DOI: 10.1002/cmdc.202200050
Availability: https://hdl.handle.net/11365/1208349; https://doi.org/10.1002/cmdc.202200050; https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cmdc.202200050; https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9321596/
Rights: info:eu-repo/semantics/openAccess
Accession Number: edsbas.192BB04
Database: BASE