Publications de Inmaculada Rentero Rebollo

De novo identification of lipid II binding lipopeptides with antibacterial activity against vancomycin-resistant bacteria

Creative strategies for identifying new antibiotics are essential to addressing the looming threat of a post-antibiotic era. We here report the use of a targeted peptide phage display screen as a means of generating novel antimicrobial lipopeptides. Specif ...

Royal Soc Chemistry2017

Development of potent and selective S. aureus sortase A inhibitors Based on Peptide Macrocycles

Christian Heinis, Inmaculada Rentero Rebollo, Davide Bertoldo

Sortases are transpeptidase enzymes that anchor surface proteins, including virulence factors, to the cell wall of Gram-positive bacteria, and they are potential targets for the development of anti-infective agents. While several large compound libraries w ...

2016

Identification of target-binding peptide motifs by high-throughput sequencing of phage-selected peptides

Christian Heinis, Inmaculada Rentero Rebollo, Vanessa Baeriswyl, Michal Sabisz

High-throughput sequencing was previously applied to phage-selected peptides in order to gain insight into the abundance and diversity of isolated peptides. Herein we developed a procedure to efficiently compare the sequences of large numbers of phage-sele ...

Oxford Univ Press2014

Improving Bicyclic Peptide Phage Display and Development of Sortase A Inhibitors

Inmaculada Rentero Rebollo

Bicyclic peptide ligands are promising molecules for the development of new therapeutics. They combine advantages from large protein therapeutics and small molecule drugs. Large combinatorial libraries of bicyclic peptides can be generated and screened by ...

EPFL2014

Phage Selection of Photoswitchable Peptide Ligands

Christian Heinis, Inmaculada Rentero Rebollo, Shiyu Chen, Silvia Bellotto, Hermann A. Wegner

Photoswitchable ligands are powerful tools to control biological processes at high spatial and temporal resolution. Unfortunately, such ligands exist only for a limited number of proteins and their development by rational design is not trivial. We have dev ...

2014

Phage selection of bicyclic peptides

Christian Heinis, Inmaculada Rentero Rebollo

Bicyclic peptides are small, constrained peptides that can bind with high affinity and selectivity to protein targets. Their small size provides a number of advantages over larger protein-based ligands, including access to chemical synthesis, better tissue ...

Academic Press Inc Elsevier Science2013

Phage display libraries of differently sized bicyclic peptides

Christian Heinis, Inmaculada Rentero Rebollo, Alessandro Angelini

Phage selections with combinatorial libraries of uniformly sized bicyclic peptides have recently yielded potent and selective binders of several protein targets. In this work we varied in a combinatorial fashion the ring sizes of bicyclic peptides in phage ...

Royal Soc Chemistry2013

Bicyclic peptide ligands pulled out of cysteine-rich peptide libraries

Christian Heinis, Petr Leiman, Inmaculada Rentero Rebollo, Shiyu Chen, Jeremy Touati, Julia Morales Sanfrutos

Bicyclic peptide ligands were found to have good binding affinity and target specificity. However, the method applied to generate bicyclic ligands based on phage-peptide alkylation is technically complex and limits its application to specialized laboratori ...

2013

Boosting the Sensitivity of Ligand-Protein Screening by NMR of Long-Lived States

Geoffrey Bodenhausen, Christian Heinis, Aurélien Bornet, Inmaculada Rentero Rebollo, Alessandro Angelini, Simone Ulzega, Nicola Salvi, Roberto Buratto

A new NMR method for the study of ligand protein interactions exploits the unusual lifetimes of long-lived states (LLSs). The new method provides better contrast between bound and free ligands and requires a protein-ligand ratio ca. 25 times lower than for ...

2012