Pepscan Approach for the Identification of Protein–Protein Interfaces: Lessons from Experiment
PEPscan is an old approach that has recently gained renewed interest for the identification of interfering peptides (IPs), i.e., peptides able to interfere with protein–protein interactions (PPIs). Its principle is to slice a protein sequence as a series of short overlapping peptides that are synthe...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-05-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/11/6/772 |
| _version_ | 1797533181727997952 |
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| author | Angelita Rebollo Eric Savier Pierre Tuffery |
| author_facet | Angelita Rebollo Eric Savier Pierre Tuffery |
| author_sort | Angelita Rebollo |
| collection | DOAJ |
| description | PEPscan is an old approach that has recently gained renewed interest for the identification of interfering peptides (IPs), i.e., peptides able to interfere with protein–protein interactions (PPIs). Its principle is to slice a protein sequence as a series of short overlapping peptides that are synthesized on a peptide array and tested for their ability to bind a partner, with positive spots corresponding to candidate IPs. PEPscan has been applied with a rather large success in various contexts, but the structural determinants underlying this success remain obscure. Here, we analyze the results of 14 PEPscan experiments, and confront the in vitro results with the available structural information. PEPscan identifies candidate IPs in limited numbers that in all cases correspond to solvent-accessible regions of the structures, their location at the protein–protein interface remaining to be further demonstrated. A strong point of PEPscan seems to be its ability to identify specific IPs. IPs identified from the same protein differ depending on the target PPI, and correspond to patches not frequently involved in the interactions seen in the 3D structures available. Overall, PEPscan seems to provide a cheap and rapid manner to identify candidate IPs, that also comes with room for improvement. |
| first_indexed | 2024-03-10T11:10:53Z |
| format | Article |
| id | doaj.art-034050a8b9af4a798e3596b8afae9926 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T11:10:53Z |
| publishDate | 2021-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-034050a8b9af4a798e3596b8afae99262023-11-21T20:45:24ZengMDPI AGBiomolecules2218-273X2021-05-0111677210.3390/biom11060772Pepscan Approach for the Identification of Protein–Protein Interfaces: Lessons from ExperimentAngelita Rebollo0Eric Savier1Pierre Tuffery 2UTCBS, Inserm 1265, Faculté de Pharmacie, Université de Paris, 75013 Paris, FranceDepartment of Hepatobiliary and Liver Transplantation Surgery, Pitié–Salpêtrière Hospital, AP-HP, Sorbonne Université, 75013 Paris, FranceBFA, CNRS, UMR 8251, Inserm U1133, Université de Paris, F-75013 Paris, FrancePEPscan is an old approach that has recently gained renewed interest for the identification of interfering peptides (IPs), i.e., peptides able to interfere with protein–protein interactions (PPIs). Its principle is to slice a protein sequence as a series of short overlapping peptides that are synthesized on a peptide array and tested for their ability to bind a partner, with positive spots corresponding to candidate IPs. PEPscan has been applied with a rather large success in various contexts, but the structural determinants underlying this success remain obscure. Here, we analyze the results of 14 PEPscan experiments, and confront the in vitro results with the available structural information. PEPscan identifies candidate IPs in limited numbers that in all cases correspond to solvent-accessible regions of the structures, their location at the protein–protein interface remaining to be further demonstrated. A strong point of PEPscan seems to be its ability to identify specific IPs. IPs identified from the same protein differ depending on the target PPI, and correspond to patches not frequently involved in the interactions seen in the 3D structures available. Overall, PEPscan seems to provide a cheap and rapid manner to identify candidate IPs, that also comes with room for improvement.https://www.mdpi.com/2218-273X/11/6/772PEP-scanprotein–protein interactioninterfering peptidebinding specificity |
| spellingShingle | Angelita Rebollo Eric Savier Pierre Tuffery Pepscan Approach for the Identification of Protein–Protein Interfaces: Lessons from Experiment Biomolecules PEP-scan protein–protein interaction interfering peptide binding specificity |
| title | Pepscan Approach for the Identification of Protein–Protein Interfaces: Lessons from Experiment |
| title_full | Pepscan Approach for the Identification of Protein–Protein Interfaces: Lessons from Experiment |
| title_fullStr | Pepscan Approach for the Identification of Protein–Protein Interfaces: Lessons from Experiment |
| title_full_unstemmed | Pepscan Approach for the Identification of Protein–Protein Interfaces: Lessons from Experiment |
| title_short | Pepscan Approach for the Identification of Protein–Protein Interfaces: Lessons from Experiment |
| title_sort | pepscan approach for the identification of protein protein interfaces lessons from experiment |
| topic | PEP-scan protein–protein interaction interfering peptide binding specificity |
| url | https://www.mdpi.com/2218-273X/11/6/772 |
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