7L98
Connecting hydrophobic surfaces in cyclic peptides increases membrane permeability
Summary for 7L98
| Entry DOI | 10.2210/pdb7l98/pdb |
| NMR Information | BMRB: 30839 |
| Descriptor | Cyclic peptide ALA-MEA-PRO-ILE-PRO-ITZ (1 entity in total) |
| Functional Keywords | cyclic peptides, peptide binding protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 753.95 |
| Authors | Hoang, H.N. (deposition date: 2021-01-03, release date: 2021-09-08, Last modification date: 2024-11-13) |
| Primary citation | Hoang, H.N.,Hill, T.A.,Fairlie, D.P. Connecting Hydrophobic Surfaces in Cyclic Peptides Increases Membrane Permeability. Angew.Chem.Int.Ed.Engl., 60:8385-8390, 2021 Cited by PubMed Abstract: N- or C-methylation in natural and synthetic cyclic peptides can increase membrane permeability, but it remains unclear why this happens in some cases but not others. Here we compare three-dimensional structures for cyclic peptides from six families, including isomers differing only in the location of an N- or Cα-methyl substituent. We show that a single methyl group only increases membrane permeability when it connects or expands hydrophobic surface patches. Positional isomers, with the same molecular weight, hydrogen bond donors/acceptors, rotatable bonds, calculated LogP, topological polar surface area, and total hydrophobic surface area, can have different membrane permeabilities that correlate with the size of the largest continuous hydrophobic surface patch. These results illuminate a key local molecular determinant of membrane permeability. PubMed: 33185961DOI: 10.1002/anie.202012643 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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