7l96 | pdb_00007l96

Connecting hydrophobic surfaces in cyclic peptides increases membrane permeability

spinqualitylabelsall models 7l96 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7l96 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: DLE, DPR, N9K Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 Calpha-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. Connecting Hydrophobic Surfaces in Cyclic Peptides Increases Membrane Permeability.,Hoang HN, Hill TA, Fairlie DP Angew Chem Int Ed Engl. 2021 Apr 6;60(15):8385-8390. doi: 10.1002/anie.202012643., Epub 2021 Mar 4. PMID:33185961 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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