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X‐Ray Crystal Structure of a Second‐Generation Peptide Dendrimer in Complex with Pseudomonas aeruginosa Lectin LecB
Author(s) -
Baeriswyl Stéphane,
Javor Sacha,
Stocker Achim,
Darbre Tamis,
Reymond JeanLouis
Publication year - 2019
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.201900178
Subject(s) - chemistry , dendrimer , protein data bank (rcsb pdb) , crystallography , hydrogen bond , dimer , stereochemistry , intramolecular force , peptide , crystal structure , monomer , molecule , biochemistry , organic chemistry , polymer
Dendrimers are regularly branched molecular trees which are notoriously difficult to crystallize. Herein we report the crystal structure of a C ‐fucosylated second generation peptide dendrimer as complex with lectin LecB in which the only dendrimer‐lectin contact is the LecB bound glycoside (PDB 6S5S). In contrast to a previously reported crystal structure of a first‐generation peptide dendrimer as LecB complex in which the dendrimer formed trimers connected by intermolecular β ‐sheets (PDB 5D2A), the present structure features a globular monomeric state held together by intramolecular backbone hydrogen bonds and assembled into a non‐covalent dimer stabilized by hydrophobic contacts between leucine side‐chains and proline‐phenylalanine CH‐ π stacking interactions. Molecular dynamics and circular dichroism studies suggest that this crystal structure resembles the structure of the peptide dendrimer in solution. Structures of a partially resolved dendrimer (PDB 6S5R) and of C ‐fucosylated disulfide bridged peptide dimers connecting different LecB tetramers are also reported (PDB 6S7G, PDB 6S5P).