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X‐Ray Crystal Structure of a Second‐Generation Peptide Dendrimer in Complex with Pseudomonas aeruginosa Lectin LecB

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Author Baeriswyl Stéphane, Javor Sacha, Stocker Achim, Darbre Tamis, Reymond Jean‐Louis,
Project Chemical Space Design of Small Molecules and Peptides
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Original article (peer-reviewed)

Journal Helvetica Chimica Acta
Volume (Issue) 102(9)
Page(s) e1900178
Title of proceedings Helvetica Chimica Acta
DOI 10.1002/hlca.v102.9

Abstract

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).
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