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Studies of arginine-arene interactions through synthesis and evaluation of a series of galectin-binding aromatic lactose esters

In English

Författare

Summary, in English

Aromatic lactose 2-O-esters were synthesized and used to probe arene-arginine interactions with the galectin family of proteins. They were found to be low mu m inhibitors of galectin-1, -3, and -9N-terminal domain and moderate inhibitors of galectin-7, but not inhibitors of galectin-8N-terminal, which locks an arginine residue close to the critical, esterified lactose 2-O-position. Molecular modeling of galectins in complex with aromatic lactose 2-O-esters, as well as binding studies with a galectin-3 R186S mutant, confirmed that the inhibitory efficiency of the lactose 2-O-esters was due to the formation of strong interactions between the aromatic ester moieties and the arginine guanidinium groups of galectin-1 and -3. An important common feature shared by galectin-1 and -3 was that the arginines formed in-plane ion pairs with two side-chain carboxylates, which resulted in extended planar pi-electron surfaces that did not require solvation by water; these surfaces were ideal for stocking with aromatic moieties of the ligands. The results provide a basis for the design of lectin inhibitors and drugs that exploit interactions with arginine side-chains via aromatic moieties, which are involved in intramolecular protein salt bridges.

Publiceringsår

2007

Språk

Engelska

Sidor

1389-1398

Publikation/Tidskrift/Serie

ChemBioChem

Volym

8

Issue

12

Dokumenttyp

Artikel i tidskrift

Förlag

John Wiley & Sons Inc.

Ämne

  • Microbiology in the medical area
  • Immunology in the medical area

Nyckelord

  • inhibitors
  • galectin
  • cation-pi interaction
  • arenes
  • carbohydrates

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 1439-4227