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Title: Crystal structure of N-{N-[N-acetyl-(S)-leucyl]-(S)-leucyl}norleucinal (ALLN), an inhibitor of proteasome

The title compound, C20H37N3O4, also known by the acronym ALLN, is a tripeptidic inhibitor of the proteolytic activity of the proteasomes, enzyme complexes implicated in several neurodegenerative diseases and other disorders, including cancer. Thus, the crystal structure of ALLN, solved from synchrotron radiation diffraction data, revealed the molecules in extended conformation of the backbone and engaging all peptide N and O atoms in intermolecular hydrogen bonds forming an infinite antiparallel β-sheet.
Authors:
 [1] ;  [1] ;  [2] ;  [2]
  1. Peptides International, Inc., Louisville, KY (United States)
  2. Argonne National Lab. (ANL), Argonne, IL (United States)
Publication Date:
OSTI Identifier:
1225201
Grant/Contract Number:
AC02-06CH11357; W-31-109-ENG-38
Type:
Accepted Manuscript
Journal Name:
Acta Crystallographica. Section E, Crystallographic Communications
Additional Journal Information:
Journal Volume: 71; Journal Issue: 3; Journal ID: ISSN 2056-9890
Publisher:
International Union of Crystallography
Research Org:
Argonne National Laboratory (ANL), Argonne, IL (United States)
Sponsoring Org:
USDOE
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES crystal structure; proteasome inhibitor; hydrogen bonding; antiparallel β-sheet