Conformational ensembles explored dynamically from disordered peptides targeting chemokine receptor CXCR4

Marian Vincenzi, Susan Costantini, Stefania Scala, Diego Tesauro, Antonella Accardo, Marilisa Leone, Giovanni Colonna, Jean Guillon, Luigi Portella, Anna Maria Trotta, Luisa Ronga, Filomena Rossi

Research output: Contribution to journalArticlepeer-review


This work reports on the design andthe synthesis of two short linear peptides both containing a few amino acids with disorder propensity and an allylic ester group at the  C-terminal end. Their structural properties were firstly analyzed by means of experimental techniques in solution such as CD and NMR methodsthat highlighted peptide flexibility. These results were further confirmed by MD simulationsthat demonstrated the ability of the peptides to assume conformational ensembles. Theyrevealed a network of transient and dynamic -bonds and interactions with water molecules. Binding assays with a well-known drug-target, i.e., the CXCR4 receptor, were also carried out in an attempt to verify their biological function and the possibility to use the assays to develop new specific targets for CXCR4. Moreover, our data indicate that these peptides represent useful tools for molecular recognition processes in which a flexible conformation is required in order to obtain an interaction with a specific target.

Original languageEnglish
Pages (from-to)12159-12173
Number of pages15
JournalInternational Journal of Molecular Sciences
Issue number6
Publication statusPublished - May 28 2015


  • CD
  • Chemokine
  • Conformational ensemble
  • Intrinsically disordered protein (ID)
  • Intrinsically disordered region(IDR)
  • MD
  • NMR

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Spectroscopy
  • Inorganic Chemistry
  • Catalysis
  • Molecular Biology
  • Computer Science Applications


Dive into the research topics of 'Conformational ensembles explored dynamically from disordered peptides targeting chemokine receptor CXCR4'. Together they form a unique fingerprint.

Cite this