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Press release

Potential anti-AIDS drug compound shows enhanced activity

Molecule against HIV – small change yields major effect

Perfect Fit: The modified anti-HIV molecule (center) binds with higher affinity to the CXCR4 receptor on the surface of immune cells. Copyright: Wiley-VCH Verlag GmbH & Co. KGaA, reproduced with permission. A Conformationally Frozen Peptoid Boosts CXCR4 Affinity and Anti-HIV Activity, Kessler et al., Angewandte Chemie Int. Ed.  2012, 51, 8110-8113
Swarm of Human Immunodeficiency Virus (HIV) – image: iStockphoto

Research news

Researchers from Munich and Naples have shown that minimal modification of a synthetic peptide with anti-HIV activity results in a new compound with more than two orders of magnitude higher binding affinity to the chemokine receptor CXCR4 and greatly improved anti-HIV activity. This could be a step toward the design of new, more effective drugs against AIDS, inflammatory diseases, and some forms of cancer.

Different strains of HIV-1 use either the chemokine receptor CCR5 or CXCR4 for entry into immune cells. While drugs that block usage of CCR5 by the virus are already available for anti-HIV therapy, no drugs have been approved that prevent the virus from using the CXCR4 receptor. Because the new cyclic peptide may be used to block CXCR4, it is a promising new drug candidate to block HIV-1 infections.

An international, interdisciplinary team including researchers in pharmaceutical radiochemistry and chemistry at the Technische Universität München (TUM), a group of molecular modelers at the University of Naples, and virologists at the Helmholtz Zentrum München reported the results in Angewandte Chemie International Edition. This work was initiated by the radiochemists and organic chemists at TUM, who realized that their approach to modifying peptides as high-affinity CXCR4 ligands for imaging of cancers also has the potential to open a whole new area of drug research. 

Perfect Fit: The modified anti-HIV molecule (center) binds with higher affinity to the CXCR4 receptor on the surface of immune cells. Copyright: Wiley-VCH Verlag GmbH & Co. KGaA, reproduced with permission.