Cancer and Infectious Diseases


Through interdisciplinary collaborations, the cluster aims at discovery and optimization of anticancer and/or antimicrobial lead compounds that combat emerging multidrug resistance. These are validated by in vitro and in vivo models. Our mission is to:

• Design peptides/peptidomimetics and small molecules that combat multidrug-resistant bacterial infections and identify novel targets

• Develop and apply cutting-edge technologies for identification of natural products with potential as antibiotics and chemotherapeutic leads

• Explore and validate novel anticancer compounds and targets



In a recent study published in Antibiotics, Hansen and coworkers describe the synthesis of C-locked analogues of the antimicrobial peptide BP214 which is an efficient strategy for obtaining cyclic lipopeptides.


In a recent study led by Daniela De Zio and Elena Papaleo (Danish Cancer Society and DTU) published in Cell Death and Disease, a new bioinformatic tool Cancermuts, able to retrieve, annotate and prioritize cancer-associated mutations, was presented. Cancermuts can predict the pathogenic impact of missense cancer variants in any protein target. To validate the tool, AMBRA1 mutations in melanoma, where AMBRA1 is highly mutated and displays a tumor-suppressive role, were selected as a case study.


In a recent study published in International Journal of Molecular Sciences, Hansen, Sheykhzhade and coworkers describe the synthesis of three different fluorescent analogues of α-calcitonin gene-related peptide with potent vasodilator activity. The analogues are promising tool compounds for further studies of the mechanism for internalization of CGRP receptors in live tissue and neuronal reuptake of the α-CGRP peptide.


In a collaborative study led by Jan Stenvang and Dan Staerk, a natural product isolated from the Australian desert plant Eremophila galeata was shown to inhibit the Breast Cancer Resistance Pump (BCRP) involved in multidrug resistance. Docking studies show that the isolated compound binds to the same BCRP site as the active metabolite of the natural product-derived irinotecan, and this discovery opens up for design of new drug leads for reversal of BCRP-mediated multidrug resistance.















Cluster Leader

Henrik Franzyk
Associate professor

Communications representativ

Communications Representative

Dan Stærk