We are looking for outstanding graduates from all over the world and are delighted to provide them with the best possible conditions for their scientific careers. The candidate will be employed and strongly connected to the scientific activities at Apoglyx AB. In addition, the candidate will join the graduate program at Lund University at faculty of medicine, providing an interdisciplinary education for doctoral candidates at the interface of molecular life sciences and clinical science. If you have a passion for structural biology, molecular biology, cell biology, protein biochemistry and drug discovery and want to work in an interdisciplinary setting between Lund University at the faculty of medicine, and ApoGlyx AB - this is the doctoral program for you!

You have:

· an above-average master's or comparable degree in molecular biology, biochemistry, or any related areas, awarded by March 2025 or earlier;

· some experience with protein biochemistry or structural biology;

· very good written and spoken English;

We offer:

· cutting-edge research within medical structural biology with unique conditions as you will be employed by the biotech company Apoglyx AB (website: https://apoglyx.com) and admitted to the doctoral program at faculty of medicine at Lund University

· 4 years funding to work on your doctoral project

· a degree from Lund University

· excellent structured supervision

· a diverse community to exchange ideas with

· a flexible and challenging curriculum of scientific courses and transferable skills

· support for attending conferences to present your work

· an international graduate program in one of Europe's most exciting cities

Timeline:

· Apply asap or by 30^th of January 2025 (18:00 CET) by sending an email to Prof. Lindkvist

· Short-listed candidates are invited to Lund for interviews in January 2025

· Successful candidates start their doctorate as soon as possible, at the lasted the 1^st of June 2025

Application:

Please prepare your CV and motivation letter, your academic record, a research proposal and the name of two referees willing to provide references, then apply by the 30^th of January 2025.

Contact: Prof. Karin Lindkvist (karin.lindkvist@med.lu.se)

Short summary of the project with a few references from Lindkvist laboratory.

Maintaining a balance between activation and suppression of immune response is critical for the immune system. Systemic Inflammatory Response Syndrome (SIRS) is an exaggerated response of the immune system and is a potentially life-threatening medical condition that is characterized by a self-harming immune response. SIRS can

be initiated by an infection (then called sepsis), or by sterile causes of cell damage, such as trauma. A hallmark of both sepsis and SIRS is the massive recruitment neutrophils from the bone marrow into the circulation. Together with academic collaborators, ApoGlyx AB has demonstrated that genetic ablation of AQP9 is an effective way for interfering with SIRS, by preventing tissue infiltration of neutrophils. Based on these promising results, the aim is to decipher the structural-functional activity of AQP9 and develop a series of compounds blocking its activity. The 3D structure of AQP9 will be determined with and without inhibitors by single particle cryo-EM to augment structure-based drug design. Furthermore, the inhibitor-effect of the newly developed compounds will be evaluated in neutrophils.

Molecular basis for human aquaporin inhibition.

Huang P, Åbacka H, Wilson CJ, Wind ML, Rützler M, Hagström-Andersson A, Gourdon P, de Groot BL, Venskutonytė R, Lindkvist-Petersson K.

Proc Natl Acad Sci U S A. 2024 Feb 13;121(7):e2319682121. doi: 10.1073/pnas.2319682121.

SMS121, a new inhibitor of CD36, impairs fatty acid uptake and viability of acute myeloid leukemia

Åbacka H, Masoni S, Poli G, Huang P, Gusso F, Granchi C, Minutolo F, Tuccinardi T, Hagström-Andersson AK, Lindkvist-Petersson K.

Sci Rep. 2024 Apr 20;14(1):9104. doi: 10.1038/s41598-024-58689-1.

Cryo-EM structure supports a role of AQP7 as a junction protein.

Huang P, VenskutonytėT R PrasadRB, ArdalaniH, de MaréSW, FanX, LiP, SpégelP, YanN, GourdonP, ArtnerI, Lindkvist-Petersson K.

Nature Commun. 2023 Feb 3;14(1):600. doi: 10.1038/s41467-023-36272-y

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