Three early-career researchers have each been awarded a Starting Grant by the European Research Council (ERC) for their projects with LMU.

Nano researcher Quinten Akkermann, cultural scientist Marianna Mazzola, and biophysicist Lukas Milles have each been awarded a Starting Grant by the European Research Council (ERC) for their new research projects at LMU. In each case, the funding is worth some 1.5 million euros. The ERC awards Starting Grants based on the scientific excellence of the applicant and of the proposed project. They are among the most prestigious research awards in Europe.

The individual projects:

Control of quantum dots
Dr. Quinten Akkerman leads the Quantum Dot Synthesis and Characterization research group in the Chair of Photonics and Optoelectronics at LMU’s Nano-Institute.
Quantum dots (QDs) have become a focus of nanophysics research in recent years. These dots possess novel and unexpected properties, which can be used for innovative devices in electronics, optoelectronics, and quantum information processing. One example is lead halide perovskite quantum dots (PQDs). These PQDs are a promising candidate for fulfilling the rising demand for smaller, more efficient, and more complex components. Their ion chemistry is difficult to control, however, which limits their tunability, stability, processability, and efficiency. Consequently, it remains difficult to integrate them into efficient optoelectronic and quantum devices.

This is where Quinten Akkerman’s project CONTROL, which has now been awarded an ERC Starting Grant, comes in. Its goal is to develop the first generation of PQDs with fully tunable ligand shells and epitaxial interfaces with non-perovskite semiconductors. CONTROL thus seeks to furnish not only fundamental insights into the synthesis and ligands of PQDs, but also obtain significant advances in the tuning of their optical properties and their surface chemistry. The basis for this is a fundamental understanding of the complex and rapid chemical processes. To this end, CONTROL will develop new instruments, such as an automated in-situ spectroscopic synthesis platform.

The findings of CONTROL, will serve to redesign the synthesis of PQDs, with the overall goal to improve their optical characteristics and surface chemistry and prepare the QDs to facilitate their efficient integration into the next generation of innovative devices.

Christian bishops in the Islamic period
Dr. Marianna Mazzola is assistant professor at Pisa Unviersity. She is also an associate member of the Munich Research Centre for Jewish-Arabic Cultures.
In her research, Marianna Mazzola explores how the social, religious, and political transformations of the Islamic period (from the middle of the 7th into the 10th century) shaped the Christian communities of the Middle East, changing their episcopal leadership, networks and power structures. Her new project MASLAB (Making the Islamicate Bishop: Episcopal Governance and Networks under Islam), draws for the first time on a multilingual and cross-genre corpus. This enables her to investigate how the bishops navigated shifting circumstances and what relationships and resources they mobilized in response to the new sociopolitical and religious dynamics. These include the legal codification of the social status of non-Muslims, the downgrading of Christianity from a religion enjoying imperial backing to a political minority, the emergence of internal denominational boundaries within Christianity, and a fluid and federalized conception of power and territoriality.

Mazzola’s approach offers a novel understanding of episcopal leadership in the Islamic period. This deconstructs the dominant paradigm, which views non-Muslim groups as monolithic, state-recognized units and understands the episcopal relationship to power exclusively through the dyadic “bishop-caliph” model. MASLAB shifts the analytical lens from binary paradigms toward a multi-actor model, and and emphasizes political, rather than solely religious, interpretations, taking proper account of the sociopolitical variability of Islamic rule.

Determining protein mechanics more efficiently
Lukas Milles is Professor of De Novo Protein Design, leads a research group at LMU’s Gene Center Munich, and is a member of the BioSysteM Cluster of Excellence. He researches how to design completely new proteins with specific properties with the aid of artificial intelligence.

Mechanical forces that control the interactions and folding of proteins play a key role in biology. They determine the fate of cells and are decisive factors in the infection processes of pathogens and the immune response to them. So-called catch bonds are particularly important in these processes. Catch bonds are atypical bonds which increase their lifetime with mechanical force, whereas one would intuitively expect their lifetime to decrease with force.

“Currently we possess neither models nor sufficiently large datasets to predict a catch bond based on protein structure alone, never mind synthetically design new catch bonds,” says Milles. Consequently, scientists investigate the protein mechanics experimentally in the laboratory. With single-molecule force spectroscopy (SMFS), it is possible to study the forces involved very precisely. However, the method is very slow and time-consuming. Correspondingly few protein interactions have been measured with this technique to date. A database with proteins that have been characterized using SMFS over the past 30 years contains scarcely more than 85 entries.

The overarching goal of PHENOMECHANICAL (Phenotyping of protein mechanics libraries to unravel the design principles of catch bonds) is therefore to compile a comprehensive library with datasets for thousands of protein-protein interactions. To this end, Milles plans to establish a method that can measure mechanical forces between proteins with high throughput: “The key innovation consists in linking the lifetime of a bond with DNA sequencing by coupling the phenotype to the sequenceable genotype.” The resolution will be comparable to established approaches, while the throughput will be accelerated by at least two orders of magnitude.

It is precisely this increased throughput that is used to identify the design principles of catch bonds using de novo protein design. “Ultimately, it’s my goal to develop synthetically designed catch bonds with adjustable lifetimes, which could be used in novel biomaterials or as synthetic cell receptors,” says Milles. “The combination of protein design and high-throughput analyses will establish large datasets for protein mechanics, which will be suitable for machine learning approaches and may thus open up new paths for predicting the catch bonding behavior from protein structure alone.”