Centre of Molecular and Macromolecular Studies of the PAS

The Centre of Molecular and Macromolecular Studies of the Polish Academy of Sciences (CMMS PAS) invites research institutions, companies, and innovation-driven partners to engage with us in collaborative use of our advanced analytical and biophysical capabilities.

We offer specialized research services in the field of molecular interaction analysis and structural characterization of substances and materials, with particular emphasis on biologically relevant systems, such as proteins, peptides, ligands, or pharmaceutical compounds. The CMMS PAS team consists of experienced experts conducting both basic and applied research at the intersection of chemistry, biophysics, and materials science. Our laboratory is equipped with state-of-the-art instrumentation along with a solid track record in securing and implementing scientific and industrial projects.

We support both academic research and development activities carried out by industry. Our cooperation model is flexible – ranging from routine analyses to in-depth expert involvement in R&D projects. We analyze samples provided by clients, including biological substances, chemical compounds, composites, and functional materials.

Our analyses target studies of biologically active compounds and complex materials, the development of new drugs and drug delivery strategies, validation of molecular interactions, as well as the design and evaluation of novel functional materials. We provide services to research institutes and universities, R&D laboratories, pharmaceutical, biotech, and chemical companies, as well as entities in materials engineering, bioengineering, and environmental sciences.

Scope of Services

Our laboratory is equipped with modern, specialized analytical instrumentation that enables implementation of advanced molecular and biophysical studies.

Vibrational Spectroscopy (FT-IR / FT-Raman)

We offer access to an advanced FT-IR/FT-Raman research system, equipped with a dedicated module for the analysis of proteins and bioactive substances in aqueous solutions.

In addition to conventional chemical structural analysis, the system enables:

• operation across a broad spectral range using both transmission and reflection techniques (MIR, FIR, NIR),
• determination of protein concentrations in aqueous solutions using sensitive detectors and short optical path lengths – suitable for low-concentration samples,
• assessment of protein conformation and stability under both physiological and extreme conditions,
• monitoring of structural changes during ligand binding or under environmental stress (pH, temperature, ions),
• quantitative analysis of secondary structure content (α-helices, β-sheets, unordered structures),
• characterization of materials in the terahertz range – useful in the study of lattice vibrations, polymorphism, and phase transitions in solids (e.g. pharmaceuticals, biomaterials, semiconductors, composites),
• verification of the physical state of materials and identification of the amorphous phase content (in drugs, supplements, lyophilized proteins, etc.),
• monitoring of dehydration/rehydration processes in pharmaceutical and biological materials,
• analysis of composites and functional materials under varying temperature conditions,
• analysis of nanomaterials, pigments, and dyes – even at low concentrations,
• detection of contaminants in environmental, material, and biological samples, along with spectroscopic identification of unknown substances,
• spectroscopy of highly fluorescent samples – enabling high-quality spectral acquisition from challenging samples (e.g. pigments, plant extracts, tissues, dyes).

Microscale Thermophoresis (MST)

We offer a high-end analytical system for the study of biomolecular interactions using Microscale Thermophoresis (MST). This method allows precise analysis in aqueous solution, without immobilizing the molecules and under near-physiological conditions. With high sensitivity and minimal sample consumption, MST is suitable for both targeted measurements and high-throughput screening.

Applications of MST include:

• investigation of protein–ligand, protein–DNA/RNA, RNA–RNA, protein–protein, and aptamer–target interactions,
• determination of binding parameters (e.g. Kd, EC50) and comparison of molecular affinities,
• testing the influence of environmental factors (pH, ionic solutions, presence of ligands/inhibitors) on interaction stability,
• measurements in complex biological matrices (cellular fractions, serum, biological buffers),
• detection using intrinsic fluorescence or external labels,
• screening of active compounds and evaluation of their selectivity.

Bio-Layer Interferometry (BLI)

We provide precise analysis of molecular interactions using label-free Bio-Layer Interferometry (BLI) technology. This allows real-time measurements of binding events without the need for fluorescent or radioactive labeling. With high sensitivity and real-time capabilities, BLI is a powerful tool for diagnostics, experimental research, and biotechnological applications.

Applications of BLI include:

• analysis of protein–ligand, protein–protein, nucleic acid–ligand, and antigen–antibody interactions,
• determination of kinetic parameters (association/dissociation rates) and complex stability,
• measurements in unpurified environments – such as cell extracts, serum, or other complex biological matrices,
• evaluation of environmental effects on binding events (pH, salt concentrations, cofactors, inhibitors),
• verification of binding selectivity and screening of ligand libraries,
• comparative assessment of molecule variants in drug development or functional material design.