Dimeric State Research Articles

Molecular docking study of britannin binding to PD-L1 and related anticancer pseudoguaianolide sesquiterpene lactones

The pseudoguaianolide-type sesquiterpene lactone (SL) britannin (BRT), found in different Inula species, has been characterized as a potent anticancer agent acting via modulation of the transcription factor NFkB and the Nrf2-Keap1 signaling pathway. In addition, a BRT-induced down-regulation of the immune checkpoint PD-L1 (programmed cell death ligand 1) expressed on cancer cells has been evidenced. Here we have performed a docking analysis of the direct binding of BRT to the PD-L1 protein, both in its monomeric and dimeric state. BRT appears to form stable complexes with PD-L1, with a preference for the dimeric form, binding at the interface of the two monomers. The calculated empirical energy of interaction (ΔE) value reaches −63.1 kcal/mol for the BRT-PD-L1 dimer complex, not far from the value calculated with the reference PD-L1 ligand BMS-202 (ΔE = −73.4 kcal/mol) under identical conditions. We also studied the potential PD-L1 dimer binding of 15 pseudoguaianolide sesquiterpene lactones analogues to BRT, including helenalin, gaillardin, bigelovin, coronopilin, and others. The docking analysis predicted that the SL chamissonolide (CHM) can also form equally stable complexes with PD-L1 dimer (ΔE = −64.8 kcal/mol). Preliminary compound structure-PD-L1 binding relationships have been delineated. This computational study supports the proposed interaction of BRT with PD-L1 and provides a guidance to the design of novel PD-L1 binders incorporating a SL-like tricyclic core unit.

Experimental and theoretical studies of pegylated-β-cyclodextrin: A step forward to understand its tunable self-aggregation abilities

In this work we studied the self-aggregation abilities of βCDPEG5, a star-shaped pegylated derivative comprising seven PEG chains selectively conjugated to the primary face of βCD via triazole linkers. The critical aggregation concentration, determined by density measurements, yielded a value of 0.5 mM. Dynamic light scattering (DLS) showed that βCDPEG5 forms nanoaggregates of a hydrodynamic diameter (Dh) of ∼150 nm in water at 25 °C. βCDPEG5 significantly decreased the surface tension of water, thus confirming the aggregation phenomenon. Transmission electron microscopy upheld the presence of the nanoaggregates and revealed their quasi-spherical shape. Nanostructures of 9 nm coexisting with the nanoaggregates were also observed in DLS and correspond to βCDPEG5 dimers. Computational studies analyzed dimers as the initial stage in the βCDPEG5 nanoaggregation process.Both βCDPEG5 nanoaggregates and dimers displayed their same Dh pattern in acidic, neutral, and basic conditions; likewise, when modifying the ionic strength of the medium. Interestingly, the nanoaggregates and dimers varied depending on the experimental conditions, being the former predominant when increasing pH and ionic strength, a behavior attributed to the triazole linkers, which seem to respond smartly to changes in the environment. At 37 °C, only βCDPEG5 nanoaggregates were present with a Dh mean value similar to that at 25 °C. The scattering behavior of nanoaggregates and dimers was studied for 55 days. We found that Dh of both species remains unchanged; nevertheless, at the end of the analysis, the nanoaggregates population was predominant.These overall results demonstrate that βCDPEG5 is an amphiphilic non-ionic system with a remarkable ability to aggregate in water and form defined nanostructures. Moreover, depending on the βCDPEG5 concentration, pH, ionic strength, and temperature, the dimeric or nanoaggregated state can be tuned, being this an attractive feature to load and control the release of a drug.

Ab initio calculation of the ground and first excited states of the lithium dimer

Based on a high level ab initio calculation which is carried out with the multireference configuration interaction method under the aug-cc-pVXZ (AVXZ) basis sets, X = T, Q, 5, the accurate potential energy curves (PECs) of the ground state and the first excited state of Li2 are constructed. By fitting the ab initio potential energy points with the Murrell–Sorbie potential function, the analytic potential energy functions (APEFs) are obtained. The molecular bond length at the equilibrium (R e ), the potential well depth (D e ), and the spectroscopic constants (B e , ω e , α e , and ω e χ e ) for the state and the state are deduced from the APEFs. The vibrational energy levels of the two electronic states are obtained by solving the time-independent Schrödinger equation with the Fourier grid Hamiltonian method. All the spectroscopic constants and the vibrational levels agree well with the experimental results. The Franck–Condon factors (FCFs) corresponding to the transitions from the vibrational level (v′ = 0) of the ground state to the vibrational levels (v″ = 0–74) of the first excited state have been calculated. The FCF for the vibronic transition of (v″ = 0) ←(v′ = 0) is the strongest. These PECs and corresponding spectroscopic constants provide reliable theoretical references to both the spectroscopic and the molecular dynamic studies of the Li2 dimer.

Non-conventional octameric structure of C-phycocyanin

C-phycocyanin (CPC), a blue pigment protein, is an indispensable component of giant phycobilisomes, which are light-harvesting antenna complexes in cyanobacteria that transfer energy efficiently to photosystems I and II. X-ray crystallographic and electron microscopy (EM) analyses have revealed the structure of CPC to be a closed toroidal hexamer by assembling two trimers. In this study, the structural characterization of non-conventional octameric CPC is reported for the first time. Analyses of the crystal and cryogenic EM structures of the native CPC from filamentous thermophilic cyanobacterium Thermoleptolyngbya sp. O–77 unexpectedly illustrated the coexistence of conventional hexamer and novel octamer. In addition, an unusual dimeric state, observed via analytical ultracentrifugation, was postulated to be a key intermediate structure in the assemble of the previously unobserved octamer. These observations provide new insights into the assembly processes of CPCs and the mechanism of energy transfer in the light-harvesting complexes.

Archaeal Hsp14 drives substrate shuttling between small heat shock proteins and thermosome: insights into a novel substrate transfer pathway.

Heat shock proteins maintain protein homeostasis and facilitate the survival of an organism under stress. Archaeal heat shock machinery usually consists of only sHsps, Hsp70, and Hsp60. Moreover, Hsp70 is absent in thermophilic and hyperthermophilic archaea. In the absence of Hsp70, how aggregating protein substrates are transferred to Hsp60 for refolding remains elusive. Here, we investigated the crosstalk in the heat shock response pathway of thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. In the present study, we biophysically and biochemically characterized one of the small heat shock proteins, Hsp14, of S. acidocaldarius. Moreover, we investigated its ability to interact with Hsp20 and Hsp60 to facilitate the substrate proteins' folding under stress conditions. Like Hsp20, we demonstrated that the dimer is the active form of Hsp14, and it forms an oligomeric storage form at a higher temperature. More importantly, the dynamics of the Hsp14 oligomer are maintained by rapid subunit exchange between the dimeric states, and the rate of subunit exchange increases with increasing temperature. We also tested the ability of Hsp14 to form hetero-oligomers via subunit exchange with Hsp20. We observed hetero-oligomer formation only at higher temperatures (50 °C-70 °C). Furthermore, experiments were performed to investigate the interaction between small heat shock proteins and Hsp60. We demonstrated an enthalpy-driven direct physical interaction between Hsp14 and Hsp60. Our results revealed that Hsp14 could transfer sHsp-captured substrate proteins to Hsp60, which then refolds them back to their active form.

Field-induced anomalous magnetic state beyond the magnetically ordered state in the slightly distorted triangular S=12 rare-earth antiferromagnet CeZn3P3

Magnetic properties of ${\mathrm{CeZn}}_{3}{\mathrm{P}}_{3}$, which has been believed to have the same hexagonal ${\mathrm{ScAl}}_{3}{\mathrm{C}}_{3}$-type crystal structure as that of a spin dimer system of ${\mathrm{YbAl}}_{3}{\mathrm{C}}_{3}$ at room temperature, have been investigated by magnetization, magnetostriction, specific heat ($C$), and magnetocaloric effect measurements. In this research, we have found that ${\mathrm{CeZn}}_{3}{\mathrm{P}}_{3}$ certainly has a slightly deformed crystal structure from the hexagonal one even at room temperature, which is in contrast to the structural phase transition of ${\mathrm{YbAl}}_{3}{\mathrm{C}}_{3}$ occuring at around 80 K, although the very slight deformation along the $c$ plane, i.e., slightly deformed triangular lattice, and the formation of the multidomain structure are common to both compounds. ${\mathrm{CeZn}}_{3}{\mathrm{P}}_{3}$ is thought to maintain its deformed structure from a high-temperature region above room temperature to an extremely low-temperature region and shows a magnetic order below ${T}_{\mathrm{N}}=0.8$ K. The analysis of the temperature dependence of the magnetic susceptibility ($\ensuremath{\chi}$) and $C$ has revealed that a Kramers doublet ground state with an easy-plane type anisotropy on the $c$ plane is well isolated from the excited states by the crystal field splitting energy of more than 300 K. Above ${T}_{\mathrm{N}}, \ensuremath{\chi}$ makes a broad peak at around 2 K, which certainly originates from the dimer formation due to the slight deformation of the triangular lattice. On the other hand, below ${T}_{\mathrm{N}}$, a magnetic phase diagram reminiscent of a magnetic flower blooming on the $c$ plane was observed, which may have a close relation to a quantum effect of a quasi $S=\frac{1}{2}$ spin system and a contribution of the orbital component. With increasing magnetic field, we have found an anomalous magnetic state beyond the usual magnetically ordered state, where $C/T$ is anomalously enhanced. This anomalous magnetic state is similar to that observed in ${\mathrm{YbAl}}_{3}{\mathrm{C}}_{3}$ induced by the field, although the magnetic ground state in ${\mathrm{YbAl}}_{3}{\mathrm{C}}_{3}$ is a nonmagnetic dimer state different from the normal magnetically ordered state in ${\mathrm{CeZn}}_{3}{\mathrm{P}}_{3}$.

Trop2 Forms a Stable Dimer with Significant Structural Differences within the Membrane-Distal Region as Compared to EpCAM.

Trop2 is a cell-surface transmembrane glycoprotein involved in the maintenance of epithelial tissue integrity and is an important carcinoma marker. It shares similar claudin-interaction capacity with its paralogue EpCAM, and both are implicated in signaling triggered by proteolytic cleavage within the ectodomain. However, the cell proliferation-regulating interactions with IGF-1, neuregulin-1, and α5β1 integrin appear to be Trop2-specific. To illuminate the structural differences between Trop2 and EpCAM, we report the first crystal structure of a Trop2 ectodomain dimer and compare it to the analogous part of EpCAM. While the overall fold of the two proteins is similar, the dimers differ. In Trop2, the inter-subunit contacts are more extensive than in EpCAM, and there are two major differences in the membrane-distal regions. The immunogenic N-terminal domain is in Trop2 almost colinear with the dimer interface plain and consequently more laterally exposed, and the cleft of yet unknown functionality between the two subunits is almost absent. Furthermore, the site of initial signaling-associated proteolytic cleavage in Trop2 is accessible in the dimeric state, while in EpCAM dimer destabilization is required. The structural differences highlight the divergent evolutionary path of the two proteins and pave the way for their structure-based utilization in therapy.

Engineering Photoresponsive Ligand Tethers for Mechanical Regulation of Stem Cells.

Regulating stem cell functions by precisely controlling the nanoscale presentation of bioactive ligands has a substantial impact on tissue engineering and regenerative medicine but remains a major challenge. Here it is shown that bioactive ligands can become mechanically "invisible" by increasing their tether lengths to the substrate beyond a critical length, providing a way to regulate mechanotransduction without changing the biochemical conditions. Building on this finding, light switchable tethers are rationally designed, whose lengths can be modulated reversibly by switching a light-responsive protein, pdDronpa, in between monomer and dimer states. This allows the regulation of the adhesion, spreading, and differentiation of stem cells by light on substrates of well-defined biochemical and physical properties. Spatiotemporal regulation of differential cell fates on the same substrate is further demonstrated, which may represent an important step toward constructing complex organoids or mini tissues by spatially defining the mechanical cues of the cellular microenvironment with light.

Protease-sensitive regions in amyloid light chains: what a common pattern of fragmentation across organs suggests about aggregation.

Light‐chain (AL) amyloidosis is characterized by deposition of immunoglobulin light chains (LC) as fibrils in target organs. Alongside the full‐length protein, abundant LC fragments are always present in AL deposits. Herein, by combining gel‐based and mass spectrometry analyses, we identified and compared the fragmentation sites of amyloid LCs from multiple organs of an AL λ amyloidosis patient (AL‐55). The positions pinpointed here in kidney and subcutaneous fat, alongside those previously detected in heart of the same patient, were aligned and mapped on the LC’s dimeric and fibrillar states. All tissues contain fragmented LCs along with the full‐length protein; the fragment pattern is coincident across organs, although microheterogeneity exists. Multiple cleavage positions were detected; some are shared, whereas some are organ‐specific, likely due to a complex of proteases. Cleavage sites are concentrated in ‘proteolysis‐prone’ regions, common to all tissues. Several proteolytic sites are not accessible on native dimers, while they are compatible with fibrils. Overall, data suggest that the heterogeneous ensemble of LC fragments originates in tissues and is consistent with digestion of preformed fibrils, or with the hypothesis that initial proteolytic cleavage of the constant domain triggers the amyloidogenic potential of LCs, followed by subsequent proteolytic degradation. This work provides a unique set of molecular data on proteolysis from ex vivo amyloid, which allows discussing hypotheses on role and timing of proteolytic events occurring along amyloid formation and accumulation in AL patients.

Structure and dynamics of UBA5-UFM1 complex formation showing new insights in the UBA5 activation mechanism

Ubiquitin fold modifier 1 (UFM1) is an ubiquitin-like protein (Ubl) involved especially in endoplasmic stress response. Activation occurs via a three-step mechanism like other Ubls. Data obtained reveal that UFM1 regulates the oligomeric state of ubiquitin activating enzyme 5 (UBA5) to initiate the activation step. Mixtures of homodimers and heterotrimers are observed in solution at the equilibrium state, demonstrating that the UBA5-UFM1 complex undergoes several concentration dependent oligomeric translational states to form a final functional complex. The oligomerization state of unbound UBA5 is also concentration dependent and shifts from the monomeric to the dimeric state. Data describing different oligomeric states are complemented with binding studies that reveal a negative cooperativity for the complex formation and thereby provide more detailed insights into the complex formation mechanism.

The regulatory light chain mediates inactivation of myosin motors during active shortening of cardiac muscle

The normal function of heart muscle depends on its ability to contract more strongly at longer length. Increased venous filling stretches relaxed heart muscle cells, triggering a stronger contraction in the next beat- the Frank-Starling relation. Conversely, heart muscle cells are inactivated when they shorten during ejection, accelerating relaxation to facilitate refilling before the next beat. Although both effects are essential for the efficient function of the heart, the underlying mechanisms were unknown. Using bifunctional fluorescent probes on the regulatory light chain of the myosin motor we show that its N-terminal domain may be captured in the folded OFF state of the myosin dimer at the end of the working-stroke of the actin-attached motor, whilst its C-terminal domain joins the OFF state only after motor detachment from actin. We propose that sequential folding of myosin motors onto the filament backbone may be responsible for shortening-induced de-activation in the heart.

The protein hydration layer in high glucose concentration: Dynamical responses in folded and intrinsically disordered dimeric states

This exposition reveals the effect of glucose as a molecular crowder on the solvent environment in proximity of the protein surface in putative folded (Ubiquitin) and intrinsically disordered (dimeric Amyloid beta) states. Atomistic simulations reveal markedly higher structural perturbation in the disordered systems due to crowding effects, while the folded state retains overall structural fidelity. Key hydrophobic contacts in the disordered dimer are lost. However, glucose induced crowding results in elevated hydration on surfaces of both protein systems. Despite evident differences in their structural responses, the hydration layer of both the folded and disordered states display a distinct enhancement in lifetimes of mean residence and rotational relaxation under the hyperglycemic conditions. The results are crucial in the light of emergent co-solvent induced biological phenomena in crowded media.

Potential bioactive compounds as SARS-CoV-2 inhibitors from extracts of the marine red alga Halymenia durvillei (Rhodophyta) - A computational study.

The respiratory infection COVID-19 caused by the virus SARS CoV-2 has continued to be a major health problem worldwide and has caused more than a million mortalities. Even if the development of COVID-19 vaccines has shown much progress, efforts to find novel, natural anti-viral drugs should be pursued. Halymenia durvillei is a marine red alga widely distributed around Southeast Asia. This study aimed to develop new anti SARS CoV-2 compounds from ethanolic and ethyl acetate extracts of H. durvillei via a computational approach, focusing onthe inhibitory action against the main protease (3CL-Mpro). In this study, 37 compounds were extracted and identified by GC–MS analysis. The potentials of compounds 1–2 tetradecandiol and E,E,Z-1,3,12-nonadecatriene-5,14-diol were identified for therapeutic purposes based on our pharmacophore study, while cholest-5-En-3-Ol (3.Beta.)- had a high fitness score in molecular docking studies both in monomer and dimer state compared to the N3 inhibitor and remdesivir affinity scores. As these compounds show competitive affinity scores against the 3CL-Mpro, these natural compounds may be effective for the treatment of COVID-19 infection. The ADME and pharmacokinetic studies should also be employed to assess the ability of the natural compounds as oral drugs. These promising results have shown the potentials of H. durvillei as an alternative drug in addressing COVID-19 infection. Accordingly, further studies should explore the effectiveness of these active compounds.

Unconventional, Gram-Scale Synthesis of a Molecular Dimer Organic Luminogen with Aggregation-Induced Emission.

Organic luminogens have been widely used in optoelectronic devices, bioimaging, and sensing. Conventionally, the synthesis of organic luminogens requires sophisticated, multistep design, reaction, and isolation procedures. Herein, the products of the melt-phase condensation of benzoguanamine (BG; 2,4-diamino-6-phenyl-1,3,5-triazine) at 370-410 °C display interesting reaction-condition-dependent luminescence properties, including photoluminescence (PL) at a variety of wavelengths in the visible spectrum and quantum efficiencies (PLQE) of up to 58% in the powder form. With a simple and straightforward solvent washing procedure, the prominent blue luminescent component BG dimer was obtained in gram scale with >93% purity (96.5% purity after fractional sublimation). The BG dimer exhibited distinct aggregation-induced emission (AIE) properties. PL measurements indicate that the electronically excited state of the BG dimer undergoes efficient intramolecular nonradiative deactivation in room-temperature solution, leading to a significantly reduced PLQE (<0.1%) in solution. These nonradiative processes are substantially inhibited when the dimer existed in the form of crystals, solid aggregates in solution or being fixed in a rigid polymer film, resulting in a significant increase in the PLQE and lifetime. This work not only provided a new understanding for PL properties of self-condensation luminescent products but also represented an unconventional strategy for large-scale preparation of organic luminogens with high purity.

Dimerization underlies the aggregation propensity of intrinsically disordered coiled-coil domain-containing 124.

Coiled-coil domain-containing 124 (CCDC124) is a recently discovered ribosome-binding protein conserved in eukaryotes. CCDC124 has regulatory functions on the mediation of reversible ribosomal hibernation and translational recovery by direct attachment to large subunit ribosomal protein uL5, 25S rRNA backbone, and tRNA-binding P/A-site major groove. Moreover, it independently mediates cell division and cellular stress response by facilitating cytokinetic abscission and disulfide stress-dependent transcriptional regulation, respectively. However, the structural characterization and intracellular physiological status of CCDC124 remain unknown. In this study, we employed advanced in silico protein modeling and characterization tools to generate a native-like tertiary structure of CCDC124 and examine the disorder, low sequence complexity, and aggregation propensities, as well as high-order dimeric/oligomeric states. Subsequently, dimerization of CCDC124 was investigated with co-immunoprecipitation (CO-IP) analysis, immunostaining, and a recent live-cell protein-protein interaction method, bimolecular fluorescence complementation (BiFC). Results revealed CCDC124 as a highly disordered protein consisting of low complexity regions at the N-terminus and an aggregation sequence (151-IAVLSV-156) located in the middle region. Molecular docking and post-docking binding free energy analyses highlighted a potential involvement of V153 residue on the generation of high-order dimeric/oligomeric structures. Co-IP, immunostaining, and BiFC analyses were used to further confirm the dimeric state of CCDC124 predominantly localized at the cytoplasm. In conclusion, our findings revealed in silico structural characterization and in vivo subcellular physiological state of CCDC124, suggesting low-complexity regions located at the N-terminus of disordered CCDC124 may regulate the formation of aggregates or high-order dimeric/oligomeric states.

Structures of dimeric human NPC1L1 provide insight into mechanisms for cholesterol absorption.

Polytopic Niemann-Pick C1-like 1 (NPC1L1) plays a major role in intestinal absorption of biliary cholesterol, vitamin E (VE), and vitamin K (VK). The drug ezetimibe inhibits NPC1L1-mediated absorption of cholesterol, lowering of circulating levels of low-density lipoprotein cholesterol. Here, we report cryo-electron microscopy structures of human NPC1L1 (hNPC1L1) bound to either cholesterol or a lipid resembling VE. These findings, together with functional assays, reveal that the same intramolecular channel in hNPC1L1 mediates transport of VE and cholesterol. hNPC1L1 exists primarily as a homodimer; dimerization is mediated by aromatic residues within a region of transmembrane helix 2 that exhibits a horizonal orientation in the membrane. Mutation of tryptophan-347 lies in this region disrupts dimerization and the resultant monomeric NPC1L1 exhibits reduced efficiency of cholesterol uptake. These findings identify the oligomeric state of hNPC1L1 as a target for therapies that inhibit uptake of dietary cholesterol and reduce the incidence of cardiovascular disease.

Electronic and Magnetic Properties of Building Blocks of Mn and Fe Atomic Chains on Nb(110).

We present results for the electronic and magnetic structure of Mn and Fe clusters on Nb(110) surface, focusing on building blocks of atomic chains as possible realizations of topological superconductivity. The magnetic ground states of the atomic dimers and most of the monatomic chains are determined by the nearest-neighbor isotropic interaction. To gain physical insight, the dependence on the crystallographic direction as well as on the atomic coordination number is analyzed via an orbital decomposition of this isotropic interaction based on the spin-cluster expansion and the difference in the local density of states between ferromagnetic and antiferromagnetic configurations. A spin-spiral ground state is obtained for Fe chains along the [] direction as a consequence of the frustration of the isotropic interactions. Here, a flat spin-spiral dispersion relation is identified, which can stabilize spin spirals with various wave vectors together with the magnetic anisotropy. This may lead to the observation of spin spirals of different wave vectors and chiralities in longer chains instead of a unique ground state.

Effect of Dimer Structure and Inhomogeneous Broadening of Energy Levels on the Action of Flavomononucleotide in Rigid Polyvinyl Alcohol Films.

The results of time-resolved fluorescence measurements of flavin mononucleotide (FMN) in rigid polyvinyl alcohol films (PVA) demonstrate that fluorescence intensity decays are strongly accelerated in the presence of fluorescent dimers and nonradiative energy transfer processes. The fluorescence decay originating both from H and J dimer states of FMN was experimentally observed for the first time. The mean fluorescence lifetimes for FMN dimers were obtained: = 2.66 ns (at λexc = 445 nm) and = 2.02 (at λexc = 487 nm) at λobs = 600 nm and T = 253 K from H and J state of dimers, respectively. We show that inhomogeneous orientational broadening of energy levels (IOBEL) affects the shape of the fluorescence decay and leads to the dependence of the average monomer fluorescence lifetime on excitation wavelength. IOBEL affected the nonradiative energy transfer and indicated that different flavin positioning in the protein pocket could (1) change the spectroscopic properties of flavins due to the existence of “blue” and “red” fluorescence centers, and (2) diminish the effectiveness of energy transfer between FMN molecules.

Direct ab initio molecular dynamics study on the reactions of multi-valence ionized states of water dimer

We investigated the reaction of multi-valence (+2) ionization states of water dimer (H2O)2 using direct ab initio molecular dynamics method. The following multi-valence ionization states were considered. In the direct two-electron ionization state, (H2O)2 was ionized to form (H2O)2 2+ in one step; in the stepwise two-electron ionization state, (H2O)2 was first converted to (H2O)2 + and further ionized after structural relaxation. The (H2O)2 2+ from direct ionization dissociated into two H2O+ ions, while (H2O)2 2+ in stepwise ionization generated H3O+ and OH+ ions from H3O+–OH radical-ion pairs. Additionally, we performed dynamics calculations for the excited state of (H2O)2 2+ generated through direct ionization. The excited (H2O)2 2+ ions also dissociated to form H3O+ and OH+ ions. The reaction mechanism of multi-valence ionization states of (H2O)2 is discussed on the basis of calculation results.

Coupling of Yu-Shiba-Rusinov states in one-dimensional chains of Fe atoms on Nb(110)

The hybridization of Yu-Shiba-Rusinov states in dimers of magnetic impurities leads to molecular-like bonding and antibonding modes. In many-impurity systems, the interaction gives rise to YSR bands and can even result in the formation of a topologically non-trivial superconducting state, characterized by Majorana fermions at the edges of the system. To obtain a more detailed understanding of these interactions, we investigate the coupling of YSR states in short one-dimensional Fe chains on clean Nb(110). We observe a splitting of the single-atom YSR peaks into multiple states with even or odd spatial symmetry and identify a peculiar dependence of the even and odd states' energy position on the chain length.