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PubMed1997

Structural and kinetic investigations on the 15-21 and 42-45 loops of muscle acylphosphatase: evidence for their involvement in enzyme catalysis and conformational stabilization.

The structural and catalytic importance of the 15-21 and 42-45 loop residues of the acylphosphatase muscular isoenzyme has been investigated by oligonucleotide-directed mutagenesis. Seven mutants involving conserved residues of the two loops have been prepared and characterized for structural, kinetic, and stability features by using different spectroscopic techniques and compared to the wild-type enzyme. The results are discussed in light of the crystal structure of the highly homologous common type acylphosphatase [Thunnissen et al. (1997) Structure 5, 69-79]. A differential role of the two loops has emerged: the 15-21 and the 42-45 loops appear mainly involved in active site formation and enzyme structural stabilization, respectively. These conclusions are supported by a strong impairment of the catalytic efficiency, in terms of enzymatic activity and substrate binding capability, for most of the 15-21 loop mutants. In particular, the Gly15Ala mutant is completely inactive and displays a native-like overall fold, indicating that the correct geometry of the 15-21 loop is an essential requisite for optimal enzymatic catalysis. Instead, the Gly45Ala mutant, though revealing unchanged catalytic properties, shows a considerably reduced conformational stability, as judged by circular dichroism and 1H NMR spectroscopy. This finding confirms previous results relative to Thr42 and Thr46 residues [Taddei et al. (1996) Biochemistry 35, 7077-7083] underlining the structural importance of the 42-45 loop as a linker for the two beta alpha beta units constituting the overall enzyme structure.

Acid Anhydride Hydrolases↗

PubMed1997

Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus.

The basis of protein stability has been investigated by the structural comparison of themophilic enzymes with their mesophilic counterparts. A number of characteristics have been found that can contribute to the stabilization of thermophilic proteins, but no one is uniquely capable of imparting thermostability. The crystal structure of 3-isopropylmalate dehydrogenase (IPMDH) from the mesophiles Escherichia coli and Salmonella typhimurium have been determined by the method of molecular replacement using the known structure of the homologous Thermus thermophilus enzyme. The structure of the E. coli enzyme was refined at a resolution of 2.1 A to an R-factor of 17.3%, that of the S. typhimurium enzyme at 1.7 A resolution to an R-factor of 19.8%. The three structures were compared to elucidate the basis of the higher thermostability of the T. thermophilus enzyme. A mutant that created a cavity in the hydrophobic core of the thermophilic enzyme was designed to investigate the importance of packing density for thermostability. The structure of this mutant was analyzed. The main stabilizing features in the thermophilic enzyme are an increased number of salt bridges, additional hydrogen bonds, a proportionately larger and more hydrophobic subunit interface, shortened N and C termini and a larger number of proline residues. The mutation in the hydrophobic core of T. thermophilus IPMDH resulted in a cavity of 32 A3, but no significant effect on the activity and thermostability of the mutant was observed.

3-Isopropylmalate Dehydrogenase↗

PubMed1976

Unique properties of the camel erythrocyte membrane, II. Organization of membrane proteins.

Camel erythrocyte membranes are distinguished by some unique properties of stability and composition. Notable is their abundance in proteins (protein:lipid ratio of 3:1). Membrane proteins of camel erythrocytes were compared with those of human eruthrocytes, which have been intensively investigated. Proteins were extracted with various aqueous media (EDTA, alkaline or high ionic strength) and with ionic and non-ionic detergents and were analyzed by gel electrophoresis. In membranes of camel erythrocytes, the peripheral proteins constitute, proportionally, a much smaller fraction of total proteins than in the human erythrocyte, while their distribution is identical per unit of surface area. The camel erythrocyte membrane is particularly rich in integral proteins and in intramembranous particles. The proteins in this membrane are more closely organized than in the human system, as revealed by crosslinking and freeze-etching studies. It is proposed that protein-protein interaction of integral proteins, presumably constituting an "integral skeleton", is a dominant structural feature stabilizing the camel erythrocyte membrane.

Animals↗

PubMed2003

Thermotoga neapolitana adenylate kinase is highly active at 30 degrees C.

The adenylate kinase (AK) gene from Thermotoga neapolitana, a hyperthermophilic bacterium, was cloned and overexpressed in Escherichia coli, and the recombinant enzyme was biochemically characterized. The T. neapolitana AK (TNAK) sequence indicates that this enzyme belongs to the long bacterial AKs. TNAK contains the four cysteine residues that bind Zn(2+) in all Gram-positive AKs and in a few other Zn(2+)-containing bacterial AKs. Atomic emission spectroscopy and titration data indicate a content of 1 mol of Zn(2+)/mol of recombinant TNAK. The EDTA-treated enzyme has a melting temperature (T (m)=93.5 degrees C) 6.2 degrees C below that of the holoenzyme (99.7 degrees C), identifying Zn(2+) as a stabilizing feature in TNAK. TNAK is a monomeric enzyme with a molecular mass of approx. 25 kDa. TNAK displays V (max) and K (m) values at 30 degrees C identical with those of the E. coli AK at 30 degrees C, and displays very high activity at 80 degrees C, with a specific activity above 8000 units/mg. The unusually high activity of TNAK at 30 degrees C makes it an interesting model to test the role of enzyme flexibility in activity.

Adenylate Kinase↗

PubMed2004

Cloning and analysis of WF146 protease, a novel thermophilic subtilisin-like protease with four inserted surface loops.

Cloning and sequencing of the gene encoding WF146 protease, an extracellular subtilisin-like protease from the thermophile Bacillus sp. WF146, revealed that the WF146 protease was translated as a 416-amino acid precursor consisting of a putative 18-amino acid signal peptide, a 10-kDa N-terminal propeptide and a 32-kDa mature protease region. The mature WF146 protease shares a high degree of amino acid sequence identity with two psychrophilic subtilisins, S41 (68.2%) and S39 (65.4%), and a mesophilic subtilisin, SSII (67.1%). Significantly, these closely related proteases adapted to different temperatures all had four inserted surface loops not found in other subtilisins. However, unlike those of S41, S39 and SSII, the inserted loops of the WF146 protease possessed stabilizing features, such as the introduction of Pro residues into the loop regions. Interestingly, the WF146 protease contained five of the seven mutations previously found in a hyperstable variant of subtilisin S41 obtained by directed evolution. The proform of WF146 protease (pro-WF146 protease) was overexpressed in Escherichia coli in an inactive soluble form. After heat treatment, the 42-kDa pro-WF146 protease converted to a 32-kDa active mature form by processing the N-terminal propeptide. The purified mature WF146 protease hydrolyzed casein with an optimum temperature of 85 degrees C, and lost activity with a half-life of 30 min at 80 degrees C in the presence of 10 mM CaCl2.

Amino Acid Sequence↗

PubMed2000

Anatomical basics, variations, and degenerative changes of the shoulder joint and shoulder girdle.

This paper summarizes the anatomical basics of the shoulder, their variations, and precise definitions, including differential diagnoses. It also describes the characteristic degenerative changes caused by aging. A typical variation (7-15%) is the os acromiale, which forms the triangular epiphysis of the scapular spine. This abnormality must be differentiated from a fracture of the acromion or a pseudarthrosis. Because ossification of the acromion is complete after age 25, the os acromiale should be diagnosed only after this age. The shape of the acromion is a further important feature. In a recent anatomical study, the following frequencies of the Bigliani-types of the acromial shape were anatomically determined - type 1 (flat), 10.2% and type 2 (curved), 89.8%. Type 3 (hooked) was not observed, which indicates that this type is probably a misinterpretation of the so-called acromial spur. Minor dehiscences and perforations in the infraspinate or supraspinate fossa should not be confused with malignant osteolyses. The scapula has three ligaments of its own, (1) the coracoacromial ligament and its osseous fixations form an osteofibrous arch above the shoulder joint, which plays a part in impingement syndrome; (2) the superior transverse scapular ligament or its ossified correlate arches the scapular incisure and can cause a typical compression syndrome of the suprascapular nerve; (3) the inferior transverse scapular ligament is of no great clinical importance. Two intraarticular structures (glenoid labrum and tendon of the long bicipital head) must be mentioned. The glenoid labrum consists of dense connective tissue and surrounds the margin of the glenoid cavity. Two areas exhibit specialized conditions, cranial at the supraglenoid tubercle an intimate relationship exists to the tendon of the long bicipital head and in about 55% of cases, the labrum is stretched over the glenoid rim at the ventral side. At the area of the biceps-tendon-labrum complex, so-called SLAP-lesions may occur and at the glenoid rim, where the labrum is often not fixed to the bony margin, avulsions of the labrum may occur. This well-established anatomical condition must not be mistaken for a manifest Bankart-lesion. The glenohumeral ligaments, which are located in the ventral articular capsule, have a stabilizing function for the ventral part of the glenoid labrum. The glenohumeral ligaments lift the articular lip where it crosses the glenoid notch. This 'labrum-lift effect' supports the stabilizing features of the articular lip and the glenohumeral ligaments. The rotator cuff is composed of the tendons of the teres minor, infraspinatus, supraspinatus, and subscapularis muscles. This cuff has a poorly vascularized area, due to mechanical conditions, about 1.5 cm from the major tubercle, which causes degenerative changes and eventually may lead to ruptures. Results of the impingement-syndrome and the osteoarthrotic changes of the shoulder and acromioclavicular joint are also presented and discussed. Finally, the coracoclavicular joint, which probably represents no congenital entity but appears due to a changed, lowered position of the shoulder girdle, is discussed. The paper also presents instructive figures of anatomical preparations that can be used to make more precise radiological and differential diagnoses. All preparations were done by the author and are part of a series of more than 300 preparations of the shoulder joint and girdle.

Acromion↗

PubMed2005

The Orbitrap: a new mass spectrometer.

Research areas such as proteomics and metabolomics are driving the demand for mass spectrometers that have high performance but modest power requirements, size, and cost. This paper describes such an instrument, the Orbitrap, based on a new type of mass analyzer invented by Makarov. The Orbitrap operates by radially trapping ions about a central spindle electrode. An outer barrel-like electrode is coaxial with the inner spindlelike electrode and mass/charge values are measured from the frequency of harmonic ion oscillations, along the axis of the electric field, undergone by the orbitally trapped ions. This axial frequency is independent of the energy and spatial spread of the ions. Ion frequencies are measured non-destructively by acquisition of time-domain image current transients, with subsequent fast Fourier transforms (FFTs) being used to obtain the mass spectra. In addition to describing the Orbitrap mass analyzer, this paper also describes a complete Orbitrap-based mass spectrometer, equipped with an electrospray ionization source (ESI). Ions are transferred from the ESI source through three stages of differential pumping using RF guide quadrupoles. The third quadrupole, pressurized to less than 10(-3) Torr with collision gas, acts as an ion accumulator; ion/neutral collisions slow the ions and cause them to pool in an axial potential well at the end of the quadrupole. Ion bunches are injected from this pool into the Orbitrap analyzer for mass analysis. The ion injection process is described in a simplified way, including a description of electrodynamic squeezing, field compensation for the effects of the ion injection slit, and criteria for orbital stability. Features of the Orbitrap at its present stage of development include high mass resolution (up to 150,000), large space charge capacity, high mass accuracy (2-5 ppm), a mass/charge range of at least 6000, and dynamic range greater than 10(3). Applications based on electrospray ionization are described, including characterization of transition-metal complexes, oligosaccharides, peptides, and proteins. Use is also made of the high-resolution capabilities of the Orbitrap to confirm the presence of metaclusters of serine octamers in ESI mass spectra and to perform H/D exchange experiments on these ions in the storage quadrupole.

Alcohol Dehydrogenase↗

PubMed2000

Controlling the motion of total knee replacements using intercondylar guide surfaces.

Total knee replacements using intercondylar cams, such as posterior stabilized types, have been in use for many years. In a previous study, software was written to analyze an alternative shape of the intercondylar cams. The goal of the current study was to investigate in a more general way the potential of intercondylar cams, or guide surfaces, for reproducing the anterior-posterior motion of the natural knee throughout the flexion range. Typical sagittal outlines for the femoral and tibial bearing surfaces were defined, and a parametrized shape for the femoral guide surface was defined to produce a wide range of shapes. Software was written in which the femoral component was flexed in increments, with the posterior translation defined as a function of the flexion angle. The shape of the tibial guide surface was derived from the locus of the femoral guide surface at its multiple flexion positions. By iterating methodically through possible shapes of femoral guide surfaces, several types of total knee replacement components in common use today were identified, as well as other configurations of potential interest. For quantification of a given design, the software calculated the anterior and posterior laxity at each flexion angle. Laxity was defined as the motion before the femoral guide surface impacted the tibial guide surface or until the contact point of the bearing surfaces reached a specified slope. Convex femoral and concave saddle-shaped tibial guide surfaces produced small laxities in both directions over most of the flexion range. A saddle design with small laxities in the first half of flexion, combined with a posterior stabilized feature, was an interesting combination. Potential improvements to the currently used designs were shown in this study, and new shapes of intercondylar guide surfaces were derived that could be considered for application.

Arthroplasty, Replacement, Knee↗

PubMed1995

An equilibrium partially folded state of human lysozyme at low pH.

Temperature-induced unfolding of human lysozyme has been monitored by circular dichroism and by nuclear magnetic resonance experiments at a variety of low pH values. The results indicate that, although at pH values above 3 unfolding appears to be consistent with a two-state model, at lower pH values this is not the case. At pH 1.2, for example, unfolding of the tertiary structure occurs at a temperature approximately 10 deg. C lower than that of the secondary structure. At 60 degrees C there is no detectable native tertiary structure remaining for human lysozyme at pH 1.2, although far-UV CD results show preservation of some 40% of the signal attributable to alpha-helical elements in the protein. This indicates the existence of a partially folded state of human lysozyme at low pH that has at least some characteristics of the well-defined molten globule state of the homologous alpha-lactalbumins and of the kinetic intermediates observed in the folding of alpha-lactalbumins and of c-type lysozymes. These results suggest that the absolute distinction between these two groups of proteins in terms of their different unfolding behaviour is not valid, and provide insights into possible features stabilizing such states.

Animals↗

PubMed1996

In vivo repair of 3'-end deletions in a TCV satellite RNA may involve two abortive synthesis and priming events.

RNA viruses that do not have the stabilizing features of poly(A) tails or amino acids covalently linked to their 3' ends must develop other means for protecting or repairing their genomes from damage caused by cellular RNases. We previously found that deletions in the single-stranded tails of a satellite RNA (sat-RNA D) associated with turnip crinkle virus are repaired in vivo (C. D. Carpenter and A. E. Simon, 1996, J. Virol. 70, 478-486). We now extend this analysis to show that sat-RNA D transcripts with 3'-end deletions of 5 bases give rise to wild-type sat-RNA, while deletions of 6 to 11 bases result in sat-RNA with additional deletions to the -14 position joined to internal TCV genomic RNA (or other) sequence followed by replacement of the terminal C1-2UGC1-3 motif. In addition, we have determined that the selection of internal TCV sequence used in the repair of sat-RNA D 3' ends is not random and generation of these short TCV segments likely involves primer-mediated synthesis of abortive products facilitated by base-pairing between internal regions of TCV genomic RNA and oligoribonucleotides generated by abortive cycling from the 3' end of the TCV genome.

Carmovirus↗

PubMed1989

Activation of the lac promoter and its variants. Synergistic effects of catabolite activator protein and supercoiling in vitro.

Escherichia coli lac promoter variants are shown to be subject to large synergistic transcriptional activation by catabolite activator protein (CRP) and DNA supercoiling in vitro. Activation was studied for the lac wild-type promoter, a promoter with a variant spacing (lac delta l) and two promoters with variant -10 regions (lac ps, lac UV5). The variant promoters respond to the simultaneous presence of CRP and supercoiling by exhibiting large multiplicative activation at the low to moderate superhelicities that are most pertinent in vivo. Although all four promoters can be activated by CRP, those made stronger by changing downstream promoter elements are less CRP-activated even though each contains an identical CRP binding site. When each of the variant promoters is made stronger by introducing DNA supercoils, the apparent CRP activation initially remains constant but eventually declines at higher superhelicities. Thus, strengthening the lac promoter through either DNA sequence changes or the introduction of high-level DNA supercoiling can lead to diminished potential for activation by CRP. These results are interpreted in terms of a role for CRP in providing extra stabilizing contacts for RNA polymerase binding that are necessary only when other stabilizing features of promoter structure are lacking.

Bacterial Proteins↗

PubMed2004

Effectiveness of inpatient dialectical behavioral therapy for borderline personality disorder: a controlled trial.

Dialectical Behavioral Therapy (DBT) was initially developed and evaluated as an outpatient treatment program for chronically suicidal individuals meeting criteria for borderline personality disorder (BPD). Within the last few years, several adaptations to specific settings have been developed. This study aims to evaluate a three-month DBT inpatient treatment program. Clinical outcomes, including changes on measures of psychopathology and frequency of self-mutilating acts, were assessed for 50 female patients meeting criteria for BPD. Thirty-one patients had participated in a DBT inpatient program, and 19 patients had been placed on a waiting list and received treatment as usual in the community. Post-testing was conducted four months after the initial assessment (i.e. four weeks after discharge for the DBT group). Pre-post-comparison showed significant changes for the DBT group on 10 of 11 psychopathological variables and significant reductions in self-injurious behavior. The waiting list group did not show any significant changes at the four-months point. The DBT group improved significantly more than participants on the waiting list on seven of the nine variables analyzed, including depression, anxiety, interpersonal functioning, social adjustment, global psychopathology and self-mutilation. Analyses based on Jacobson's criteria for clinically relevant change indicated that 42% of those receiving DBT had clinically recovered on a general measure of psychopathology. The data suggest that three months of inpatient DBT treatment is significantly superior to non-specific outpatient treatment. Within a relatively short time frame, improvement was found across a broad range of psychopathological features. Stability of the recovery after one month following discharge, however, was not evaluated and requires further study.

Adolescent↗

PubMed2003

Coordination and stability of one-legged hopping patterns in patients with anterior cruciate ligament reconstruction: preliminary results.

OBJECTIVES: To investigate whether the intralimb coordination of the lower extremity during one-legged hopping in patients with anterior cruciate ligament reconstruction is different and less stable compared to control subjects. DESIGN: Measures of coordination dynamics are applied to study the coordination and stability of movement patterns of the knee and ankle in patients and control subjects. BACKGROUND: Due to several factors, such as loss of proprioceptive function and muscle weakness, the intralimb coordination of the lower extremity might be altered. METHODS: Seven patients and 13 healthy control subjects were instructed to hop in place on one leg for 10 seconds at a comfortable frequency for each leg separately. RESULTS AND CONCLUSIONS: The one-legged hopping movement pattern of patients with anterior cruciate ligament reconstruction one-year post-operative is different and less stable compared to healthy subjects, and thus is still impaired. RELEVANCE: This paper shows that patients, one year after reconstruction of the anterior cruciate ligament, have a different coordination pattern of the lower limb compared to a matched control group. Intersegmental coordination and stability, features that are often observed by eye during a rehabilitation process, are objectified in this study.

Adolescent↗

PubMed1975

[Detection of HBs with latex tests].

Since 1971, several inert particles have been tested and proposed for HBs antigen screening, none of them being really used in routine. An evaluation is realized and presented, pointing out the main characteristics and the practical problems. We report our experience on two types of latex, simultaneously conducted through manual techniques and through Groupamatic 360 equipments. For one of them, TG Antigex, sensitivity and specificity are very satisfying and several batches are presently tested in order to quantify the reproducibility and stability features of the reagent.

Blood Specimen Collection↗

PubMed1995

The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures.

BACKGROUND: The hyperthermophile Pyrococcus furiosus is one of the most thermostable organisms known, with an optimum growth temperature of 100 degrees C. The proteins from this organism display extreme thermostability. We have undertaken the structure determination of glutamate dehydrogenase from P. furiosus in order to gain further insights into the relationship between molecular structure and thermal stability. RESULTS: The structure of P. furiosus glutamate dehydrogenase, a homohexameric enzyme, has been determined at 2.2 A resolution and compared with the structure of glutamate dehydrogenase from the mesophile Clostridium symbiosum. CONCLUSIONS: Comparison of the structures of these two enzymes has revealed one major difference: the structure of the hyperthermophilic enzyme contains a striking series of ion-pair networks on the surface of the protein subunits and buried at both interdomain and intersubunit interfaces. We propose that the formation of such extended networks may represent a major stabilizing feature associated with the adaptation of enzymes to extreme temperatures.

Amino Acid Sequence↗

PubMed1998

Insights into tyrosine phosphorylation control of protein-protein association from the NMR structure of a band 3 peptide inhibitor bound to glyceraldehyde-3-phosphate dehydrogenase.

A protein-protein association regulated by phosphorylation of tyrosine is examined by NMR structural studies and biochemical studies. Binding of glyceraldehyde-3-phosphate dehydrogenase (G3PDH) and aldolase to the N-terminus of human erythrocyte anion transporter, band 3, inhibits enzyme activity. This inhibition is reversed upon phosphorylation of band 3 Y8, as shown by kinetic studies on purified components, as well as in vivo studies. Thus, tyrosine phosphorylation mediates against the intermolecular protein-protein association, in contrast to the positive control involving SH2 and PTB domains where phosphorylation is required for binding. To elucidate the basis of recognition and negative control by tyrosine phosphorylation, the structure of a synthetic peptide, B3P, corresponding to the first 15 residues of band 3 (MEELQDDYEDMMEEN-NH2), bound to G3PDH has been determined using the exchange-transferred nuclear Overhauser effect. The G3PDH-bound B3P structure was found to be very similar to the structure recognized by aldolase. A hydrophobic triad forms from side chains within a loop structure of residues 4 through 9 in both bound species. Another structural feature stabilizing the loop, in the case of the B3P-G3PDH complex, is a hydrogen bond between the side chains of Y8 and D10 associated with a beta-turn of residues 8-11. Based on the structure of this phosphorylation sensitive interaction (PSI) loop, it is suggested that tyrosine phosphorylation disrupts protein-protein association, in part, by intramolecular electrostatic destabilization. The inhibition by B3P is competitive with respect to the coenzyme NAD+ and noncompetitive with the substrate analog arsenate. Specific binding of B3P to G3PDH is demonstrated by reversion of the NMR spectral properties of bound B3P to those of the free peptide upon addition of coenzyme and substrate analog. The stoichiometry of binding for the B3P-G3PDH complex was determined from Sephadex G-50 displacement experiments to be 4:1. Collectively, these results are consistent with B3P binding the active site of G3PDH.

Amino Acid Sequence↗

PubMed2005

Variable-temperature X-ray crystallographic and DFT computational study of the N-H...O/N...H-O tautomeric competition in 1-(Arylazo)-2-naphthols. Outline of a transition-state hydrogen-bond theory.

Phenyl-substituted 1-arylazo-2-naphthols (AAN) display ...HN-N=C-C=O... <==>...N=N-C=C-OH... ketohydrazone-azoenol tautomerism and can form intramolecular resonance-assisted H-bonds from pure N-H...O to pure N...H-O through tautomeric and dynamically disordered N-H...O <==>N...H-O bonds according to the electronic properties of their substituents. Three compounds of this series (m-OCH(3)-AAN = mOM; p-Cl-AAN = pCl; and p-NMe(2)-AAN = pNM2) have been studied by X-ray crystallography at four temperatures (100-295 K), showing that the remarkably short H-bonds formed (2.53 < or = d(N...O) < or = 2.55 A) are a pure N-H...O in mOM, a dynamically disordered mixture in pCl (N-H...O:N...H-O = 69:31 at 100 K), and a statically disordered mixture in pNM2 (N-H...O:N...H-O = 21:79 at 100 K). These compounds, integrated by the p-H-, p-NO(2)-, p-F-, and p-O(-)-substituted derivatives, have been emulated by DFT methods (B3LYP/6-31+G(d,p) level) with full geometry optimization of the stationary points along the proton-transfer (PT) pathway: N-H...O and N...H-O ground states and N...H...O transition state. Analysis of DFT-calculated energies and geometries by the methods of the rate-equilibrium Marcus theory shows that all H-bond features (stability and tautomerism, as well as position and height of the PT barrier) can be coherently interpreted in the frame of the transition-state (or activated-complex) theory by considering the bond as a chemical reaction N-H...O <==> N...H...O <==> N...H-O which is bimolecular in both directions and proceeds via the N...H...O PT transition state (the activated complex).

Journal Article↗

PubMed2005

Alpha,omega-distyryl oligothiophenes: high mobility semiconductors for environmentally stable organic thin film transistors.

Critical to the development of organic electronics is the design and synthesis of new organic semiconductors with improved electrical performance and enhanced environmental stability. We present in this communication the synthesis of a series of simple oligothiophene derivatives that bear the styryl unit as terminal substituent. Thin film field-effect transistors incorporating these compounds show high electrical performance, such as mobilities as high as 0.1 cm2/Vs, along with exceptional stability under ambient conditions. Especially, the longer oligomer, DS-4T, containing the quaterthiophene core gives rise to devices that show no decrease in performance after more than 17 months of storage and under continuous operation. Such stability features are unprecedented in the oligothiophene series.

Journal Article↗