No description available.

No description available.

Polyhedral oligomeric silsesquioxanes (POSS) have attracted substantial academic interest for many years as hybrid materials and nanofillers for controlling thermal and mechanical properties, and providing thermal and chemical resistance while retaining ease of processing. A natural extension of these studies has been POSS-based amphiphiles and thin film coatings. Studies at the air/water (A/W) interface have shown that trisilanol-POSS derivatives are amphiphilic and form uniform Langmuir films, whereas closed-cage POSS derivatives are hydrophobic and aggregate. In previous work, a triester (POSS-triester) and a triacid (POSS-triacid) were synthesized from PSS-(3-hydroxypropyl)-heptaisobutyl (POSS-OH) and Weisocyanate and fully characterized by surface pressure – area per molecule (Π-A) isotherm and Brewster angle microscopy (BAM) studies at the A/W interface. The results indicated that POSS-triester is surface active forming a liquid expanded (LE) monolayer, whereas POSS-triacid forms a liquid condensed (LC) monolayer that is only weakly affected by pH. A face-on conformation was proposed and examined to understand the packing of POSS-based amphiphilic molecules at the A/W interface. The face-on/vertex-on comparison is rarely discussed for Langmuir monolayers at the A/W interface. In this thesis, three other POSS-based esters were synthesized from POSS-OH and aminopropylisobutyl-POSS (POSS-NH₂) using Weisocyanate and a similar isocyanate containing two tert-butyl protected carboxylic acids. The synthesized materials are characterized by Π-A isotherm and BAM. For POSS-OH based diester (PAlDE) and POSS-NH2 based diester (PAmDE), LE/LC phase transitions were observed in Π-A isotherms over part of the experimentally accessible temperature range and were attributed to a change from a vertex-on to face-on conformation. Apparent BAM images confirmed LC islands coexisted with the LE phase. The experimentally observed dynamic estimates of the critical temperatures (Tc) were estimated from a two-dimensional Clausius-Clapeyron analysis and were consistent with the temperature dependence of the Π-A isotherms. These LE/LC phase transitions are the first observed for POSS amphiphiles. / Ph. D.

Polyhedral oligomeric silsesquioxanes (POSS) have attracted substantial academic interest for many years as hybrid materials and nanofillers for controlling thermal and mechanical properties, and for providing thermal and chemical resistance while retaining ease of processing. A natural extension of these studies has been working on POSS-based amphiphiles and thin film coatings. Studies at the air/water (A/W) interface have shown that trisilanol-POSS derivatives are amphiphilic and form uniform Langmuir films, whereas closed-cage POSS derivatives are hydrophobic and aggregate. In this study, two novel POSS derivatives were synthesized from PSS-(3-hydroxypropyl)-heptaisobutyl substituted (POSS-OH) and completely characterized. Weisocyanate reacted with POSS-OH, and a POSS-based triester (POSS-triester) was obtained. Trifluoroacidolysis of the POSS-triester at room temperature afforded the corresponding triacid (POSS-triacid). Purified POSS-OH, POSS-triester, and POSS-triacid were studied by using surface pressure - area per molecule (? -A) isotherms as well as Brewster angle microscopy (BAM) at the air/water (A/W) interface. Compared with previous work on trisilanol-POSS derivatives, the results indicated that POSS-triester was surface active and formed a liquid-expanded (LE) monolayer. In contrast, POSS-triacid monolayers were more condensed (LC) and were not dramatically affected by changes in pH. Results for the lift-off areas (Alift-off), limiting areas (A0), collapse areas (Ac), and collapse pressures (? c) of POSS-OH, POSS-triester, and POSS-triacid were compared to trisilanolisobutyl-POSS (TiBP) and were interpreted in terms of possible molecular conformations. Whereas, TiBP has been hypothesized to exist in a vertex-on conformation, POSS-OH and POSS-triacid packing at the A/W interface was consistent with face-on conformations. For POSS-triester, the isotherm was consistent with a vertex-on conformation at low ? , but a face-on conformation at high ? . / Master of Science

Surface behavior of poly (epsilon-caprolactone) (PCL) have been studied at the air/water interface (A/W). PCL is a hydrophobic and crystalline polyester with a glass transition temperature around -60 degrees centigrade, a melting point around 55 degrees centigrade, excellent biocompatibility, and low toxicity. In the past decade, PCL based systems have attracted considerable interest for controlled-release drug delivery and as scaffolds for tissue engineering, that require a fundamental understanding of PCL's degradation mechanisms and crystallization properties. PCL spherulites were commonly observed in previous bulk studies. This thesis focuses on PCL crystallization in Langmuir monolayers. Brewster angle microscopy (BAM) studies show that square, distorted rectangular, and dendritic crystals form at the A/W interface. While dendritic structures have been observed in poly (ethylene oxide) (PEO) thin film on solid substrates, this study of PCL is the first time that dendritic morphologies have been observed at the A/W interface for a linear flexible-coil polymer. As far as we know, the crystallization of flexible-coil polymers at the A/W interface is a brand new area of research. These findings may provide an interesting model system for studying crystallization in confined geometries and the effect of crystallinity on enzyme catalyzed hydrolysis of this important biodegradable polymer at the A/W interface. The main objectives of this thesis were to investigate the phase behavior of PCL at the A/W interface, gain a deeper understanding of the nucleation and growth mechanism of PCL crystallization at the A/W interface through surface pressure-area isotherms and isobaric area relaxation analyses, and interpret the effects of molecular weight on the nucleation and growth mechanism, and morphologies of semicrystalline PCL crystallized in Langmuir monolayers at the A/W interface. / Master of Science

Ce travail a porté sur l'étude des propriétés des monocouches de copolymères diblocs neutres-chargés de poly(tert-butylstyrène)/poly(styrène sulfonate) à l'interface eau/air. Conformément aux modèles théoriques, l'étude des isothermes de compression des monocouches a permis de montrer que les chaînes chargées ancrées à l'interface ont une conformation de type brosse osmotique aux aires moléculaires étudiées. Nous montrons aussi l'importance du solvant d'étalement sur les isothermes de pression de surface et une restructuration de l'interface à forte compression qui apparaît sous la forme d'une relaxation de la pression de surface. Les observations de la monocouche par microscopie à l'angle de Brewster et diffusion de rayons X ont révélé l'existence d'une instabilité de flambage de l'interface. Lors de sa compression, l'interface se déforme et laisse apparaître des structures de grandes dimensions (5 à 35 micromètres), aisément observables malgré leur faible amplitude (quelques nanomètres). Nous avons montré que l'apparition du flambage résulte d'un échange de molécules entre l'interface et la sous-phase. Nous avons proposé différents mécanismes de déformation de la monocouche qui permettent de rendre compte qualitativement des différentes caractéristiques du flambage comme la dépendance de la taille des structures avec l'épaisseur de la monocouche, la dépendance de la pression d'apparition des structures avec la concentration en copolymère dans la sous-phase et l'insensibilité au sel. L'impossibilité de mesurer directement l'amplitude des structures à l'interface nous a conduit à développer une nouvelle méthode d'observation des monocouches à l'interface eau/air au moyen d'un microscope à force atomique. Les résultats obtenus sur différentes couches à l'interface eau/air montrent ainsi toutes les potentialités de cette nouvelle technique dans l'observation de monocouches présentant des domaines de taille inférieure à 100 nm.

No description available.

No description available.

A investigação dos mecanismos de interação dos vírus com as células do hospedeiro trazem informações relevantes para a identificação de alvos no desenvolvimento de drogas para impedir a penetração e/ou desenvolvimento dos vírus. Peptídeos desenhados a partir de proteínas virais foram desenvolvidos e testados quanto as suas capacidades de inibir o processo de fusão do vírus com a célula do hospedeiro. Alguns se encontram em fase de avaliação clínica. Anticorpos contra a proteína p24 do HIV-1 foram detectados no soro de pacientes HIV-positivos, e estes reconhecem pequenas seqüências peptídicas desta proteína. Neste trabalho foi analisada a interação entre uma seqüência peptídica correspondente aos aminoácidos 196-224 (AAMQMLKETINEEAAEWDRVHPVHAGPIA) da proteína p24, denominado p24- 1, com sistemas biomiméticos. Os sistemas utilizados foram filmes de Langmuir (monocamadas) de dipalmitoil fosfatidil colina (DPPC) e dipalmitoil fosfatidil glicerol (DPPG) e vesículas multilamelares (MLVs) de DPPC. O p24-1 encontra-se desorganizado em solução aquosa, mas com a interação com as MLVs de DPPC teve induzido uma conformação hélice ?, de acordo com o espectro de dicroísmo circular (CD). Esta característica foi confirmada pela predição de hélice a seguida por uma estrutura não ordenada contendo 11 resíduos do p24-1. As isotermas de pressão e potencial de superfície das monocamadas de DPPC foram afetadas com a presença de 0,05% mo1 de p24-1, com uma expansão de aproximadamente 5%. Para concentrações acima de 0,5% mo1 de p24-1 a expansão foi de 20%, com saturação do efeito da concentração. O efeito de expansão foi acompanhado por uma alteração na morfologia das monocamadas, estudados com microscopia no ângulo de Brewster (BAM). A incorporação do p24-1 impede a formação de grandes domínios de DPPC. O efeito cooperativo causado na monocamada de fosfolipídios pelo p24-1 sugere que esse tem um potencial na atividade antiviral por participar da expansão da membrana da célula hospedeira. / The investigation of the interaction mechanisms between the viruses and the host cells brings relevant information for the identification of targets on the development of drugs to prevent the penetration and/or development of the viruses. Peptides designed from viral proteins have been developed and tested on its capacities of inhibiting the merging process of the virus with the host cell. Some of them are in clinical evaluation. Antibodies against the protein p24 of the HIV-1 have been detected in the serum of HIV-positive patients, and they are able to recognize short peptide sequences of this protein. In this work, it was analyzed the interaction between a peptide sequence corresponding to amino acids 196-224 (AAMQMLKETINEEAAEWDRVHPVHAGPIA) of the protein p24, called p24- 1, and biomimetic systems. The systems used were Langmuir films (monolayers) of dipalmitoyl phosphatidyl choline (DPPC) and dipalmitoyl phosphatidyl glycerol (DPPG) and multilamelar vesicles (MLVs) of DPPC. p24-1 is found disorganized in watery solution, but with the interaction with the MLVs of DPPC it had induced a conformation ?-helix, according to the circular dichoism spectra (CD). This characteristic was confirmed by the prediction of ?-helix followed by an unordered structure with 11 residues of p24-1. The isotherms of pressure and potential of surface of the DPPC monolayers were affected by the presence of 0,05% mo1 of p24-1, with an expansion of approximately 5%. For concentrations above 0,5% mol of p24-1 the expansion was 20%, with saturation of the concentration effect. The expansion effect was followed by a morphologic alteration of the monolayers, studied with microscopy of the Brewster angle (BAM). The incorporation of p24-1 prevents the formation of large domains of DPPC. The cooperative effect caused in the phospholipid monolayer by p24-1 suggests that this peptide has a potential in the antiviral activity, once its participates on the expansion of the host cell membrane.

A investigação dos mecanismos de interação dos vírus com as células do hospedeiro trazem informações relevantes para a identificação de alvos no desenvolvimento de drogas para impedir a penetração e/ou desenvolvimento dos vírus. Peptídeos desenhados a partir de proteínas virais foram desenvolvidos e testados quanto as suas capacidades de inibir o processo de fusão do vírus com a célula do hospedeiro. Alguns se encontram em fase de avaliação clínica. Anticorpos contra a proteína p24 do HIV-1 foram detectados no soro de pacientes HIV-positivos, e estes reconhecem pequenas seqüências peptídicas desta proteína. Neste trabalho foi analisada a interação entre uma seqüência peptídica correspondente aos aminoácidos 196-224 (AAMQMLKETINEEAAEWDRVHPVHAGPIA) da proteína p24, denominado p24- 1, com sistemas biomiméticos. Os sistemas utilizados foram filmes de Langmuir (monocamadas) de dipalmitoil fosfatidil colina (DPPC) e dipalmitoil fosfatidil glicerol (DPPG) e vesículas multilamelares (MLVs) de DPPC. O p24-1 encontra-se desorganizado em solução aquosa, mas com a interação com as MLVs de DPPC teve induzido uma conformação hélice ?, de acordo com o espectro de dicroísmo circular (CD). Esta característica foi confirmada pela predição de hélice a seguida por uma estrutura não ordenada contendo 11 resíduos do p24-1. As isotermas de pressão e potencial de superfície das monocamadas de DPPC foram afetadas com a presença de 0,05% mo1 de p24-1, com uma expansão de aproximadamente 5%. Para concentrações acima de 0,5% mo1 de p24-1 a expansão foi de 20%, com saturação do efeito da concentração. O efeito de expansão foi acompanhado por uma alteração na morfologia das monocamadas, estudados com microscopia no ângulo de Brewster (BAM). A incorporação do p24-1 impede a formação de grandes domínios de DPPC. O efeito cooperativo causado na monocamada de fosfolipídios pelo p24-1 sugere que esse tem um potencial na atividade antiviral por participar da expansão da membrana da célula hospedeira. / The investigation of the interaction mechanisms between the viruses and the host cells brings relevant information for the identification of targets on the development of drugs to prevent the penetration and/or development of the viruses. Peptides designed from viral proteins have been developed and tested on its capacities of inhibiting the merging process of the virus with the host cell. Some of them are in clinical evaluation. Antibodies against the protein p24 of the HIV-1 have been detected in the serum of HIV-positive patients, and they are able to recognize short peptide sequences of this protein. In this work, it was analyzed the interaction between a peptide sequence corresponding to amino acids 196-224 (AAMQMLKETINEEAAEWDRVHPVHAGPIA) of the protein p24, called p24- 1, and biomimetic systems. The systems used were Langmuir films (monolayers) of dipalmitoyl phosphatidyl choline (DPPC) and dipalmitoyl phosphatidyl glycerol (DPPG) and multilamelar vesicles (MLVs) of DPPC. p24-1 is found disorganized in watery solution, but with the interaction with the MLVs of DPPC it had induced a conformation ?-helix, according to the circular dichoism spectra (CD). This characteristic was confirmed by the prediction of ?-helix followed by an unordered structure with 11 residues of p24-1. The isotherms of pressure and potential of surface of the DPPC monolayers were affected by the presence of 0,05% mo1 of p24-1, with an expansion of approximately 5%. For concentrations above 0,5% mol of p24-1 the expansion was 20%, with saturation of the concentration effect. The expansion effect was followed by a morphologic alteration of the monolayers, studied with microscopy of the Brewster angle (BAM). The incorporation of p24-1 prevents the formation of large domains of DPPC. The cooperative effect caused in the phospholipid monolayer by p24-1 suggests that this peptide has a potential in the antiviral activity, once its participates on the expansion of the host cell membrane.