Bibliografias temáticas / Carbamylation of the collagen triple helix

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Literatura científica selecionada sobre o tema "Carbamylation of the collagen triple helix"

Autor: Grafiati

Publicado: 29 de março de 2025

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Artigos de revistas sobre o assunto "Carbamylation of the collagen triple helix"

Brodsky, Barbara, e John A. M. Ramshaw. "The collagen triple-helix structure". Matrix Biology 15, n.º 8-9 (março de 1997): 545–54. http://dx.doi.org/10.1016/s0945-053x(97)90030-5.

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Newberry, Robert W., Brett VanVeller e Ronald T. Raines. "Thioamides in the collagen triple helix". Chemical Communications 51, n.º 47 (2015): 9624–27. http://dx.doi.org/10.1039/c5cc02685g.

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Liu, Fei, Zhe Yu, Beibei Wang e Bor-Sen Chiou. "Changes in Structures and Properties of Collagen Fibers during Collagen Casing Film Manufacturing". Foods 12, n.º 9 (29 de abril de 2023): 1847. http://dx.doi.org/10.3390/foods12091847.

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Collagen casing is an edible film, which is widely used in the industrial production of sausages. However, the detailed changes in the collagen fibers, from the raw material to the final collagen film, have rarely been reported. In this research, the changes in the collagen fibers during the manufacturing process, including the fiber arrangement, the triple-helix structure and the thermal stability, were investigated using scanning electron microscopy (SEM), thermogravimetric analysis (TGA), X-ray diffraction (XRD), differential scanning calorimetry (DSC) and Fourier-transform infrared (FTIR) spectroscopy. The relationship between the structure stability and the arrangement of the collagen fibers was also discussed. According to the SEM, XRD, TGA, DSC and FTIR results, the collagen fibers were depolymerized during the acid swelling and became uniformly aligned after the homogenization process. Degassing had no obvious effect on the triple-helix structure. Alkaline neutralization with ammonia destroyed the triple-helix structure, which could be partly reversed through the washing and soaking processes. During the final drying step, the depolymerized triple helix of the collagen fibers recombined to form new structures that showed decreased thermal stability. This study expands our knowledge about the behavior of collagen fibers during the industrial process of producing collagen biobased casings.

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Sato, Daisuke, Hitomi Goto, Yui Ishizaki, Tetsuya Narimatsu e Tamaki Kato. "Design, Synthesis, and Photo-Responsive Properties of a Collagen Model Peptide Bearing an Azobenzene". Organics 3, n.º 4 (11 de outubro de 2022): 415–29. http://dx.doi.org/10.3390/org3040027.

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Collagen is a vital component of the extracellular matrix in animals. Collagen forms a characteristic triple helical structure and plays a key role in supporting connective tissues and cell adhesion. The ability to control the collagen triple helix structure is useful for medical and conformational studies because the physicochemical properties of the collagen rely on its conformation. Although some photo-controllable collagen model peptides (CMPs) have been reported, satisfactory photo-control has not yet been achieved. To achieve this objective, detailed investigation of the isomerization behavior of the azobenzene moiety in CMPs is required. Herein, two CMPs were attached via an azobenzene linker to control collagen triple helix formation by light irradiation. Azo-(PPG)10 with two (Pro-Pro-Gly)10 CMPs linked via a photo-responsive azobenzene moiety was designed and synthesized. Conformational changes were evaluated by circular dichroism and the cis-to-trans isomerization rate calculated from the absorption of the azobenzene moiety indicated that the collagen triple helix structure was partially disrupted by isomerization of the internal azobenzene.

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Fujii, Kazunori K., Yuki Taga, Yusuke K. Takagi, Ryo Masuda, Shunji Hattori e Takaki Koide. "The Thermal Stability of the Collagen Triple Helix Is Tuned According to the Environmental Temperature". International Journal of Molecular Sciences 23, n.º 4 (12 de fevereiro de 2022): 2040. http://dx.doi.org/10.3390/ijms23042040.

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Triple helix formation of procollagen occurs in the endoplasmic reticulum (ER) where the single-stranded α-chains of procollagen undergo extensive post-translational modifications. The modifications include prolyl 4- and 3-hydroxylations, lysyl hydroxylation, and following glycosylations. The modifications, especially prolyl 4-hydroxylation, enhance the thermal stability of the procollagen triple helix. Procollagen molecules are transported to the Golgi and secreted from the cell, after the triple helix is formed in the ER. In this study, we investigated the relationship between the thermal stability of the collagen triple helix and environmental temperature. We analyzed the number of collagen post-translational modifications and thermal melting temperature and α-chain composition of secreted type I collagen in zebrafish embryonic fibroblasts (ZF4) cultured at various temperatures (18, 23, 28, and 33 °C). The results revealed that thermal stability and other properties of collagen were almost constant when ZF4 cells were cultured below 28 °C. By contrast, at a higher temperature (33 °C), an increase in the number of post-translational modifications and a change in α-chain composition of type I collagen were observed; hence, the collagen acquired higher thermal stability. The results indicate that the thermal stability of collagen could be autonomously tuned according to the environmental temperature in poikilotherms.

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Boryskina, O. P., T. V. Bolbukh, M. A. Semenov e V. Ya Maleev. "Physical factors of collagen triple helix stability". Biopolymers and Cell 22, n.º 6 (20 de novembro de 2006): 458–67. http://dx.doi.org/10.7124/bc.00074d.

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Horng, Jia-Cherng, Andrew J. Hawk, Qian Zhao, Eric S. Benedict, Steven D. Burke e Ronald T. Raines. "Macrocyclic Scaffold for the Collagen Triple Helix". Organic Letters 8, n.º 21 (outubro de 2006): 4735–38. http://dx.doi.org/10.1021/ol061771w.

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Mizuno, Kazunori, Toshihiko Hayashi, David H. Peyton e Hans Peter Bächinger. "Hydroxylation-induced Stabilization of the Collagen Triple Helix". Journal of Biological Chemistry 279, n.º 36 (1 de julho de 2004): 38072–78. http://dx.doi.org/10.1074/jbc.m402953200.

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Persikov, Anton V., John A. M. Ramshaw, Alan Kirkpatrick e Barbara Brodsky. "Amino Acid Propensities for the Collagen Triple-Helix†". Biochemistry 39, n.º 48 (dezembro de 2000): 14960–67. http://dx.doi.org/10.1021/bi001560d.

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Mizuno, Kazunori, Toshihiko Hayashi e Hans Peter Bächinger. "Hydroxylation-induced Stabilization of the Collagen Triple Helix". Journal of Biological Chemistry 278, n.º 34 (13 de junho de 2003): 32373–79. http://dx.doi.org/10.1074/jbc.m304741200.

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Mais fontes

Teses / dissertações sobre o assunto "Carbamylation of the collagen triple helix"

Msoili, Zara. "DYNAMYC : DécrYptage Numérique de processus de vieillissement biologique : Application à la carbaMYlation de la triple hélice des Collagènes". Electronic Thesis or Diss., Reims, 2024. http://www.theses.fr/2024REIMS048.

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La population mondiale vieillit de plus en plus ; ainsi les problématiques de compréhension des mécanismes du vieillissement sont devenus une priorité pour l’OMS.La matrice extracellulaire (MEC) joue un rôle clé encore peu connu dans le vieillissement, et ce en raison de son architecture 3D complexe et de sa composition qui inclut des protéines de grandes tailles tels les collagènes. Ces derniers sont des composants clés de l'intégrité, de la structure et des propriétés physico-chimiques de la MEC puisqu’ils forment des assemblages supramoléculaires qui contribuent à l’architecture des tissus. Au cours du vieillissement, La MEC subit un processus de remodelage via diverses modifications post-traductionnelles (MPTs) dont certaines contribuent à sa fonction, mais d’autres en revanche peuvent affecter ses propriétés physique et mécanique. L'une des modifications observées au sein des collagènes est la carbamylation : une MPT non enzymatique, qui résulte de la fixation d’acide isocyanique, provenant principalement de la décomposition de l’urée, sur les groupements aminés des protéines. La fixation de l’acide isocyanique sur la lysine forme le composé homocitrulline (HCT). Des études expérimentales récentes de notre unité de recherche ont montré que l'accumulation de produits dérivés des carbamylations tels que HCT dans la peau pourrait altérer les propriétés du collagène et être corrélée au vieillissement cutané.Cette thèse propose d’étudier l’impact de la carbamylation sur le collagène de type I via des approches in silico de résolution dimensionnelle plus fine que les techniques expérimentales usuelles. La stratégie proposée est translationnelle et combine des résultats de mécanique quantique, de dynamique moléculaire (DM) tout atome ainsi que des représentations gros grain, voire mésoscopiques. Dans un premier temps, puisque dans le champ de forces AMBER (optimitisé pour décrire le collagène natif), il n'y a pas de paramètres disponibles permettant de décrire HCT, cette MPT a été paramétrée en utilisant la mécanique quantique. Ensuite, l’utilisation de la modélisation moléculaire classique, et plus particulièrement de simulations numériques de DM portant sur des tronçons de collagènes a permis de caractériser le comportement dynamique de la triple hélice carbamylée. La sélection de la région spécifique a été opéré sur la base de données expérimentales issues du laboratoire et quatre systèmes différents contenant de zéro à trois HCT ont été étudiés. Les trajectoires de DM ont été analysées afin d'évaluer l'impact de la/des modification(s) sur le squelette et la chaîne latérale de la triple hélice. La présence d'un à trois HCT, colocalisés dans la même région, a peu d'impact sur la structure globale du squelette (la structure de type polyproline-II est conservée) ; en revanche, une perturbation locale de la dynamique des hélices triples est observée. En effet, la caractérisation des angles dièdres de la chaîne latérale HCT met en évidence un changement de comportement de la torsion χ4 par rapport au résidu natif lysine. De plus, toujours au niveau local, la carbamylation modifie la nature des interactions puisque les ponts salins formés par et entre les lysines sont remplacés par des interactions faibles de type liaison hydrogène entre la chaîne latérale de HCT et le squelette protéique.Les résultats obtenus soulignent, au niveau atomique, l'impact local, et non global, de la carbamylation, et ce quel que soit le nombre de modifications considéré. Cependant, compte tenu des différentes échelles d’assemblage supramoléculaire du collagène de type I (fibrilles puis fibres), aborder l’étude de ce système par le biais de simulation gros grain (regroupement d’atomes non polaires sur une seule bille) ou encore mésoscopique est une voie d’étude qui semble nécessaire pour intégrer des effets synergiques le long de la triple hélice, voire de la fibrille, et que nous avons commencé à explorer
The world population is increasingly aging; thus, understanding the mechanisms of aging has become a priority for the WHO.The extracellular matrix (ECM) plays a crucial role in aging that is still little known due to its complex 3D architecture and composition, including large proteins such as collagens. The latter are critical components of the integrity, structure, and physicochemical properties of the ECM since they form supramolecular assemblies that contribute to tissue architecture. During aging, the ECM undergoes a remodeling process via various post-translational modifications (PTMs), some contribute to its function, but others can affect its physical and mechanical properties. One of the modifications observed in collagens is carbamoylation: a non-enzymatic PTM, which results from the fixation of isocyanic acid, mainly from the decomposition of urea, on the amino groups of proteins. The binding of isocyanic acid to lysine forms the compound homocitrulline (HCT). Recent experimental studies from our research unit have shown that the accumulation of carbamoylation derivatives such as HCT in the skin could alter collagen properties and be correlated with skin aging.This thesis proposes to study the impact of carbamoylation on type I collagen via in silico approaches with finer dimensional resolution than usual experimental techniques. The proposed strategy is translational and combines results from quantum mechanics, all-atom molecular dynamics (MD), and coarse-grained or even mesoscopic representations. First, since in the AMBER force field (optimized to describe native collagen), there are no parameters available to describe HCT, this MPT was parameterized using quantum mechanics. Then, the use of classical molecular modeling, and more particularly of numerical simulations of MD on collagen sections, allowed us to characterize the dynamic behavior of the carbamoylated triple helix. The specific region was selected based on experimental data from the laboratory, and four different systems containing from zero to three HCTs were studied. The MD trajectories were analyzed to evaluate the impact of the modification(s) on the backbone and the side chain of the triple helix. The presence of one to three HCTs, colocalized in the same region, has little impact on the overall structure of the backbone (the polyproline-II type structure is preserved); on the other hand, a local perturbation of the dynamics of the triple helices is observed. Indeed, the characterization of the dihedral angles of the HCT side chain highlights a change in the behavior of the χ4 torsion compared to the native lysine residue. Furthermore, still at the local level, carbamoylation modifies the nature of the interactions since the salt bridges formed by and between the lysines are replaced by weak hydrogen bond interactions between the HCT side chain and the protein backbone.The results highlight, at the atomic level, the local, and not global, impact of carbamoylation, regardless of the number of modifications considered. However, given the different scales of supramolecular assembly of type I collagen (fibrils then fibers), approaching the study of this system through coarse-grained simulation (grouping of non-polar atoms on a single bead) or even mesoscopic is a study path that seems necessary to integrate synergistic effects along the triple helix, or even the fibril, and that we have begun to explore

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鄭隆峰 e Lung-fung Cheng. "Modelling and sequence analysis of the collagen triple helix". Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2001. http://hub.hku.hk/bib/B31969914.

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Cheng, Lung-fung. "Modelling and sequence analysis of the collagen triple helix". Hong Kong : University of Hong Kong, 2001. http://sunzi.lib.hku.hk/hkuto/record.jsp?B2373615X.

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Dai, Nan. "I. Collagen-like polypeptides. II. Helix-turn-helix peptides and turn mimetics". Diss., Virginia Tech, 2008. http://hdl.handle.net/10919/28411.

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Collagen is one of the most important and abundant proteins in mammals. It consists of three left-handed PPII helixes coiled along a common axis to form a very compact right-handed super helix. The primary structure is shown to be (Gly-Xaa-Yaa)n repeats with high content of prolyl residues at both Xaa and Yaa positions. Cis-trans isomerization of the prolyl amide bonds is one of the rate-limiting steps during collagen triple helix folding. The conformationally locked alkene isosteres Fmoc-Gly-Ψ[(E)CH=C]-Pro-Hyp(tBu)-OH and Fmoc-Pro-Ψ[(E)CH=C]-Pro-OH were designed and synthesized. The synthesis of the Gly-Pro isostere had no stereo-control, and the two diastereomers of the tripeptide isostere Fmoc-Gly-Ψ[(E)CH=C]-Pro-Hyp(tBu)-OBn were separated by normal phase HPLC. Although the stereoselectivity of the asymmetric reduction was not good for the Pro-Pro isostere, the resulting diastereomers was separable by flash chromatography, and the absolute stereochemistry of the two diastereomers was determined by Mosher's method. The Gly-Pro alkenyl peptides, and their control peptide Ac-(Gly-Pro-Hyp)8-Gly-Gly-Tyr-NH2 were synthesized and purified. All three peptides showed a maximum around 225 nm and a minimum close to 200 nm in the CD spectra, which indicated the formation of PPII helixes. The Tm value of the control peptide was determined to be 50.0 °C. The peptide with Gly-Ψ[(E)CH=C]-L-Pro-Hyp as the guest triplet formed a stable triple helix with a Tm value of 28.3 °C. The peptide with Gly-Ψ[(E)CH=C]-D-Pro-Hyp as the guest triplet showed a linear decrease in the ellipticity with increasing temperature, which indicated that no triple helix was formed. The Pro-Pro alkenyl peptide and its control peptide H-(Pro-Pro-Gly)₁₀-OH were synthesized and purified. The T_m value of control peptide was determined to be 31.6 °C by extrapolation to 0 M TMAO in PBS buffer, which was very close to the measured value of 31.5 °C. The Pro-Pro alkenyl peptide began to show a maximum around 225 nm in the CD spectra when the concentration of TMAO was higher than 2.5 M. After extrapolation to 0 M TMAO, the T_m value was determined to be –22.0 °C. These results indicate that the backbone inter-chain hydrogen bond is one of the major forces in stabilizing the collagen triple helix, while cis-trans isomerization has limited contribution. The intrinsic properties of the amide bond may have huge influence on the stability of the collagen triple helix. The helix-turn-helix motif is an important tertiary structure in DNA-binding proteins. Stepwise modifications of the Antennapedia HTH peptide (27-55) were performed to improve the helicity and stability. The peptide with more side-chain ion-pairs was over 4 times more helical than the native Antp peptide, while the Ala-based peptide was over 9 times more helical than the native peptide. A 12-membered ring, Fmoc-protected HTH-turn mimic was designed and synthesized, and was ready for solid phase peptide synthesis. The solubility of the cyclic peptide was very poor, and the purification of the final product was very difficult. The solubility problem might also affect solid phase peptide synthesis in the future.
Ph. D.

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Ip, Wency Wan Sze. "Collagen triple helix repeat containing 1 increases melanoma cell migration, adhesion and survival through modulation of the actin cytoskeleton". Thesis, University of British Columbia, 2009. http://hdl.handle.net/2429/8929.

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Background: Collagen Triple Helix Repeat Containing 1 (CTHRC1) is a recently discovered extracellular protein that can bind and activate Wnt signaling pathway. In previous gene expression profiling experiments, it was found to be aberrantly upregulated in metastatic melanoma and its expression level was correlated with melanoma progression and metastasis. Objective: The purpose of this study is to understand the functional impact of CTHRC1 on cancer using melanoma cell lines as a model. Experimental Methods: We transfected two melanoma cell lines, MMAN and MMRU, with plasmid vectors to create stable clones with high and low CTHRC1 expression to study the functional effects of CTHRC1 in vitro. Using these two cell lines, we assayed for melanoma migration, adhesion and survival using scratch wound healing assay, attachment assay and cell cycle analysis, respectively. In addition, the cells were stained for F-actin with AlexaFluor 594 labeled phalloidin to observe for actin organization. Results: Using these two pairs of cell lines, we have found that CTHRC1 expression increased melanoma cell migration, enhanced melanoma cell adhesion to both tissue culture plastic and matrigel, and protected melanoma cells from serum deprivation induced apoptosis. Further, it was demonstrated that CTHRC1’s pro-survival effect was dependent on cell adhesion, as the protection effect was lost when melanoma cells were cultured in suspension. Immunofluorescent staining of F-actin revealed that CTHRC1 expression increased the formation structures such as focal complexes, lamellipodia and filopodia. Discussion: The increased formation of the adhesion structures may be the key to CTHRC1 associated cell migration, adhesion and survival. These structures are likely regulated by the Rho family of proteins that act downstream of the Wnt/PCP pathway, with which CTHRC1 has been previously demonstrated to be involved as a co-receptor. Conclusion: Results from this study suggest that CTHRC1 expression promotes cellular behaviours associated with tumour metastases. Therefore, inhibition of this protein may be able to block melanoma metastasis and may have value as a potential therapeutic.

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Rahgoshay, Keyvan. "Incorporation de prolines et pseudoprolines fluorées dans des chaînes peptidiques, conséquences conformationnelles et applications". Thesis, Cergy-Pontoise, 2019. http://www.theses.fr/2019CERG1037.

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Cette thèse porte sur la synthèse d’analogues fluorés de mimes de collagène synthétique et sur l’étude de leurs caractéristiques thermodynamiques, cinétiques et structurales. Notre laboratoire a récemment mis au point la synthèse d'acides aminés fluorés mimes de la proline (pseudoprolines). Dans un premier temps, une étude préliminaire a été effectuée sur des triplets monomériques modèles afin de confirmer l'aptitude de nos mimes fluorés à stabiliser les conformations pré-requises pour la structuration en triple hélice du collagène. Une fois celles-ci confirmées, nous avons ensuite mis au point des voies de synthèse permettant l'incorporation de ces pseudoprolines fluorées en synthèse peptidique sur phase solide. La synthèse de mime de collagène synthétique (21 résidus) incorporant nos analogues fluorés de proline a ensuite été réalisée. Les caractéristiques thermodynamiques, cinétiques et structurales de ces peptides mimes de collagène fluoré ont été déterminées par dichroïsme circulaire et par RMN. Ces pseudoprolines fluorées possèdent des propriétés singulières permettant l’obtention d’informations structurales au niveau local et peuvent ainsi être considérées comme de réelles sondes RMN 1H et 19F. Les résultats obtenus ouvrent également la voie à de nouvelles approches pour la synthèse de mimes peptidiques de collagène
In this thesis, we approach the synthesis of fluorinated analogs of collagen model peptides (CMP) and the study of their thermodynamic, kinetic and structural characteristics. Our laboratory recently developed the synthesis of fluorinated amino acids analogs of the proline residue (pseudoprolines). Firstly, a preliminary study was carried out on model triplets in order to confirm our fluorinated analogs’ ability to stabilize the pre-requisite conformations of collagen’s triple helix. Once these structural characteristics confirmed, we developed synthetic routes for the incorporation of these fluorinated pseudoprolines in solid phase peptide synthesis (SPPS). Several CMPs (21 residues) incorporating our fluorinated pseudoproline analogs were synthesized. The thermodynamic, kinetic and structural characteristics of these fluorinated CMPs were determined by circular dichroism and NMR. The fluorinated pseudoprolines possess singular properties which enable to acquire detailed insights on their structural surroundings. Thus, they can be considered as 1H and 19F NMR probes. The results obtained in this study also open the way to novel approaches for the synthesis of collagen model peptides

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Lalande, Mathieu. "Processus induits par l'irradiation de modèles peptidiques de la triple hélice du collagène en phase gazeuse". Thesis, Normandie, 2018. http://www.theses.fr/2018NORMC235/document.

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Le collagène est la protéine la plus abondante dans les mammifères, et le constituant principal de la matrice extracellulaire du cartilage. Les propriétés mécaniques de ce tissu sont dues à la structure particulière du collagène : la triple hélice. Lors de cette thèse, nous nous sommes intéressés à des peptides modèles de la triple hélice du collagène en phase gazeuse, ce qui permet l’étude de leurs propriétés intrinsèques, dont les processus fondamentaux induits par des rayonnements ionisants. Une étude structurale de ces systèmes par spectrométrie de mobilité ionique a permis de s’assurer qu’ils conservent bien leurs propriétés structurales et de stabilité en l’absence de solvant. De plus, cette stabilité se manifeste aussi lors de l’irradiation par photons ionisants dans un piège à ions. Par ailleurs, nous avons observé, grâce à la spectrométrie de masse, une transition entre photo-excitation et photo-ionisation lorsque l’énergie du photon absorbé augmente dans la gamme VUV-X. Une partie de cette énergie est également redistribuée dans les modes de vibration du système, croît avec l’énergie du photon, et induit la fragmentation inter puis intramoléculaire de la triple hélice. Nous avons également irradié pour la première fois des peptides en phase gazeuse par un faisceau d’ions carbones à l’énergie cinétique pertinente dans le contexte de l’hadronthérapie. Un processus non-observé avec les photons a été mis en évidence : le détachement de proton. Enfin, la validation d’un nouveau dispositif expérimental dédié à l’irradiation de protéines et brins d’ADN par des ions en faisceaux croisés, ainsi que les premiers résultats obtenus, seront abordés
Collagen is the most abundant protein in mammals, and the main constituent of the extracellular matrix of cartilage. The mechanical properties of this tissue are due to the particular triple helical structure of collagen. In this thesis, we focused on peptidic models of the collagen triple helix in thegas phase, which allows reaching their intrinsic properties, including fundamental processes induced by ionizing radiations. An ion mobility spectrometry study of these systems proved that they retain their structural and stability properties in the absence of solvent. In addition, these stability properties also play a role after irradiation with ionizing photons in an ion trap. Furthermore, we have observed, thanks to mass spectrometry, a transition between photo-excitation and photoionization as the energy of the absorbed photon increases in the VUV-X range. Part of this energy is also redistributed in the vibration modes of the system, increases with photon energy, and induces intramolecular as well as intramolecular fragmentation of the triple helix. For the first time, we irradiated peptides in the gas phase by a carbon ion beam having a kinetic energy relevant in the context of hadrontherapy. A process that was absent from studies with photons has been observed : proton detachment. In the last chapter, the validation of a new experimental device dedicated to the irradiation of proteins and DNA strands in a cross-beam configuration, as well as the first results obtained, will be reported

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Chen, Chia-Ching, e 陳佳青. "Study of Cation-π interactions in the stability and self-assembly of collagen triple helix". Thesis, 2010. http://ndltd.ncl.edu.tw/handle/50835071376218003030.

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Elfert, Susanne Claudia [Verfasser]. "Correlation between triple helix stability of collagen VII and skin fragility in dystrophic epidermolysis bullosa / vorgelegt von Susanne Claudia Elfert". 2009. http://d-nb.info/993806457/34.

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Jenkins, Cara Lee. "Insights into the determinants of collagen triple helix stability : II. inhibition of RNase A by analogs of 3-prime-uridinemonophosphate /". 2004. http://www.library.wisc.edu/databases/connect/dissertations.html.

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Capítulos de livros sobre o assunto "Carbamylation of the collagen triple helix"

Engel, Jürgen, e Hans Peter Bächinger. "Structure, Stability and Folding of the Collagen Triple Helix". In Topics in Current Chemistry, 7–33. Berlin, Heidelberg: Springer Berlin Heidelberg, 2005. http://dx.doi.org/10.1007/b103818.

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Chow, Wing Ying. "Investigation of Triple-Helix Collagen Hydroxylation by Solid-State NMR Spectroscopy". In Methods in Molecular Biology, 57–77. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9095-5_5.

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Shoulders, Matthew D., e Ronald T. Raines. "Modulating Collagen Triple-Helix Stability with 4-Chloro, 4-Fluoro, and 4-Methylprolines". In Advances in Experimental Medicine and Biology, 251–52. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-73657-0_115.

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Kusebauch, Ulrike, Lisa Lorenz, Sergio A. Cadamuro, Hans-Jürgen Musiol, Martin O. Lenz, Christian Renner, Josef Wachtveitl e Luis Moroder. "Light-Switchable Folding/Unfolding of the Collagen Triple Helix with Azobenzene-Containing Model Peptides". In Advances in Experimental Medicine and Biology, 57–59. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-73657-0_25.

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Rump, Erik T., Dirk T. S. Rijkers, Philip G. de Groot e Rob M. J. Liskamp. "Stabilization of the Triple Helix of Collagen Peptides Using Fluoroproline and/or Triacid Scaffolds". In Peptides: The Wave of the Future, 379–80. Dordrecht: Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-010-0464-0_175.

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Kaur, Prerna, Hanying Bai e Hiroshi Matsui. "Genetically Modified Collagen-like Triple Helix Peptide as Biomimetic Template THIS CHAPTER HAS BEEN RETRACTED". In Hybrid Nanomaterials, 251–68. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9781118003497.ch9.

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Xu, Yujia. "Thermal Stability of Collagen Triple Helix". In Methods in Enzymology, 211–32. Elsevier, 2009. http://dx.doi.org/10.1016/s0076-6879(09)66009-2.

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Brodsky, Barbara, e Anton V. Persikov. "Molecular Structure of the Collagen Triple Helix". In Fibrous Proteins: Coiled-Coils, Collagen and Elastomers, 301–39. Elsevier, 2005. http://dx.doi.org/10.1016/s0065-3233(05)70009-7.

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Premachandra, Jagath K., e Chandima Kumudinie Jayasuriya. "Collagen". In Polymer Data Handbook, 104–12. Oxford University PressNew York, NY, 2009. http://dx.doi.org/10.1093/oso/9780195181012.003.0018.

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Abstract Class Polypeptides and proteins Structure The most common type of collagen, Collagen I, is composed of two kinds of polypeptide helices, α1 and α2, in a 2:1 ratio respectively, to form a triple helix. The α1 and α2 chains of tropocollagen have a regularly repeating sequence of amino acid residues in which glycine is found at every third residue. This sequence can be written (GLY–X–Y)n , where X and Y are often proline and hydroxyproline respectively.(1) Functions An extracellular protein, which is responsible for the strength and flexibility of connective tissue. Accounts for 25–30% of the protein in an animal.Major component in all mammalian tissues including skin, bone cartilage, tendons, and ligaments. Major Applications Biomaterial applications such as dermal implant, carrier of drugs, cell culture matrix, wound dressing, material for hybrid organ, drug delivery system, soft contact lens, tissue implants, cardiovascular graft, artificial heart, etc. Synthetic sausage casings in food industry.

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"Collagen and Skin Structure". In Tanning Chemistry: The Science of Leather, 1–31. 2^a ed. The Royal Society of Chemistry, 2019. http://dx.doi.org/10.1039/9781788012041-00001.

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In order to understand the principles that underpin the conversion of hide or skin to leather, it is necessary to know the fundamental structure of the raw material and how that structure might be modified chemically. The chemistry of collagen defines not only the sequencing of its amino acid constituents but also the physical nature of its structure and how it creates levels of structure or a hierarchy. This depends on the chains creating a triple helix as the basic unit of structure. The chemical properties of collagen are defined by the sidechains on the helices, which may be charged, depending on the pH; in this way, collagen can undergo a wide range of covalent or electrostatic reactions, which are the basis for tanning processes. At the heart of the chemistry of collagen is the relationship with water, which is an integral feature of structure: the supramolecular matrix of water around the triple helices provides the region for chemical modification, leading to tanning technology.

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Trabalhos de conferências sobre o assunto "Carbamylation of the collagen triple helix"

Deniset-Besseau, A., P. De Sa Peixoto, J. Duboisset, C. Loison, F. Hache, E. Benichou, P. F. Brevet, G. Mosser e M. C. Schanne-Klein. "Nonlinear optical response of the collagen triple helix and second harmonic microscopy of collagen liquid crystals". In BiOS, editado por Ammasi Periasamy, Peter T. C. So e Karsten König. SPIE, 2010. http://dx.doi.org/10.1117/12.840873.

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Wyatt, Karla E. K., Jonathan W. Bourne e Peter A. Torzilli. "Deformation-Dependent Enzyme Cleavage of Collagen". In ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-176502.

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Collagen degradation is a mechanism for normal musculoskeletal development and extracellular matrix (ECM) maintenance, and in response to trauma, disease and inflammation. Matrix metalloproteinases (MMP-1, 8, and 13, the collagenases) are the primary enzymes that act to degrade collagen. These MMPs gain access to the collagen triple helix by binding to the enzyme’s attachment domain along the α-chains, followed by separation (unwinding) of the α-chains to expose the 3/4–1/4 cleavage site, and then cleavage of the α-chain by the enzyme’s catalytic domain [3, 5].

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Deniset-Besseau, A., J. Duboisset, C. Loison, F. Hache, E. Benichou, P. F. Brevet e M. C. Schanne-Klein. "Second order hyperpolarizability of the collagen triple helix: Measurement and determination of its physical origin". In 11th European Quantum Electronics Conference (CLEO/EQEC). IEEE, 2009. http://dx.doi.org/10.1109/cleoe-eqec.2009.5194760.

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Rawal, Atul, Kristen L. Rhinehardt e Ram V. Mohan. "Mechanical Behavior of Collagen Mimetic Peptides Under Fraying Deformation via Molecular Dynamics". In ASME 2019 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2019. http://dx.doi.org/10.1115/imece2019-11492.

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Abstract Collagen is a pervasive, triple helical, extracellular matrix (ECM) protein, found in human body from skin and bones to blood vessels and lungs, making it biocompatible, biodegradable, capable of cell attachment, and relevant for applications in bio-polymers, tissue engineering and a plethora of other bio-medical fields. Natural collagen’s extraction from natural sources is time consuming, sometimes costly, and it is difficult to render, and could present undesired biological and pathogenic changes. Nanoscale collagen mimetic peptides (Synthetic Collagen), without the unwanted biological entities present in the medium, has shown to mimic the unique properties that are present in natural collagen. Synthetic collagen, thus provides a superior alternative compared to natural collagen for its utilization in several applications. Their properties are affected by surrounding environments, including various solvents, and can be tailored toward specific applications. The focus of this paper is to investigate the mechanical properties of these nanoscale collagen mimetic peptides with lengths of about 10nm, leading to understanding of their feasibility in bio-printing of a composite polymeric collagen biomaterial with a blend of multiple synthetic collagen molecules. Molecular dynamics modeling is used to simulate, model and analyze mechanical properties of synthetic collagen peptides. In particular, mechanical behavior of these peptides are studied. An in-depth insight into the deformation and structural properties of the collagen peptides are of innovative significance for a multitude of bio medical engineering applications. Present paper employed steered molecular dynamics as the principal method of investigating the mechanical properties of nanoscale collagen mimetic peptide 1BKV, which closely resembles natural collagen with a shorter sequence length of 30 amino acids. A detailed comprehension of the protein’s mechanical properties is investigated through fraying deformation behavior studied. A calculated Gibbs free energy value of 40 Kcal/mol corresponds with a complete unfolding of a single alpha-helix peptide chain from a triple helical protein in case of fraying. Force needed for complete separation of the alpha-helix from the triple-helical protein is analyzed, and discussed in this paper.

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Taylor, Phillip. "Computational design of collagen-like-peptides (CLP) for desired CLP triple helix melting transition and assembled structure." In Proposed for presentation at the 2022 CINT Annual User Conference held September 20-22, 2022 in Albuquerque , NM. US DOE, 2022. http://dx.doi.org/10.2172/2004798.

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Zareian, Ramin, Kelli P. Church e Jeffrey W. Ruberti. "Influence of Mechanical Load on the Degradation of Corneal Collagen". In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-193036.

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Collagen is one of the most important structural proteins in vertebrate animals. Over 25 different types of collagen have been identified, but type I collagen is the most abundant fibril forming collagen and contributes to the structural performance numerous connective tissues including ligaments, tendons and cornea [1]. In addition to collagen self-assembly, collagen degradation is an important step in the development, remodeling, homeostasis and pathology of load-bearing ECM. Matrix Metalloproteinase (MMP) types I and VIII, bacterial collagenase and cathepsin are the best known enzymes capable of directly degrading the collagen triple helix [2, 3]. Several researchers have hypothesized that straining collagen fibrils makes them less susceptible to enzymatic degradation [4, 5]. This concept, which we refer to as “strain-stabilization” has important implications for our understanding of collagen as an engineering material.

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Rahgoshay, Keyvan, Anas Terrien, Nathalie Lensen, Thierry Brigaud, Emeric Miclet e Grégory Chaume. "Use of Trifluoromethylated Pseudoprolines for the Design of Collagen Triple Helix containing Unusual C(5)-Substituted Proline Surrogates". In 35th European Peptide Symposium. Prompt Scientific Publishing, 2018. http://dx.doi.org/10.17952/35eps.2018.206.

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Swickrath, Michael J., Kevin Dorfman, Yoav Segal e Victor H. Barocas. "The Effect of Composition and Inter- and Intrafibrillar Interactions on the Structure of Collagen IV Networks in the Computer-Simulated Glomerular Basement Membrane". In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-205518.

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The glomerular basement membrane of the kidney, responsible for performing ultrafiltration blood plasma, is largely comprised of type-IV collagen and laminin. Type-IV collagen self-assembles into a heterotrimer composed of three distinct domains (fig. 1A): (1) the globular non-collagenous NCl domain of ∼10 nm in diameter, (2) the non-collagenous 7S domain ∼30 nm in length and ∼3nm in diameter, and (3) the collagenous triple helix of ∼370 nm in length and ∼3 nm in diameter composed of a repeating Gly-X-Y subunit [1]. The heterotrimers associate with remarkable specificity from six genetically distinct α-chains, α1(IV) to α6(IV) forming α1α1α2, α3α4α5, and α5α5α6 heterotrimers [2]. In the healthy glomerulus, α1α1α2 ([α1]2α2) is the predominate collagen while significant α3α4α5 is present; α5α5α6 exists only in negligible quantities [2].

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Sun-Hee, Leem, Kang Tae-Hong, Chung Jin Woong, Hwang Yeonsil, Kim Seokho e Koh Sang Seok. "Abstract A85: Collagen triple helix repeat containing-1 enhances the aggressiveness of pancreatic tumor by increased cancer cell motility and adhesiveness". In Abstracts: AACR Special Conference on Pancreatic Cancer: Innovations in Research and Treatment; May 18-21, 2014; New Orleans, LA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.panca2014-a85.

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Deniset-Besseau, A., M. Strupler, J. Duboisset, P. De Sa Peixoto, E. Benichou, C. Fligny, P. L. Tharaux, G. Mosser, P. F. Brevet e M. C. Schanne-Klein. "Measurement of the quadratic hyperpolarizability of the collagen triple helix and application to second harmonic imaging of natural and biomimetic collagenous tissues". In SPIE Europe Security + Defence, editado por James G. Grote, François Kajzar e Roberto Zamboni. SPIE, 2009. http://dx.doi.org/10.1117/12.829882.

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