Journal articles: 'Carbamylation of the collagen triple helix'

1

Brodsky, Barbara, and John A. M. Ramshaw. "The collagen triple-helix structure." Matrix Biology 15, no. 8-9 (March 1997): 545–54. http://dx.doi.org/10.1016/s0945-053x(97)90030-5.

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Newberry, Robert W., Brett VanVeller, and Ronald T. Raines. "Thioamides in the collagen triple helix." Chemical Communications 51, no. 47 (2015): 9624–27. http://dx.doi.org/10.1039/c5cc02685g.

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Liu, Fei, Zhe Yu, Beibei Wang, and Bor-Sen Chiou. "Changes in Structures and Properties of Collagen Fibers during Collagen Casing Film Manufacturing." Foods 12, no. 9 (April 29, 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, and Tamaki Kato. "Design, Synthesis, and Photo-Responsive Properties of a Collagen Model Peptide Bearing an Azobenzene." Organics 3, no. 4 (October 11, 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, and Takaki Koide. "The Thermal Stability of the Collagen Triple Helix Is Tuned According to the Environmental Temperature." International Journal of Molecular Sciences 23, no. 4 (February 12, 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, and V. Ya Maleev. "Physical factors of collagen triple helix stability." Biopolymers and Cell 22, no. 6 (November 20, 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, and Ronald T. Raines. "Macrocyclic Scaffold for the Collagen Triple Helix." Organic Letters 8, no. 21 (October 2006): 4735–38. http://dx.doi.org/10.1021/ol061771w.

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Mizuno, Kazunori, Toshihiko Hayashi, David H. Peyton, and Hans Peter Bächinger. "Hydroxylation-induced Stabilization of the Collagen Triple Helix." Journal of Biological Chemistry 279, no. 36 (July 1, 2004): 38072–78. http://dx.doi.org/10.1074/jbc.m402953200.

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9

Persikov, Anton V., John A. M. Ramshaw, Alan Kirkpatrick, and Barbara Brodsky. "Amino Acid Propensities for the Collagen Triple-Helix†." Biochemistry 39, no. 48 (December 2000): 14960–67. http://dx.doi.org/10.1021/bi001560d.

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Mizuno, Kazunori, Toshihiko Hayashi, and Hans Peter Bächinger. "Hydroxylation-induced Stabilization of the Collagen Triple Helix." Journal of Biological Chemistry 278, no. 34 (June 13, 2003): 32373–79. http://dx.doi.org/10.1074/jbc.m304741200.

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Acevedo-Jake, Amanda M., Daniel H. Ngo, and Jeffrey D. Hartgerink. "Control of Collagen Triple Helix Stability by Phosphorylation." Biomacromolecules 18, no. 4 (March 10, 2017): 1157–61. http://dx.doi.org/10.1021/acs.biomac.6b01814.

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12

De Simone, Alfonso, Luigi Vitagliano, and Rita Berisio. "Role of hydration in collagen triple helix stabilization." Biochemical and Biophysical Research Communications 372, no. 1 (July 2008): 121–25. http://dx.doi.org/10.1016/j.bbrc.2008.04.190.

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13

Schweizer, Sabine, Andreas Bick, Lalitha Subramanian, and Xenophon Krokidis. "Influences on the stability of collagen triple-helix." Fluid Phase Equilibria 362 (January 2014): 113–17. http://dx.doi.org/10.1016/j.fluid.2013.09.033.

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Lee, Song-Gil, Jee Yeon Lee, and Jean Chmielewski. "Investigation of pH-Dependent Collagen Triple-Helix Formation." Angewandte Chemie International Edition 47, no. 44 (October 20, 2008): 8429–32. http://dx.doi.org/10.1002/anie.200802224.

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Lee, Song-Gil, Jee Yeon Lee, and Jean Chmielewski. "Investigation of pH-Dependent Collagen Triple-Helix Formation." Angewandte Chemie 120, no. 44 (October 20, 2008): 8557–60. http://dx.doi.org/10.1002/ange.200802224.

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16

Baker, A. T., J. A. M. Ramshaw, D. Chan, W. G. Cole, and J. F. Bateman. "Changes in collagen stability and folding in lethal perinatal osteogenesis imperfecta. The effect of α1(I)-chain glycine-to-arginine substitutions." Biochemical Journal 261, no. 1 (July 1, 1989): 253–57. http://dx.doi.org/10.1042/bj2610253.

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The effect of glycine-to-arginine mutations in the alpha 1 (I)-chain on collagen triple-helix structure in lethal perinatal osteogenesis imperfecta was studied by determination of the helix denaturation temperature and by computerized molecular modelling. Arginine substitutions at glycine residues 391 and 667 resulted in similar small decreases in helix stability. Molecular modelling suggested that the glycine-to-arginine-391 mutant resulted in only a relatively small localized disruption to the helix structure. Thus the glycine-to-arginine substitutions may lead to only a small structural abnormality of the collagen helix, and it is most likely that the over-modification of lysine, poor secretion, increased degradation and other functional sequelae result from a kinetic defect in collagen helix formation resulting from the mutation.

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Walker, Kenneth T., Ruodan Nan, David W. Wright, Jayesh Gor, Anthony C. Bishop, George I. Makhatadze, Barbara Brodsky, and Stephen J. Perkins. "Non-linearity of the collagen triple helix in solution and implications for collagen function." Biochemical Journal 474, no. 13 (June 16, 2017): 2203–17. http://dx.doi.org/10.1042/bcj20170217.

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Collagen adopts a characteristic supercoiled triple helical conformation which requires a repeating (Xaa-Yaa-Gly)n sequence. Despite the abundance of collagen, a combined experimental and atomistic modelling approach has not so far quantitated the degree of flexibility seen experimentally in the solution structures of collagen triple helices. To address this question, we report an experimental study on the flexibility of varying lengths of collagen triple helical peptides, composed of six, eight, ten and twelve repeats of the most stable Pro-Hyp-Gly (POG) units. In addition, one unblocked peptide, (POG)10unblocked, was compared with the blocked (POG)10 as a control for the significance of end effects. Complementary analytical ultracentrifugation and synchrotron small angle X-ray scattering data showed that the conformations of the longer triple helical peptides were not well explained by a linear structure derived from crystallography. To interpret these data, molecular dynamics simulations were used to generate 50 000 physically realistic collagen structures for each of the helices. These structures were fitted against their respective scattering data to reveal the best fitting structures from this large ensemble of possible helix structures. This curve fitting confirmed a small degree of non-linearity to exist in these best fit triple helices, with the degree of bending approximated as 4–17° from linearity. Our results open the way for further studies of other collagen triple helices with different sequences and stabilities in order to clarify the role of molecular rigidity and flexibility in collagen extracellular and immune function and disease.

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Kubyshkin, Vladimir, and Nediljko Budisa. "Promotion of the collagen triple helix in a hydrophobic environment." Organic & Biomolecular Chemistry 17, no. 9 (2019): 2502–7. http://dx.doi.org/10.1039/c9ob00070d.

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19

Egli, Jasmine, Roman S. Erdmann, Pascal J. Schmidt, and Helma Wennemers. "Effect of N- and C-terminal functional groups on the stability of collagen triple helices." Chemical Communications 53, no. 80 (2017): 11036–39. http://dx.doi.org/10.1039/c7cc05837c.

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20

Aumailley, M., and R. Timpl. "Attachment of cells to basement membrane collagen type IV." Journal of Cell Biology 103, no. 4 (October 1, 1986): 1569–75. http://dx.doi.org/10.1083/jcb.103.4.1569.

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Of ten different cell lines examined, three showed distinct attachment and spreading on collagen IV substrates, and neither attachment nor spreading was enhanced by adding soluble laminin or fibronectin. This reaction was not inhibited by cycloheximide or antibodies to laminin, indicating a direct attachment to collagen IV without the need of mediator proteins. Cell-binding sites were localized to the major triple-helical domain of collagen IV and required an intact triple helical conformation for activity. Fibronectin showed preferential binding to denatured collagen IV necessary to mediate cell binding to the substrate. Fibronectin binding sites of collagen IV were mapped to unfolded structures of the major triple-helical domain and show a similar specificity to fibronectin-binding sites of collagen I. The data extend previous observations on biologically potential binding sites located in the triple helix of basement membrane collagen IV.

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21

Shen, Yiming, Deyi Zhu, Wenhui Lu, Bing Liu, Yanchun Li, and Shan Cao. "The Characteristics of Intrinsic Fluorescence of Type I Collagen Influenced by Collagenase I." Applied Sciences 8, no. 10 (October 16, 2018): 1947. http://dx.doi.org/10.3390/app8101947.

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The triple helix structure of collagen can be degraded by collagenase. In this study, we explored how the intrinsic fluorescence of type I collagen was influenced by collagenase I. We found that tyrosine was the main factor that could successfully excite the collagen fluorescence. Initially, self-assembly behavior of collagen resulted in a large amount of tyrosine wrapped with collagen, which decreased the fluorescence intensity of type I collagen. After collagenase cleavage, some wrapped-tyrosine could be exposed and thereby the intrinsic fluorescence intensity of collagen increased. By observation and analysis, the influence of collagenase to intrinsic fluorescence of collagen was investigated and elaborated. Furthermore, collagenase cleavage to the special triple helix structure of collagen would result in a slight improvement of collagen thermostability, which was explained by the increasing amount of terminal peptides. These results are helpful and effective for reaction mechanism research related to collagen, which can be observed by fluorescent technology. Meantime, the reaction behaviors of both collagenase and collagenolytic proteases can also be analyzed by fluorescent technology. In conclusion, this research provides a foundation for the further investigation of collagen reactions in different areas, such as medicine, nutrition, food and agriculture.

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Kubyshkin, Vladimir. "Stabilization of the triple helix in collagen mimicking peptides." Organic & Biomolecular Chemistry 17, no. 35 (2019): 8031–47. http://dx.doi.org/10.1039/c9ob01646e.

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Sun, Xiuxia, Jun Fan, Weiran Ye, Han Zhang, Yong Cong, and Jianxi Xiao. "A highly specific graphene platform for sensing collagen triple helix." Journal of Materials Chemistry B 4, no. 6 (2016): 1064–69. http://dx.doi.org/10.1039/c5tb02218e.

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We have designed a dye-labeled, highly positively charged single stranded collagen (ssCOL) peptide probe whose adsorption into GO quenches its fluorescence. The hybridization of the ssCOL probe with a complementary target sequence forms a triple stranded collagen (tsCOL) peptide, resulting in the retention of the fluorescence of the probe.

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24

Klein, G., CA Muller, E. Tillet, ML Chu, and R. Timpl. "Collagen type VI in the human bone marrow microenvironment: a strong cytoadhesive component." Blood 86, no. 5 (September 1, 1995): 1740–48. http://dx.doi.org/10.1182/blood.v86.5.1740.bloodjournal8651740.

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Collagen type VI, which forms characteristic microfibrillar structures, is assembled from three individual alpha(VI) chains that form a short triple helix and two adjacent globular domains. Expression of all three alpha (VI) collagen chains in the human bone marrow (BM) microenvironment could be detected by chain-specific antibodies in tissue sections and in the adherent stromal layer of long-term BM cultures. In functional studies, collagen type VI was shown to be a strong adhesive substrate for various hematopoietic cell lines and light-density BM mononuclear cells. The adhesive site within the molecule seems to be restricted to the triple helical domain of all three alpha (VI) chains, because individual alpha (VI) chains were not active in the attachment assays. Adhesion of the hematopoietic cell lines to collagen VI was dose-dependent and could be inhibited by heparin. Although the triple helix contains several RGD sequences, adhesion of the hematopoietic cell types to collagen VI could be blocked neither by RGD-containing peptides nor by a neutralizing antibody to the beta 1 integrin subunit. In combination with an antiadhesive substrate, the binding properties of collagen VI could be downregulated. These data suggest that this collagen type may play an important role in the adhesion of hematopoietic cells within the BM microenvironment.

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Rainey, Jan K., and M. Cynthia Goh. "A statistically derived parameterization for the collagen triple-helix." Protein Science 11, no. 11 (April 13, 2009): 2748–54. http://dx.doi.org/10.1110/ps.0218502.

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26

Bann, James G., and Hans Peter Bächinger. "Glycosylation/Hydroxylation-induced Stabilization of the Collagen Triple Helix." Journal of Biological Chemistry 275, no. 32 (May 25, 2000): 24466–69. http://dx.doi.org/10.1074/jbc.m003336200.

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27

Li, Y., C. A. Foss, D. D. Summerfield, J. J. Doyle, C. M. Torok, H. C. Dietz, M. G. Pomper, and S. M. Yu. "Targeting collagen strands by photo-triggered triple-helix hybridization." Proceedings of the National Academy of Sciences 109, no. 37 (August 27, 2012): 14767–72. http://dx.doi.org/10.1073/pnas.1209721109.

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Tronci, Giuseppe, Stephen J. Russell, and David J. Wood. "Photo-active collagen systems with controlled triple helix architecture." Journal of Materials Chemistry B 1, no. 30 (2013): 3705. http://dx.doi.org/10.1039/c3tb20720j.

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Kirkness, Michael WH, Kathrin Lehmann, and Nancy R. Forde. "Mechanics and structural stability of the collagen triple helix." Current Opinion in Chemical Biology 53 (December 2019): 98–105. http://dx.doi.org/10.1016/j.cbpa.2019.08.001.

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Rainey, Jan K., and M. Cynthia Goh. "A statistically derived parameterization for the collagen triple-helix." Protein Science 13, no. 8 (August 2004): 2276. http://dx.doi.org/10.1002/pro.132276.

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Persikov, Anton V., John A. M. Ramshaw, and Barbara Brodsky. "Collagen model peptides: Sequence dependence of triple-helix stability." Biopolymers 55, no. 6 (2000): 436–50. http://dx.doi.org/10.1002/1097-0282(2000)55:6<436::aid-bip1019>3.0.co;2-d.

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32

Bächinger, Hans Peter, and Janice M. Davis. "Sequence specific thermal stability of the collagen triple helix." International Journal of Biological Macromolecules 13, no. 3 (June 1991): 152–56. http://dx.doi.org/10.1016/0141-8130(91)90040-2.

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Kusebauch, Ulrike, Sergio A. Cadamuro, Hans-Jürgen Musiol, Martin O. Lenz, Josef Wachtveitl, Luis Moroder, and Christian Renner. "Photocontrolled Folding and Unfolding of a Collagen Triple Helix." Angewandte Chemie International Edition 45, no. 42 (October 27, 2006): 7015–18. http://dx.doi.org/10.1002/anie.200601432.

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Pantelopulos, George A., and Robert B. Best. "BPS2025 - Free energy landscape of collagen triple helix association." Biophysical Journal 124, no. 3 (February 2025): 229a. https://doi.org/10.1016/j.bpj.2024.11.1256.

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35

KAFIENAH, Wa'el, Dieter BRÖMME, David J. BUTTLE, Lisa J. CROUCHER, and Anthony P. HOLLANDER. "Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix." Biochemical Journal 331, no. 3 (May 1, 1998): 727–32. http://dx.doi.org/10.1042/bj3310727.

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Cathepsin K (EC 3.4.22.38) is a recently described enzyme that has been shown to cleave type I collagen in its triple helix. The aim of this study was to determine if it also cleaves type II collagen in the triple helix and to identify the helical cleavage site(s) in types I and II collagens. Soluble human and bovine type II collagen, and rat type I collagen, were incubated with cathepsin K before the reaction was stopped with trans-epoxysuccinyl-l-leucylamido-(4-guanidino)butane (E-64). Analysis by SDS/PAGE of the collagen digests showed that optimal activity of cathepsin K against native type II collagen was between pH 5.0 and 5.5 and against denatured collagen between pH 4.0 and 7.0. The enzyme cleaved telopeptides as well as the α1(II) chains, generating multiple fragments in the range 90–120 kDa. The collagenolytic activity was not due to a contaminating metalloenzyme or serine proteinase as it was not inhibited by 1,10-phenanthroline, EDTA or 3,4-dichloroisocoumarin. Western blotting with anti-peptide antibodies to different regions of the α1(II) chain suggested that cathepsin K cleaved native α1(II) chains in the N-terminal region of the helical domain rather than at the well-defined collagenase cleavage site. This was confirmed by N-terminal sequencing of one of the fragments, revealing cleavage at a Gly-Lys bond, 58 residues from the N-terminus of the helical domain. By using a similar approach, cathepsin K was found to cleave native type I collagen close to the N-terminus of its triple helix. These results indicate that cathepsin K could have a role in the turnover of type II collagen, as well as type I collagen.

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Pan, Hao, Xuehua Zhang, Jianbo Ni, Qianqian Liang, Xin Jiang, Zihui Zhou, and Wenzheng Shi. "Effects of Ultrasonic Power on the Structure and Rheological Properties of Skin Collagen from Albacore (Thunnus alalunga)." Marine Drugs 22, no. 2 (February 10, 2024): 84. http://dx.doi.org/10.3390/md22020084.

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The effects of ultrasonic power (0, 150, 300, 450, and 600 W) on the extraction yield and the structure and rheological properties of pepsin-soluble collagen (PSC) from albacore skin were investigated. Compared with the conventional pepsin extraction method, ultrasonic treatment (UPSC) significantly increased the extraction yield of collagen from albacore skin, with a maximum increase of 8.56%. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis revealed that peptides of low molecular weight were produced when the ultrasonic power exceeded 300 W. Meanwhile, secondary structure, tertiary structure, and X-ray diffraction analyses showed that the original triple helix structure of collagen was intact after the ultrasonic treatment. The collagen solutions extracted under different ultrasonic powers had significant effects on the dynamic frequency sweep, but a steady shear test suggested that the collagen extracted at 150 W had the best viscosity. These results indicate that an ultrasonic power between 150 and 300 W can improve not only the extraction yield of natural collagen, but also the rheological properties of the collagen solution without compromising the triple helix structure.

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Qiang, Shumin, Cheng Lu, and Fei Xu. "Disrupting Effects of Osteogenesis Imperfecta Mutations Could Be Predicted by Local Hydrogen Bonding Energy." Biomolecules 12, no. 8 (August 11, 2022): 1104. http://dx.doi.org/10.3390/biom12081104.

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Osteogenesis imperfecta(OI) is a disease caused by substitution in glycine residues with different amino acids in type I collagen (Gly-Xaa-Yaa)n. Collagen model peptides can capture the thermal stability loss of the helix after Gly mutations, most of which are homotrimers. However, a majority of natural collagen exists in heterotrimers. To investigate the effects of chain specific mutations in the natural state of collagen more accurately, here we introduce various lengths of side-chain amino acids into ABC-type heterotrimers. The disruptive effects of the mutations were characterized both experimentally and computationally. We found the stability decrease in the mutants was mainly caused by the disruption of backbone hydrogen bonds. Meanwhile, we found a threshold value of local hydrogen bonding energy that could predict triple helix folding or unfolding. Val caused the unfolding of triple helices, whereas Ser with a similar side-chain length did not. Structural details suggested that the side-chain hydroxyl group in Ser forms hydrogen bonds with the backbone, thereby compensating for the mutants’ decreased stability. Our study contributes to a better understanding of how OI mutations destabilize collagen triple helices and the molecular mechanisms underlying OI.

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Nagai, Naoko, Masanori Hosokawa, Shigeyoshi Itohara, Eijiro Adachi, Takatoshi Matsushita, Nobuko Hosokawa, and Kazuhiro Nagata. "Embryonic Lethality of Molecular Chaperone Hsp47 Knockout Mice Is Associated with Defects in Collagen Biosynthesis." Journal of Cell Biology 150, no. 6 (September 18, 2000): 1499–506. http://dx.doi.org/10.1083/jcb.150.6.1499.

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Triple helix formation of procollagen after the assembly of three α-chains at the C-propeptide is a prerequisite for refined structures such as fibers and meshworks. Hsp47 is an ER-resident stress inducible glycoprotein that specifically and transiently binds to newly synthesized procollagens. However, the real function of Hsp47 in collagen biosynthesis has not been elucidated in vitro or in vivo. Here, we describe the establishment of Hsp47 knockout mice that are severely deficient in the mature, propeptide-processed form of α1(I) collagen and fibril structures in mesenchymal tissues. The molecular form of type IV collagen was also affected, and basement membranes were discontinuously disrupted in the homozygotes. The homozygous mice did not survive beyond 11.5 days postcoitus (dpc), and displayed abnormally orientated epithelial tissues and ruptured blood vessels. When triple helix formation of type I collagen secreted from cultured cells was monitored by protease digestion, the collagens of Hsp47+/+ and Hsp47+/− cells were resistant, but those of Hsp47−/− cells were sensitive. These results indicate for the first time that type I collagen is unable to form a rigid triple-helical structure without the assistance of molecular chaperone Hsp47, and that mice require Hsp47 for normal development.

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Schwob, Lucas, Mathieu Lalande, Jimmy Rangama, Dmitrii Egorov, Ronnie Hoekstra, Rahul Pandey, Samuel Eden, Thomas Schlathölter, Violaine Vizcaino, and Jean-Christophe Poully. "Single-photon absorption of isolated collagen mimetic peptides and triple-helix models in the VUV-X energy range." Physical Chemistry Chemical Physics 19, no. 28 (2017): 18321–29. http://dx.doi.org/10.1039/c7cp02527k.

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Hartmann, Julian, and Martin Zacharias. "Mechanism of collagen folding propagation studied by Molecular Dynamics simulations." PLOS Computational Biology 17, no. 6 (June 8, 2021): e1009079. http://dx.doi.org/10.1371/journal.pcbi.1009079.

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Collagen forms a characteristic triple helical structure and plays a central role for stabilizing the extra-cellular matrix. After a C-terminal nucleus formation folding proceeds to form long triple-helical fibers. The molecular details of triple helix folding process is of central importance for an understanding of several human diseases associated with misfolded or unstable collagen fibrils. However, the folding propagation is too rapid to be studied by experimental high resolution techniques. We employed multiple Molecular Dynamics simulations starting from unfolded peptides with an already formed nucleus to successfully follow the folding propagation in atomic detail. The triple helix folding was found to propagate involving first two chains forming a short transient template. Secondly, three residues of the third chain fold on this template with an overall mean propagation of ~75 ns per unit. The formation of loops with multiples of the repeating unit was found as a characteristic misfolding event especially when starting from an unstable nucleus. Central Gly→Ala or Gly→Thr substitutions resulted in reduced stability and folding rates due to structural deformations interfering with folding propagation.

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Yang, Ke, Jing Sun, Dan Wei, Lu Yuan, Jirong Yang, Likun Guo, Hongsong Fan, and Xingdong Zhang. "Photo-crosslinked mono-component type II collagen hydrogel as a matrix to induce chondrogenic differentiation of bone marrow mesenchymal stem cells." Journal of Materials Chemistry B 5, no. 44 (2017): 8707–18. http://dx.doi.org/10.1039/c7tb02348k.

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42

He, Xiaofeng, Liling Xie, Xiaoshan Zhang, Fan Lin, Xiaobo Wen, and Bo Teng. "The Structural Characteristics of Collagen in Swim Bladders with 25-Year Sequence Aging: The Impact of Age." Applied Sciences 11, no. 10 (May 17, 2021): 4578. http://dx.doi.org/10.3390/app11104578.

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Aged swim bladders from the yellow drum (Protonibea diacanthus) are considered collagen-based functional food with extremely high market value. The structural integrity of collagen may be crucial for its biological functions. In the current study, swim bladders with 25-year-old sequences were collected and found to be basically composed of collagen. Then, thermogravimetry (TG), differential scanning calorimetry (DSC), X-ray diffraction (XRD), and attenuated total reflectance–Fourier transform infrared spectroscopy (ATR–FTIR) were conducted to evaluate the integrity of the peptide chain and triple helix in the collagen. The structures of microfibers and fiber bundles were revealed with atomic force microscopy (AFM), scanning electrical microscopy (SEM), and optical spectroscopy. The collagens in the aged swim bladders were found to have similar thermal properties to those of fresh ones, but the relative content of the triple helixes was found to be negatively correlated with aging. The secondary structure of the remaining triple helix showed highly retained characteristics as in fresh swim bladders, and the microfibrils also showed a similar D-period to that of the fresh one. However, the fiber bundles displayed more compact and thick characteristics after years of storage. These results indicate that despite 25 years of aging, the collagen in the swim bladders was still partially retained with structures.

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Renugopalakrishnan, V., L. A. Carreira, T. W. Collette, J. C. Dobbs, G. Chandraksasan, and R. C. Lord. "Non-Uniform Triple Helical Structure in Chick Skin Type I Collagen on Thermal Denaturation: Raman Spectroscopic Study." Zeitschrift für Naturforschung C 53, no. 5-6 (June 1, 1998): 383–88. http://dx.doi.org/10.1515/znc-1998-5-613.

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The individual chains in the triple helix of collagen occur in a conformation related to polyproline II because of the presence of large number of imino peptide bonds. However, these residues are not evenly distributed in the collagen molecule which also contains many non-imino residues. These non-imino regions of collagen may be expected to show preference for other than triple helical conformations. The appearance of several Raman bands in solution phase at 65 °C raises the possibility of non-uniform triple helical structure in collagen. Raman spectroscopic studies on collagen in the solid state and in solution at a temperature greater than its denaturation temperature, reported here suggest that denatured collagen may exhibit an ensemble of conformational states with yet unknown implications to the biochemical interactions of this important protein component of connective tissues.

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Delsuc, N., S. Uchinomiya, A. Ojida, and I. Hamachi. "A host–guest system based on collagen-like triple-helix hybridization." Chemical Communications 53, no. 51 (2017): 6856–59. http://dx.doi.org/10.1039/c7cc03055j.

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QUAN, JUN-MIN, and YUN-DONG Wu. "A THEORETICAL STUDY OF THE SUBSTITUENT EFFECT ON THE STABILITY OF COLLAGEN." Journal of Theoretical and Computational Chemistry 03, no. 02 (June 2004): 225–43. http://dx.doi.org/10.1142/s0219633604001008.

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Theoretical calculations have been carried out to investigate the effect of the 4(R)-substituents ( OH , F , NH 2, and [Formula: see text]) in proline on the stability of the collagen triple helix. A series of substituted proline models were studied first with density functional (B3LYP/6-31+G*) calculations. The solvent effect was studied using the SCIPCM method. While the F , OH and NH 2 groups increase the stability of the trans-up conformation with respect to the trans-down conformation, [Formula: see text] appears to favor the trans-down conformation in an aqueous solution. Second, the triple helices of the tripeptide models, Ac – Pro – Pro(X) – Gly – H with the two proline residues in the down/down and down/up puckering conformations, were optimized with a repeating unit approach using the HF/6-31G* method. For the Ac – Pro – Pro – Gly – H model peptide, the calculated binding energies of the two triple helices with the different puckering modes are similar. All four substituents, F , OH , NH 2, and [Formula: see text], considerably increased the binding energy of the down/up helix, but only [Formula: see text] stabilizes the down/down triple helix. Our calculations indicate that the inter-chain electrostatic interactions involving the 4(R)-substituents play an important role in stabilizing triple helical collagen models and allow the rationalization of all available experimental observations. Further model studies indicate that the substituent effects by the F , OH and NH 2 substituents are local while the effect of [Formula: see text] is long-range in nature.

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Mrevlishvili, George M., and David V. Svintradze. "Complex between triple helix of collagen and double helix of DNA in aqueous solution." International Journal of Biological Macromolecules 35, no. 5 (June 2005): 243–45. http://dx.doi.org/10.1016/j.ijbiomac.2005.02.004.

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Maaßen, Andreas, Jan M. Gebauer, Elena Theres Abraham, Isabelle Grimm, Jörg‐Martin Neudörfl, Ronald Kühne, Ines Neundorf, Ulrich Baumann, and Hans‐Günther Schmalz. "Triple‐Helix‐Stabilizing Effects in Collagen Model Peptides Containing PPII‐Helix‐Preorganized Diproline Modules." Angewandte Chemie International Edition 59, no. 14 (February 3, 2020): 5747–55. http://dx.doi.org/10.1002/anie.201914101.

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Maaßen, Andreas, Jan M. Gebauer, Elena Theres Abraham, Isabelle Grimm, Jörg‐Martin Neudörfl, Ronald Kühne, Ines Neundorf, Ulrich Baumann, and Hans‐Günther Schmalz. "Triple‐Helix‐Stabilizing Effects in Collagen Model Peptides Containing PPII‐Helix‐Preorganized Diproline Modules." Angewandte Chemie 132, no. 14 (February 3, 2020): 5796–804. http://dx.doi.org/10.1002/ange.201914101.

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Berisio, Rita, Luigi Vitagliano, Lelio Mazzarella, and Adriana Zagari. "Recent Progress on Collagen Triple Helix Structure, Stability and Assembly." Protein & Peptide Letters 9, no. 2 (April 1, 2002): 107–16. http://dx.doi.org/10.2174/0929866023408922.

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Fields, Gregg B. "The Collagen Triple-Helix: Correlation of Conformation with Biological Activities." Connective Tissue Research 31, no. 3 (January 1995): 235–43. http://dx.doi.org/10.3109/03008209509010815.

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Journal articles on the topic 'Carbamylation of the collagen triple helix'

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