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

Author: Grafiati

Published: 29 March 2025

Last updated: 31 July 2025

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1

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

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2

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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3

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 (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)

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4

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 (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 be

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5

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 (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 st

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6

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 (2006): 458–67. http://dx.doi.org/10.7124/bc.00074d.

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7

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 (2006): 4735–38. http://dx.doi.org/10.1021/ol061771w.

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8

Baker, A. T., J. A. M. Ramshaw, D. Chan, W. G. Cole та 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, № 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 abn

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9

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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10

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 (2004): 38072–78. http://dx.doi.org/10.1074/jbc.m402953200.

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11

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

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12

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

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13

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

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14

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

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15

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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16

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

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17

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

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18

Walker, Kenneth T., Ruodan Nan, David W. Wright, et al. "Non-linearity of the collagen triple helix in solution and implications for collagen function." Biochemical Journal 474, no. 13 (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 pept

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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 (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 c

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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 (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 obser

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22

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 (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

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23

Pan, Hao, Xuehua Zhang, Jianbo Ni, et al. "Effects of Ultrasonic Power on the Structure and Rheological Properties of Skin Collagen from Albacore (Thunnus alalunga)." Marine Drugs 22, no. 2 (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 structu

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24

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 (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 typ

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25

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 (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 exp

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26

Nagai, Naoko, Masanori Hosokawa, Shigeyoshi Itohara, et al. "Embryonic Lethality of Molecular Chaperone Hsp47 Knockout Mice Is Associated with Defects in Collagen Biosynthesis." Journal of Cell Biology 150, no. 6 (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 mol

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27

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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28

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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29

Schwob, Lucas, Mathieu Lalande, Jimmy Rangama, et al. "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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30

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

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31

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

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32

Li, Y., C. A. Foss, D. D. Summerfield, et al. "Targeting collagen strands by photo-triggered triple-helix hybridization." Proceedings of the National Academy of Sciences 109, no. 37 (2012): 14767–72. http://dx.doi.org/10.1073/pnas.1209721109.

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33

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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34

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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35

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

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36

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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37

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

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38

Kusebauch, Ulrike, Sergio A. Cadamuro, Hans-Jürgen Musiol, et al. "Photocontrolled Folding and Unfolding of a Collagen Triple Helix." Angewandte Chemie International Edition 45, no. 42 (2006): 7015–18. http://dx.doi.org/10.1002/anie.200601432.

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39

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

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40

Yang, Ke, Jing Sun, Dan Wei, et al. "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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41

Hartmann, Julian, and Martin Zacharias. "Mechanism of collagen folding propagation studied by Molecular Dynamics simulations." PLOS Computational Biology 17, no. 6 (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

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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 (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 tri

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43

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 (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 s

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44

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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45

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 (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 tri

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46

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 (2005): 243–45. http://dx.doi.org/10.1016/j.ijbiomac.2005.02.004.

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47

Maaßen, Andreas, Jan M. Gebauer, Elena Theres Abraham, et al. "Triple‐Helix‐Stabilizing Effects in Collagen Model Peptides Containing PPII‐Helix‐Preorganized Diproline Modules." Angewandte Chemie International Edition 59, no. 14 (2020): 5747–55. http://dx.doi.org/10.1002/anie.201914101.

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48

Maaßen, Andreas, Jan M. Gebauer, Elena Theres Abraham, et al. "Triple‐Helix‐Stabilizing Effects in Collagen Model Peptides Containing PPII‐Helix‐Preorganized Diproline Modules." Angewandte Chemie 132, no. 14 (2020): 5796–804. http://dx.doi.org/10.1002/ange.201914101.

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49

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 (2002): 107–16. http://dx.doi.org/10.2174/0929866023408922.

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50

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

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