Journal articles: '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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3

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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5

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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6

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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7

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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8

Clark, C. C., and C. F. Richards. "Underhydroxylated minor cartilage collagen precursors cannot form stable triple helices." Biochemical Journal 250, no. 1 (February 15, 1988): 65–70. http://dx.doi.org/10.1042/bj2500065.

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Matrix-free cells from chick-embryo sterna were incubated with various concentrations of 2,2′-bipyridyl, an iron chelator that inhibits prolyl hydroxylase and lysyl hydroxylase. At concentrations in the region of 0.1 mM, significant effects on cartilage collagen hydroxylation and secretion were observed. When the underhydroxylated collagens were subsequently digested with chymotrypsin or chymotrypsin plus trypsin at 4 degrees C for 15 min, the minor cartilage collagen precursors (namely types IX and XI) were extensively degraded; type II procollagen was only partially susceptible and was converted into underhydroxylated collagen. The results demonstrate that there were significant differences in triple-helix stability among cartilage collagens such that the underhydroxylated minor collagen precursors were unable to attain a native structure under conditions where type II procollagen was successful.

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9

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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10

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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11

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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12

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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13

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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14

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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15

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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16

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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17

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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18

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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19

Verkleij, Marilyn W., Laurence F. Morton, C. Graham Knight, Philip G. de Groot, Michael J. Barnes, and Jan J. Sixma. "Simple Collagen-Like Peptides Support Platelet Adhesion Under Static But Not Under Flow Conditions: Interaction Via α2β1 and von Willebrand Factor With Specific Sequences in Native Collagen Is a Requirement to Resist Shear Forces." Blood 91, no. 10 (May 15, 1998): 3808–16. http://dx.doi.org/10.1182/blood.v91.10.3808.

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AbstractThe aim of this study was to define the need for specific collagen sequences and the role of their conformation in platelet adhesion to collagen under both static and flow conditions. We recently reported that simple triple-helical collagen-related peptides (CRPs), GCP*(GPP*)10GCP*G and GKP*(GPP*)10GKP*G (single-letter amino acid code, P* = hydroxyproline; Morton et al,Biochem J 306:337, 1995) were potent stimulators of platelet activation and were able to support the adhesion of gel-filtered platelets examined under static conditions. The present study investigated whether these same peptides were able to support platelet adhesion under more physiologic conditions by examining static adhesion with platelet-rich plasma (PRP) and adhesion under flow conditions. In the static adhesion assay, we observed 20% surface coverage with platelet aggregates. In marked contrast, there was a total lack of adhesion under flow conditions examined at shear rates of 50 and 300 s−1. Thus, the interaction of platelets with the CRPs is a low-affinity interaction unable on its own to withstand shear forces. However, the addition of CRPs to whole blood, in the presence of 200 μmol/L D-arginyl-glycyl-L-aspartyl-L-tryptophan (dRGDW) to prevent platelet aggregation, caused an inhibition of about 50% of platelet adhesion to collagens I and III under flow. These results suggest that the collagen triple helix per se, as defined by these simple collagen sequences, plays an important contributory role in the overall process of adhesion to collagen under flow. The monoclonal antibody (MoAb) 176D7, directed against the α2 subunit of the integrin α2β1, was found to inhibit static platelet adhesion to monomeric but not fibrillar collagens I and III. However, under flow conditions, anti-α2 MoAbs (176D7 anf 6F1) inhibited adhesion to both monomeric and fibrillar collagens, indicating that α2β1 is essential for adhesion to collagen under flow, independent of collagen conformation, whether monomeric or polymeric. To obtain further insight into the nature of the different adhesive properties of CRPs and native collagen, we investigated the relative importance of von Willebrand factor (vWF) and the integrin α2β1 in platelet adhesion to collagen types I and III, using the same shear rate (300 s−1) as used when testing CRPs under flow conditions. Our results, together with recent data of others, support a two-step mechanism of platelet interaction with collagen under flow conditions. The first step involves adhesion via both the indirect interaction of platelet glycoprotein (GP) Ib with collagen mediated by vWF binding to specific vWF-recognition sites in collagen and the direct interaction between platelet α2β1 and specific α2β1-recognition sites in collagen. This suffices to hold platelets at the collagen surface. The second step occurs via another collagen receptor (thought to be GPVI) that binds to simple collagen sequences, required essentially to delineate the collagen triple helix. Recognition of the triple helix leads to strengthening of attachment and platelet activation.

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20

Verkleij, Marilyn W., Laurence F. Morton, C. Graham Knight, Philip G. de Groot, Michael J. Barnes, and Jan J. Sixma. "Simple Collagen-Like Peptides Support Platelet Adhesion Under Static But Not Under Flow Conditions: Interaction Via α2β1 and von Willebrand Factor With Specific Sequences in Native Collagen Is a Requirement to Resist Shear Forces." Blood 91, no. 10 (May 15, 1998): 3808–16. http://dx.doi.org/10.1182/blood.v91.10.3808.3808_3808_3816.

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The aim of this study was to define the need for specific collagen sequences and the role of their conformation in platelet adhesion to collagen under both static and flow conditions. We recently reported that simple triple-helical collagen-related peptides (CRPs), GCP*(GPP*)10GCP*G and GKP*(GPP*)10GKP*G (single-letter amino acid code, P* = hydroxyproline; Morton et al,Biochem J 306:337, 1995) were potent stimulators of platelet activation and were able to support the adhesion of gel-filtered platelets examined under static conditions. The present study investigated whether these same peptides were able to support platelet adhesion under more physiologic conditions by examining static adhesion with platelet-rich plasma (PRP) and adhesion under flow conditions. In the static adhesion assay, we observed 20% surface coverage with platelet aggregates. In marked contrast, there was a total lack of adhesion under flow conditions examined at shear rates of 50 and 300 s−1. Thus, the interaction of platelets with the CRPs is a low-affinity interaction unable on its own to withstand shear forces. However, the addition of CRPs to whole blood, in the presence of 200 μmol/L D-arginyl-glycyl-L-aspartyl-L-tryptophan (dRGDW) to prevent platelet aggregation, caused an inhibition of about 50% of platelet adhesion to collagens I and III under flow. These results suggest that the collagen triple helix per se, as defined by these simple collagen sequences, plays an important contributory role in the overall process of adhesion to collagen under flow. The monoclonal antibody (MoAb) 176D7, directed against the α2 subunit of the integrin α2β1, was found to inhibit static platelet adhesion to monomeric but not fibrillar collagens I and III. However, under flow conditions, anti-α2 MoAbs (176D7 anf 6F1) inhibited adhesion to both monomeric and fibrillar collagens, indicating that α2β1 is essential for adhesion to collagen under flow, independent of collagen conformation, whether monomeric or polymeric. To obtain further insight into the nature of the different adhesive properties of CRPs and native collagen, we investigated the relative importance of von Willebrand factor (vWF) and the integrin α2β1 in platelet adhesion to collagen types I and III, using the same shear rate (300 s−1) as used when testing CRPs under flow conditions. Our results, together with recent data of others, support a two-step mechanism of platelet interaction with collagen under flow conditions. The first step involves adhesion via both the indirect interaction of platelet glycoprotein (GP) Ib with collagen mediated by vWF binding to specific vWF-recognition sites in collagen and the direct interaction between platelet α2β1 and specific α2β1-recognition sites in collagen. This suffices to hold platelets at the collagen surface. The second step occurs via another collagen receptor (thought to be GPVI) that binds to simple collagen sequences, required essentially to delineate the collagen triple helix. Recognition of the triple helix leads to strengthening of attachment and platelet activation.

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21

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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22

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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23

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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24

Ruggiero, F., J. Comte, C. Cabanas, and R. Garrone. "Structural requirements for alpha 1 beta 1 and alpha 2 beta 1 integrin mediated cell adhesion to collagen V." Journal of Cell Science 109, no. 7 (July 1, 1996): 1865–74. http://dx.doi.org/10.1242/jcs.109.7.1865.

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A large variety of cells adhere to and spread on specific regions within the triple helix of collagens, mainly via alpha 1 beta 1 and alpha 2 beta 1 integrins. Disruption of collagen triple helical integrity generally affects the efficiency of cell adhesion on different collagens including collagen V. This report addresses the question of the importance of the linear sequence of the constitutive alpha-chains versus the triple helical conformation in the recognition of collagen V binding sites. To investigate this question, in vitro renaturation of the isolated alpha 1 (V) and alpha 2 (V) chains was performed according to the annealing procedure and formation of the triple helix was monitored by rotary shadowing and by mild trypsin digestion followed by electrophoretic analysis. The results indicate that the alpha 1 (V) and alpha 2 (V) homotrimeric reassociation can occur up to a full-length triple helix but intermediate forms of 50–200 nm long rod-like segments are also observed. We have previously shown that alpha 1 beta 1 and alpha 2 beta 1 integrins, the major collagen receptors, are also involved in cell adhesion to native collagen V. Therefore we chose the following two different cell lines for this study: HT1080 (a human fibrosarcoma cell line) expressing alpha 2 beta 1 and HBL100 (a human mammary epithelial cell line) containing significant amounts of alpha 1 beta 1 and alpha 2 beta 1 integrins. We showed that both alpha 1 (V) and alpha 2(V) homotrimers induced cell adhesion but refolded alpha2(V) chains were more efficient and promoted cell adhesion as well as native collagen V. Thermal stability of refolded alpha-chains was monitored by adhesion promoting activity and showed that cell adhesion was dependent on triple helical conformation of the substrates. Adhesion in all cases was strongly Mg2+ and Mn(2+)-dependent and Ca2+ ions alone were ineffective. Antibodies against alpha 2 and beta 1 integrin subunits completely inhibited HT1080 cell adhesion to all substrates. Moreover, addition of cyclic RGD peptides, which had been shown to interact with alpha 2 beta 1, dramatically affected HT1080 cell adhesion to native collagen V and to the refolded alpha-chains. Antibody to beta 1 subunits abolished HBL100 cell adhesion to all substrates. A complete inhibition of HBL100 cell adhesion to native collagen V was achieved only by simultaneous addition of function-blocking specific monoclonal antibodies against alpha 1 and alpha 2 integrin subunits. However, only alpha 2 beta 1 was engaged obviously in HBL100 cell adhesion to refolded alpha-chains. These data indicate that triple helical conformation is particularly critical for alpha 2 beta 1- and alpha 1 beta 1-dependent adhesion and that the integrin alpha 2 beta 1 is a dominant functional receptor for refolded alpha-chains. We conclude that alpha 2 beta 1-dependent adhesion seems to involve multiple different conformational binding sites while alpha 1 beta 1-dependent adhesion is more restricted to the heterotrimeric native form of the molecule.

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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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26

Ge, Baolin, Chunyu Hou, Bin Bao, Zhilin Pan, José Eduardo Maté Sánchez de Val, Jeevithan Elango, and Wenhui Wu. "Comparison of Physicochemical and Structural Properties of Acid-Soluble and Pepsin-Soluble Collagens from Blacktip Reef Shark Skin." Marine Drugs 20, no. 6 (June 2, 2022): 376. http://dx.doi.org/10.3390/md20060376.

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Fish collagen has been widely used in tissue engineering (TE) applications as an implant, which is generally transplanted into target tissue with stem cells for better regeneration ability. In this case, the success rate of this research depends on the fundamental components of fish collagen such as amino acid composition, structural and rheological properties. Therefore, researchers have been trying to find an innovative raw material from marine origins for tissue engineering applications. Based on this concept, collagens such as acid-soluble (ASC) and pepsin-soluble (PSC) were extracted from a new type of cartilaginous fish, the blacktip reef shark, for the first time, and were further investigated for physicochemical, protein pattern, microstructural and peptide mapping. The study results confirmed that the extracted collagens resemble the protein pattern of type-I collagen comprising the α1, α2, β and γ chains. The hydrophobic amino acids were dominant in both collagens with glycine and hydroxyproline as major amino acids. From the FTIR spectra, α helix (27.72 and 26.32%), β-sheet (22.24 and 23.35%), β-turn (21.34 and 22.08%), triple helix (14.11 and 14.13%) and random coil (14.59 and 14.12%) structures of ASC and PSC were confirmed, respectively. Collagens retained their triple helical and secondary structure well. Both collagens had maximum solubility at 3% NaCl and pH 4, and had absorbance maxima at 234 nm, respectively. The peptide mapping was almost similar for ASC and PSC at pH 2, generating peptides ranging from 15 to 200 kDa, with 23 kDa as a major peptide fragment. The microstructural analysis confirmed the homogenous fibrillar nature of collagens with more interconnected networks. Overall, the preset study concluded that collagen can be extracted more efficiently without disturbing the secondary structure by pepsin treatment. Therefore, the blacktip reef shark skin could serve as a potential source for collagen extraction for the pharmaceutical and biomedical applications.

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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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28

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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29

Keene, D. R., L. Y. Sakai, H. P. Bächinger, and R. E. Burgeson. "Type III collagen can be present on banded collagen fibrils regardless of fibril diameter." Journal of Cell Biology 105, no. 5 (November 1, 1987): 2393–402. http://dx.doi.org/10.1083/jcb.105.5.2393.

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Monoclonal antibodies that recognize an epitope within the triple helix of type III collagen have been used to examine the distribution of that collagen type in human skin, cornea, amnion, aorta, and tendon. Ultrastructural examination of those tissues indicates antibody binding to collagen fibrils in skin, amnion, aorta, and tendon regardless of the diameter of the fibril. The antibody distribution is unchanged with donor age, site of biopsy, or region of tissue examined. In contrast, antibody applied to adult human cornea localizes to isolated fibrils, which appear randomly throughout the matrix. These studies indicate that type III collagen remains associated with collagen fibrils after removal of the amino and carboxyl propeptides, and suggests that fibrils of skin, tendon, and amnion (and presumably many other tissues that contain both types I and III collagens) are copolymers of at least types I and III collagens.

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30

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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31

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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32

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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33

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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34

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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35

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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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 (June 1991): 152–56. http://dx.doi.org/10.1016/0141-8130(91)90040-2.

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38

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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39

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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40

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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41

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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42

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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43

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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44

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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45

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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46

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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47

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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48

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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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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50

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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Journal articles on the topic 'Collagen triple helix'

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