Hydrolyzed Collagen Powder (Bovine) New

Hydrolyzed Collagen Powder (Bovine)

Derived from the Greek word Kolla which means glue, collagen is the most abundant type of protein found in the human body. This is a food that has been used for thousands of years for its nourishing and healing qualities. One of the more unspoken about superfoods is bone broth which provides you all the nourishment from the typically uneaten parts of the animal (cartilage, bones and hides).

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This type of collagen and the healing qualities it provides us is very similar to the collagen we have in our own body. Our grass fed hydrolyzed collagen tested at 90% protein provides us with both type I and type III collagen which is the major component in skin, hair, nails, muscles, tendons, ligaments, bones, gums, teeth, eyes and blood vessels.

Hydrolyzed collagen is a true superstar food which offers a highly nourishing level of specific amino acids known for their ability to rebuild and repair. One of the more common reasons collagen is used to nourish and support a healthy body is that it may support joint, tendon and cartilage health. Many of the popular supplements on the market today for joint health like glucosamine, chondroitin and msm are all naturally contained within the cartilage and bones of animals. Also, the amino acids which may help to form collagen in the human body like glycine, proline, and lysine are found in highly nourishing amounts in hydrolyzed collagen. One specific study showed that a diet rich in glycine improved both biochemical and biomechanical properties following inflammation of the achilles tendon. It is thought that glycine has positive effects against toxicity and may support a healthy inflammation response. Glycine may restructure the collagen molecules faster due to its possible broad effects on the inflammation process. This study had 3 groups (control, inflammatory group and glycine+inflammatory group). Higher concentrations of hydroxyproline and glycosaminoglycans were found in the glycine inflammation group. The biomechanical results indicated that the tendon was more resistant to loading to rupture upon treatment with a glycine diet in that specific group. The conclusion was drawn that “Glycine induced the synthesis of important components of the tendon”.

Another study (double blind, placebo controlled) done at Penn state university that was conducted for 24 weeks showing the possible joint health benefits of ingesting 10 grams of collagen daily in active athletes. This study had 147 subjects (72 men and 75 women) where one group received a formula with 10 grams of collagen and the other a xanthan. The study was looking at pain, mobility and inflammation. At the completion of the study 5 parameters (joint pain while walking, at rest, standing, carrying objects, and lifting) showed significant changes with the group that took the collagen. The results of this study have implications for the use of collagen to support joint health and possibly reduce the risk of joint deterioration in a high-risk group. The results also suggest that athletes consuming collagen can also prevent and support specific parameters (like pain) that may have a direct effect on the athlete’s performance.

Finally, because of collagens unique amino acid profile this food is a wonderful way to possibly support gut health. The 18 amino acids found in collagen may help to support and repair an unhealthy gut lining. Amino acids may increase gastric acid secretion which in turn may help those with reflux issues. The amino acids lysine and proline have been shown to also possibly support and protect the stomach lining from injury. Finally the superstar amino acid glutamine has been shown in many studies its ability to possibly improve digestion and heal the gut. This amino acid is a staple for those who have been diagnosed with a condition known as “leaky gut”. Therefore the implications for its use in supporting a healthy immune and allergy response shows great potential.

Some possible traditional uses of Hydrolyzed Collagen Powder (Bovine) may include:
  • Grass fed and Tested at 90% protein
  • May support joint health
  • May support a healthy inflammation response
  • May support a healthy immune response
  • May support a healthy allergy response
  • May support gut health
  • May support muscle and tissue recovery
  • May support skin health

Constituents in Hydrolyzed Collagen Powder (Bovine) include:
  • Protein, amino acids, collagen type l and lll

This product is 100% natural and minimally processed. Taste, smell, texture, and color may vary from batch to batch.

Suggested Use: Mix 4.5 level tablespoons / 1 ounce (28 grams ) with 12 ounces of cold water, skim milk or juice and thoroughly mix in a blender, shaker or with a fork for 20-30 seconds. For best results, consume 1-2 servings daily, with one serving post exercise. Can also be blended into your favorite smoothie.

Mixing suggestion: To make a delicious smoothie, mix with our 100% pure cacao and gelatinized maca root powder. Can also be added to coffee to make a great high protein coffee.

Other Names: Collagen Protein, Collagen Hydrolysate, Collagen Hydrolysis, Collagen Hydrolyzed.

Parts Used: Grass-fed Bovine Hide.

Ingredients: Hydrolyzed Collagen (Bovine source).

Origin: Raised and processed in Argentina. Packaged with care in Florida, USA.

Z Natural Foods strives to offer the highest quality organically grown, raw, vegan, gluten free, non-GMO products available and exclusively uses low temperature drying techniques to preserve all the vital enzymes and nutrients. Our Hydrolyzed Collagen Powder (Bovine) passes our strict quality assurance which includes testing for botanical identity, chemicals, and microbiological contaminants. ZNaturalFoods.com offers Hydrolyzed Collagen Powder (Bovine) packaged in airtight stand-up, resealable foil pouches for optimum freshness. Once opened, just push the air out of the pouch before resealing it in order to preserve maximum potency. We recommend refrigerating your Hydrolyzed Collagen Powder (Bovine) to maintain freshness.
1. Brinckmann J. Collagens at a glance. Top. Curr. Chem. 2005;247:1–-6.

2. Veit G, Kobbe B, Keene DR, Paulsson M, Koch M, Wagener R. Collagen XXVIII, a novel von Willebrand factor A domain-containing protein with many imperfections in the collagenous domain. J. Biol. Chem. 2006;281:3494–3504.

3. Schweitzer MH, Suo Z, Avci R, Asara JM, Allen MA, et al. Analyses of soft tissue from Tyrannosaurus rex suggest the presence of protein. Science. 2007;316:277–280.

4. Asara JM, Schweitzer MH, Freimark LM, Phillips M, Cantley LC. Protein sequences from mastodon and Tyrannosaurus rex revealed by mass spectrometry. Science. 2007;316:280–285.

5. Buckley M, Walker A, Ho SYW, Yang Y, Smith C, et al. Comment on “Protein sequences from mastodon and Tyrannosaurus rex revealed by mass spectrometry.” Science. 2008;319:333.

6. Pevzner PA, Kim S, Ng J. Comment on “Protein sequences from mastodon and Tyrannosaurus rex revealed by mass spectrometry.” Science. 2008;321:1040.

7. Berisio R, Vitagliano L, Mazzarella L, Zagari A. Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3. Protein Sci. 2002;11:262–270.

8. Brazel D, Oberbäumer I, Dieringer H, Babel W, Glanville RW, et al. Completion of the amino acid sequence of the a1 chain of human basement membrane collagen (type IV) reveals 21 nontriplet interruptions located within the collagenous domain. Eur. J. Biochem. 1987;168:529–536.

9. Ramshaw JAM, Shah NK, Brodsky B. Gly-X-Y tripeptide frequencies in collagen: a context for host-guest triple-helical peptides. J. Struct. Biol. 1998;122:86–91.

10. Fitzgerald J, Rich C, Zhou FH, Hansen U. Three novel collagen VI chains, a4(VI), a5(VI), and a6(VI) J. Biol. Chem. 2008;283:20170–20180.

11. Astbury WT, Bell FO. The molecular structure of the fibers of the collagen group. Nature. 1940;145:421–422.

12. Pauling L, Corey RB. The structure of fibrous proteins of the collagen-gelatin group. Proc. Natl. Acad. Sci. USA. 1951;37:272–281.

13. Ramachandran GN, Kartha G. Structure of collagen. Nature. 1954;174:269–270.

14. Ramachandran GN, Kartha G. Structure of collagen. Nature. 1955;176:593–595.

15. Rich A, Crick FHC. The structure of collagen. Nature. 1955;176:915–916.

17. Cowan PM, McGavin S, North ACT. The polypeptide chain configuration of collagen. Nature. 1955;176:1062–1064.

16. Rich A, Crick FHC. The molecular structure of collagen. J. Mol. Biol. 1961;3:483–-506.

18. Fields GB, Prockop DJ. Perspectives on the synthesis and application of triple-helical, collagen-model peptides. Biopolymers. 1996;40:345–357.

19. Bella J, Eaton M, Brodsky B, Berman HM. Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution. Science. 1994;266:75–81. NOTE: First high-resolution (1.9-Å) crystal structure of a collagen triple helix, formed from CRPs.

20. Bella J, Berman HM. Crystallographic evidence for Ca-H–O=C hydrogen bonds in a collagen triple helix. J. Mol. Biol. 1996;264:734–742.

21. Kramer RZ, Venugopal MG, Bella J, Mayville P, Brodsky B, Berman HM. Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair. J. Mol. Biol. 2000;301:1191–1205.

22. Emsley J, Knight CG, Farndale RW, Barnes MJ, Liddington RC. Structural basis of collagen recognition by integrin a2ß1. Cell. 2000;101:47–-56.

23. Cohen C, Bear RS. Helical polypeptide chain configuration in collagen. J. Am. Chem. Soc. 1953;75:2783–2784.

24. Okuyama K, Xu X, Iguchi M, Noguchi K. Revision of collagen molecular structure. Biopolymers. 2006;84:181–191.

25. Kramer RZ, Bella J, Mayville P, Brodsky B, Berman HM. Sequence dependent conformational variations of collagen triple-helical structure. Nat. Struct. Biol. 1999;6:454–457.

26. Boudko S, Engel J, Okuyama K, Mizuno K, Bächinger HP, Schumacher MA. Crystal structure of human type III collagen G991–G1032 cystine knot-containing peptide shows both 7/2 and 10/3 triple helical symmetries. J. Biol. Chem. 2008;283:32580–32589.

27. Sweeney SM, Guy CA, Fields GB, San Antonio JD. Defining the domains of type I collagen involved in heparin-binding and endothelial tube formation. Proc. Natl. Acad. Sci. USA. 1998;95:7275–7280.

28. Di Lullo GA, Sweeney SM, Körkkö J, Ala-Kokko L, San Antonio JD. Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen. J. Biol. Chem. 2002;277:4223–4231.

29. Sweeney SM, Orgel JP, Fertala A, McAuliffe JD, Turner KR, et al. Candidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebrates. J. Biol. Chem. 2008;283:21187–21197. NOTE: Thorough analysis of the cell interaction and matrix interaction domains of the collagen fibrils.

30. Jenkins CL, Vasbinder MM, Miller SJ, Raines RT. Peptide bond isosteres: ester or (E)-alkene in the backbone of the collagen triple helix. Org. Lett. 2005;7:2619–2622.

31. Boryskina OP, Bolbukh TV, Semenov MA, Gasan AI, Maleev VY. Energies of peptide-peptide and peptide-water hydrogen bonds in collagen: evidences from infrared spectroscopy, quartz piezogravimetry, and differential scanning calorimetry. J. Mol. Struct. 2007;827:1–10.

32. Myllyharju J, Kivirikko KI. Collagens and collagen-related diseases. Ann. Med. 2001;33:7–21.

33. Beck K, Chan VC, Shenoy N, Kirkpatrick A, Ramshaw JAM, Brodsky B. Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine. Proc. Natl. Acad. Sci. USA. 2000;97:4273–4278.

34. Tsai MI-H, Xu Y, Dannenberg JJ. Completely geometrically optimized DFT/ONIOM triple-helical collagen-like structures containing the ProProGly, ProProAla, ProProDAla, and ProProDSer triads. J. Am. Chem. Soc. 2005;127:14130–14131.

35. Horng J-C, Kotch FW, Raines RT. Is glycine a surrogate for a d-amino acid in the collagen triple helix? Protein Sci. 2007;16:208–215.

36. Bodian DL, Madhan B, Brodsky B, Klein TE. Predicting the clinical lethality of osteogenesis imperfecta from collagen glycine mutations. Biochemistry. 2008;47:5424–5432.

37. Hyde TJ, Bryan MA, Brodsky B, Baum J. Sequence dependence of renucleation after a Gly mutation in model collagen peptides. J. Biol. Chem. 2006;281:36937–36943.

38. Khoshnoodi J, Cartailler J-P, Alvares K, Veis A, Hudson BG. Molecular recognition in the assembly of collagens: Terminal noncollagenous domains are key recognition modules in the formation of triple-helical protomers. J. Biol. Chem. 2006;281:38117–38121.

39. Raghunath M, Bruckner P, Steinmann B. Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta. J. Mol. Biol. 1994;236:940–949.

40. Cram DJ. The design of molecular hosts, guests, and their complexes. Science. 1988;240:760–767.

41. Kersteen EA, Raines RT. Contribution of tertiary amides to the conformational stability of collagen triple helices. Biopolymers. 2001;59:24–28.

42. Nan D, Wang XJ, Etzkorn FA. The effect of a trans-locked Gly–Pro alkene isostere on collagen triple helix stability. J. Am. Chem. Soc. 2008;130:5396–5397.

43. Friedman L, Higgin JJ, Moulder G, Barstead R, Raines RT, Kimble J. Prolyl 4-hydroxylase is required for viability and morphogenesis in Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA. 2000;97:4736–4741. NOTE: Demonstration that 4R-hydroxylation of Pro residues in the Yaa position of collagen strands is required for animal life.

44. Holster T, Pakkanen O, Soininen R, Sormunen R, Nokelainen M, et al. Loss of assembly of the main basement membrane collagen, type IV, but not fibril-forming collagens and embryonic death in collagen prolyl 4-hydroxylase I null mice. J. Biol. Chem. 2007;282:2512–2519.

45. Berg RA, Prockop DJ. The thermal transition of a nonhydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple helix of collagen. Biochem. Biophys. Res. Commun. 1973;52:115–120.

46. Sakakibara S, Inouye K, Shudo K, Kishida Y, Kobayashi Y, Prockop DJ. Synthesis of (Pro–Hyp–Gly)n of defined molecular weights. Evidence for the stabilization of collagen triple helix by hydroxyproline. Biochim. Biophys. Acta. 1973;303:198–-202.

47. Inouye K, Sakakibara S, Prockop DJ. Effects of the stereo-configuration of the hydroxyl group in 4-hydroxyproline on the triple-helical structures formed by homogenous peptides resembling collagen. Biochim. Biophys. Acta. 1976;420:133–141.

48. Jiravanichanun N, Nishino N, Okuyama K. Conformation of alloHyp in the Y position in the host-guest peptide with the Pro-Pro-Gly sequence: implication of the destabilization of (Pro-alloHyp-Gly)10. Biopolymers. 2006;81:225–233.

49. Suzuki E, Fraser RDB, MacRae TP. Role of hydroxyproline in the stabilization of the collagen molecule via water molecules. Int. J. Biol. Macromol. 1980;2:54–56.

50. Bella J, Brodsky B, Berman HM. Hydration structure of a collagen peptide. Structure. 1995;3:893–906.

51. Dunitz JD, Taylor R. Organic fluorine hardly ever accepts hydrogen bonds. Chem. Eur. J. 1997;3:89–98.

52. Holmgren SK, Taylor KM, Bretscher LE, Raines RT. Code for collagen’s stability deciphered. Nature. 1998;392:666–667. NOTE: Overturned the long-standing hypothesis that water bridges are important for the structure and stability of the collagen triple helix.

53. Holmgren SK, Bretscher LE, Taylor KM, Raines RT. A hyperstable collagen mimic. Chem. Biol. 1999;6:63–70.

54. Bretscher LE, Jenkins CL, Taylor KM, DeRider ML, Raines RT. Conformational stability of collagen relies on a stereoelectronic effect. J. Am. Chem. Soc. 2001;123:777–778.

55. Gilli G. Molecules and molecular crystals. In: Giacovazzo C, editor. Fundamentals of Crystallography. Oxford, UK: Oxford Univ. Press; 2002. pp. 618–625.

56. DeRider ML, Wilkens SJ, Waddell MJ, Bretscher LE, Weinhold F, et al. Collagen stability: insights from NMR spectroscopic and hybrid density functional computational investigations of the effect of electronegative substituents on prolyl ring conformations. J. Am. Chem. Soc. 2002;124:2497–2505.

57. Panasik N, Jr, Eberhardt ES, Edison AS, Powell DR, Raines RT. Inductive effects on the structure of proline residues. Int. J. Pept. Protein Res. 1994;44:262–269.

58. Improta R, Benzi C, Barone V. Understanding the role of stereoelectronic effects in determining collagen stability. 1. A quantum mechanical study of proline, hydroxyproline, and fluoroproline dipeptide analogues in aqueous solution. J. Am. Chem. Soc. 2001;123:12568–12577.

59. Kotch FW, Guzei IA, Raines RT. Stabilization of the collagen triple helix by O-methylation of hydroxyproline residues. J. Am. Chem. Soc. 2008;130:2952–2953.

60. Lee S-G, Lee JY, Chmielewski J. Investigation of pH-dependent collagen triple-helix formation. Angew. Chem. Int. Ed. Engl. 2008;47:8429–8432.

61. Shoulders MD, Guzei IA, Raines RT. 4-Chloroprolines: synthesis, conformational analysis, and effect on the collagen triple helix. Biopolymers. 2008;89:443–454.

62. Persikov AV, Ramshaw JAM, Kirkpatrick A, Brodsky B. Triple-helix propensity of hydroxyproline and fluoroproline: comparison of host-guest and repeating tripeptide models. J. Am. Chem. Soc. 2003;125:11500–11501.

63. Malkar NB, Lauer-Fields JL, Borgia JA, Fields GB. Modulation of triple-helical stability and subsequent melanoma cellular responses by single-site substitution of fluoroproline derivatives. Biochemistry. 2002;41:6054–6064.

64. Nishi Y, Uchiyama S, Doi M, Nishiuchi Y, Nakazawa T, et al. Different effects of 4-hydroxyproline and 4-fluoroproline on the stability of the collagen triple helix. Biochemistry. 2005;44:6034–6042.

65. Shoulders MD, Hodges JA, Raines RT. Reciprocity of steric and stereoelectronic effects in the collagen triple helix. J. Am. Chem. Soc. 2006;128:8112–8113.

66. Cadamuro SA, Reichold R, Kusebauch U, Musiol H-J, Renner C, et al. Conformational properties of 4-mercaptoproline and related derivatives. Angew. Chem. Int. Ed. Engl. 2008;47:2143–2146.

67. Vitagliano L, Berisio R, Mazzarella L, Zagari A. Structural bases of collagen stabilization induced by proline hydroxylation. Biopolymers. 2001;58:459–464.

68. Hodges JA, Raines RT. Stereoelectronic effects on collagen stability: the dichotomy of 4-fluoroproline diastereomers. J. Am. Chem. Soc. 2003;125:9262–9263.

69. Doi M, Nishi Y, Uchiyama S, Nishiuchi Y, Nakazawa T, et al. Characterization of collagen model peptides containing 4-fluoroproline; (4(S)-fluoroproline–Pro–Gly)10 forms a triple helix, but (4(R)-fluoroproline–Pro–Gly)10 does not. J. Am. Chem. Soc. 2003;125:9922–9923.

70. Barth D, Milbradt AG, Renner C, Moroder L. A (4R)- or a (4S)-fluoroproline residue in position Xaa of the (Xaa–Yaa–Gly) collagen repeat severely affects triple-helix formation. ChemBioChem. 2004;5:79–86.

71. Lesarri A, Cocinero EJ, López JC, Alonso JL. Shape of 4S- and 4R-hydroxyproline in gas phase. J. Am. Chem. Soc. 2005;127:2572–2579.

72. Kefalides NA. Structure and biosynthesis of basement membranes. Int. Rev. Connect. Tissue Res. 1973;6:63–104.

73. Jenkins CL, Bretscher LE, Guzei IA, Raines RT. Effect of 3-hydroxyproline residues on collagen stability. J. Am. Chem. Soc. 2003;125:6422–6427.

74. Tryggvason K, Risteli J, Kivirikko K. Separation of prolyl 3-hydroxylase and 4-hydroxylase activities and the 4-hydroxyproline requirement for synthesis of 3-hydroxyproline. Biochem. Biophys. Res. Commun. 1976;76:275–281.

75. Morello R, Bertin TK, Chen Y, Hicks J, Tonachini L, et al. CRTAP is required for prolyl 3-hydroxylation and mutations cause recessive osteogenesis imperfecta. Cell. 2006;127:291–304.

76. Cabral WA, Chang W, Barnes AM, Weis M, Scott MA, et al. Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta. Nat. Genet. 2007;39:359–365.

77. Mizuno K, Peyton DH, Hayashi T, Engel J, Bächinger HP. Effect of the -Gly-3(S)-hydroxyprolyl-4(R)-hydroxyprolyl-tripeptide unit on the stability of collagen model peptides. FEBS J. 2008;275:5830–5840.

78. Schumacher MA, Mizuno K, Bächinger HP. The crystal structure of a collagen-like polypeptide with 3(S)-hydroxyproline residues in the Xaa position forms a standard 7/2 collagen triple helix. J. Biol. Chem. 2006;281:27566–27574.

79. Hodges JA, Raines RT. Stereoelectronic and steric effects in the collagen triple helix: toward a code for strand association. J. Am. Chem. Soc. 2005;127:15923–15932.

80. Sarkar SK, Young PE, Sullivan CE, Torchia DA. Detection of cis and trans X-Pro bonds in proteins by 13C NMR: application to collagen. Proc. Natl. Acad. Sci. USA. 1984;81:4800–4803.

81. Hinderaker MP, Raines RT. An electronic effect on protein structure. Protein Sci. 2003;12:1188–1194.

82. Jenkins CL, Lin G, Duo J, Rapolu D, Guzei IA, et al. Substituted 2-azabicyclo[2.1.1]hexanes as constrained proline analogues: implications for collagen stability. J. Org. Chem. 2004;69:8565–8573.

83. Hodges JA, Raines RT. Energetics of an n?p* interaction that impacts protein structure. Org. Lett. 2006;8:4695–4697.

84. Inouye K, Kobayashi Y, Kyogoku Y, Kishida Y, Sakakibara S, Prockop DJ. Synthesis and physical properties of (hydroxyproline-proline-glycine)10. Hydroxyproline in the X-position decreases the melting temperature of the collagen triple helix. Arch. Biochem. Biophys. 1982;219:198–203.

85. Berisio R, Granata V, Vitagliano L, Zagari A. Imino acids and collagen triple helix stability: Characterization of collagen-like polypeptides containing Hyp-Hyp-Gly sequence repeats. J. Am. Chem. Soc. 2004;126:11402–11403.

86. Mizuno K, Hayashi T, Peyton DH, Bächinger HP. Hydroxylation-induced stabilization of the collagen triple helix. J. Biol. Chem. 2004;279:38072–38078.

87. Kawahara K, Nishi Y, Nakamura S, Uchiyama S, Nishiuchi Y, et al. Effect of hydration on the stability of the collagen-like triple-helical structure of [4(R)-hydroxyprolyl-4(R)-hydroxyprolylglycine]10. Biochemistry. 2005;44:15812–15822.

88. Schumacher M, Mizuno K, Bächinger HP. The crystal structure of the collagen-like polypeptide (glycyl-4(R)-hydroxyprolyl-4(R)-hydroxyprolyl)9 at 1.55 angstrom resolution shows up-puckering of the proline ring in the Xaa position. J. Biol. Chem. 2005;280:20397–20403.

89. Buechert DD, Paolella DN, Leslie BS, Brown MS, Mehos KA, Gruskin EA. Co-translational incorporation of trans-4-hydroxyproline into recombinant proteins in bacteria. J. Biol. Chem. 2003;278:645–650.

90. Mann K, Mechling DE, Bächinger HP, Eckerskorn C, Gaill F, Timpl R. Glycosylated threonine but not 4-hydroxyproline dominates the triple helix stabilizing positions in the sequence of a hydrothermal vent worm cuticle collagen. J. Mol. Biol. 1996;261:255–266.

91. Bann JG, Bächinger HP. Glycosylation/hydroxylation-induced stabilization of the collagen triple helix: 4-trans-hydroxyproline in the Xaa position can stabilize the triple helix. J. Biol. Chem. 2000;275:24466–24469.

92. Mizuno K, Hayashi T, Bächinger HP. Hydroxylation-induced stabilization of the collagen triple helix. J. Biol. Chem. 2003;278:32373–32379.

93. Improta R, Berisio R, Vitagliano L. Contribution of dipole-dipole interactions to the stability of the collagen triple helix. Protein Sci. 2008;2008:955–961.

94. Doi M, Nishi Y, Uchiyama S, Nishiuchi Y, Nishio H, et al. Collagen-like triple helix formation of synthetic (Pro-Pro-Gly)10 analogues: (4(S)-hydroxyprolyl-4(R)-hydroxyprolyl-Gly)10 and (4(S)-fluoroprolyl-4(R)-fluoroprolyl-Gly)10. J. Pept. Sci. 2005;11:609–616.

95. Gauba V, Hartgerink JD. Self-assembled heterotrimeric collagen triple helices directed through electrostatic interactions. J. Am. Chem. Soc. 2007;129:2683–2690. NOTE: Formation of a 1:1:1 heterotrimeric triple-helix from a positively charged, a negatively charged, and a neutral CRP.

96. Gauba V, Hartgerink JD. Surprisingly high stability of collagen ABC heterotrimer: evaluation of side chain charge pairs. J. Am. Chem. Soc. 2007;129:15034–15041.

97. Gauba V, Hartgerink JD. Synthetic collagen heterotrimers: structural mimics of wild-type and mutant collagen type I. J. Am. Chem. Soc. 2008;130:7509–7515.

98. Persikov AV, Ramshaw JAM, Kirkpatrick A, Brodsky B. Amino acid propensities for the collagen triple helix. Biochemistry. 2000;39:14960–14967.

99. Yang W, Chan VC, Kirkpatrick A, Ramshaw JAM, Brodsky B. Gly–Pro–Arg confers stability similar to Gly–Pro–Hyp in the collagen triple-helix of host-guest peptides. J. Biol. Chem. 1997;272:28837–28840.

100. Persikov AV, Ramshaw JAM, Brodsky B. Prediction of collagen stability from amino acid sequence. J. Biol. Chem. 2005;280:19343–19349.

101. Leikina E, Mertts MV, Kuznetsova N, Leikin S. Type I collagen is thermally unstable at body temperature. Proc. Natl. Acad. Sci. USA. 2002;99:1314–1318.

102. Buehler MJ. Nature designs tough collagen: explaining the nanostructure of collagen fibrils. Proc. Natl. Acad. Sci. USA. 2006;103:12285–12290. NOTE: Analysis of the molecular evolution of collagen fibrils for the purpose of achieving maximal strength and flexibility.

103. Kadler KE, Holmes DF, Trotter JA, Chapman JA. Collagen fibril formation. Biochem. J. 1996;316:1–11.

104. Birk DE, Zycband EI, Winkelmann DA, Trelstad RL. Collagen fibrillogenesis in situ: Fibril segments are intermediates in matrix assembly. Proc. Natl. Acad. Sci. USA. 1989;86:4549–4553.

105. Holmes DF, Kadler KE. The 10+4 microfibril structure of thin cartilage fibrils. Proc. Natl. Acad. Sci. USA. 2006;103:17249–17254. NOTE: Highest-resolution structure (~4 nm) of thin cartilage fibrils determined to date.

106. Craig AS, Birtles MJ, Conway JF, Parry DA. An estimate of the mean length of collagen fibrils in rat tail tendon as a function of age. Connect. Tissue Res. 1989;19:51–62.

107. Hodge AJ, Petruska JA. Recent studies with the electron microscope on ordered aggregates of the tropocollagen macromolecule. In: Ramachandran GN, editor. Aspects of Protein Structure. London: Academic Press; 1963. pp. 289–300.

108. Hulmes DJS, Miller A. Quasi-hexagonal molecular packing in collagen fibrils. Nature. 1979;282:878–880.

109. Trus BL, Piez KA. Compressed microfibril models of the native collagen fibril. Nature. 1980;286:300–301.

110. Hulmes DJS, Jesior J-C, Miller A, Berthet-Colominas C, Wolff C. Electron microscopy shows periodic structure in collagen fibril cross sections. Proc. Natl. Acad. Sci. USA. 1981;78:3567–3571.

111. Bozec L, van der Heijden G, Horton M. Collagen fibrils: nanoscale ropes. Biophys. J. 2007;92:70–75.

112. Orgel JPRO, Miller A, Irving TC, Fischetti RF, Hammersley AP, Wess TJ. The in situ supermolecular structure of type I collagen. Structure. 2001;9:1061–1069.

113. Orgel JPRO, Irving TC, Miller A, Wess TJ. Microfibrillar structure of type I collagen in situ. Proc. Natl. Acad. Sci. USA. 2006;103:9001–9005. NOTE: Structure of a type I collagen microfibril at molecular anisotropic resolution (5.16-Å axial; 11.1-Å equatorial).

114. Orgel JP, Wess TJ, Miller A. The in situ conformation and axial location of the intermolecular cross-linked nonhelical telopeptides of type I collagen. Structure. 2000;8:137–142.

115. Perumal S, Olga A, Orgel JPRO. Collagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysis. Proc. Natl. Acad. Sci. USA. 2008;105:2824–2829.

116. Kadler KE, Hojima Y, Prockop DJ. Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. J. Biol. Chem. 1987;262:15696–15701.

117. Prockop DJ, Fertala A. Inhibition of the self-assembly of collagen I into fibrils with synthetic peptides. J. Biol. Chem. 1998;273:15598–15604.

118. Kuznetsova N, Leikin S. Does the triple helical domain of type I collagen encode molecular recognition and fiber assembly while telopeptides serve as catalytic domains? J. Biol. Chem. 1999;274:36083–36088.

119. Eyre DR, Paz MA, Gallop PM. Cross-linking in collagen and elastin. Annu. Rev. Biochem. 1984;53:717–748.

120. Howard J. Mechanics of Motor Proteins and the Cytoskeleton. Sunderland, MA: Sinauer; 2001.

121. in 't Veld PJ, Stevens MJ. Simulation of the mechanical strength of a single collagen molecule. Biophys. J. 2008;95:33–39.

122. van der Rijt JAJ, van der Werf KO, Bennink ML, Dijkstra PJ, Feijen J. Micromechanical testing of individual collagen fibrils. Macromol. Biosci. 2006;6:697–702.

123. Wenger MPE, Bozec L, Horton M, Mesquida P. Mechanical properties of collagen fibrils. Biophys. J. 2007;93:1255–1263.

124. Yang L, van der Werf KO, Fitie CFC, Bennink ML, Dijkstra PJ, Feijen J. Mechanical properties of native and cross-linked type I collagen fibrils. Biophys. J. 2008;94:2204–2211.

125. Olsen D, Yang C, Bodo M, Chang R, Leigh S, et al. Recombinant collagen and gelatin for drug delivery. Adv. Drug Deliv. Rev. 2003;55:1547–1567.

126. Kishimoto T, Morihara Y, Osanai M, Ogata S, Kamitakahara M, et al. Synthesis of poly(Pro-Hyp-Gly)n by direct polycondensation of (Pro-Hyp-Gly)n, where n = 1, 5, and 10, and stability of the triple helical structure. Biopolymers. 2005;79:163–172.

127. Paramonov SE, Gauba V, Hartgerink JD. Synthesis of collagen-like peptide polymers by native chemical ligation. Macromolecules. 2005;38:7555–7561.

128. Kar K, Amin P, Bryan MA, Persikov AV, Mohs A, et al. Self-association of collagen triple-helix peptides into higher order structures. J. Biol. Chem. 2006;281:33283–33290.

129. Kar K, Wang Y-H. Sequence dependence of kinetics and morphology of collagen model peptide self-assembly into higher order structures. Protein Sci. 2008;17:1086–1095.

130. Koide T, Homma DL, Asada S, Kitagawa K. Self-complementary peptides for the formation of collagen-like triple helical supramolecules. Bioorg. Med. Chem. Lett. 2005;15:5230–5233.

131. Kotch FW, Raines RT. Self-assembly of synthetic collagen triple helices. Proc. Natl. Acad. Sci. USA. 2006;103:3028–3033. NOTE: Synthesis of lengthy collagen triple helices (up to 400 nm) by molecular self-assembly.

132. Yamazaki CM, Asada S, Kitagawa K, Koide T. Artificial collagen gels via self-assembly of de novo designed peptides. Biopolymers. 2008;90:816–823.

133. Cejas M, Kinney WA, Chen C, Leo GC, Tounge BA, et al. Collagen-related peptides: self-assembly of short, single strands into a functional biomaterial of micrometer scale. J. Am. Chem. Soc. 2007;129:2202–2203.

134. Cejas MA, Kinney WA, Chen C, Vinter JG, Almond HRJ, et al. Thrombogenic collagen-mimetic peptides: self-assembly of triple helix-based fibrils driven by hydrophobic interactions. Proc. Natl. Acad. Sci. USA. 2008;105:8513–8518.

135. Gottlieb DG, Morin S, Jin S, Raines RT. Self-assembled collagen-like peptide fibers as templates for metallic nanowires. J. Mater. Chem. 2008;18:3865–3870.

136. Przybyla DE, Chmielewski J. Metal-triggered radial self-assembly of collagen peptide fibers. J. Am. Chem. Soc. 2008;130:12610–12611.

137. Rele S, Song Y, Apkarian RP, Qu Z, Conticello VP, Chaikof EL. D-periodic collagen-mimetic microfibers. J. Am. Chem. Soc. 2007;129:14780–14787. NOTE: First self-assembly of CRPs into micrometer-scale fibrils that have D-periodicity–-a hallmark of natural collagen fibrils.

138. Holmes DF, Chapman JA, Prockop DJ, Kadler KE. Growing tips of type I collagen fibrils formed in vitro are near-paraboloidal in shape, implying a reciprocal relationship between accretion and diameter. Proc. Natl. Acad. Sci. USA. 1992;89:9855–9859.

139. Johnson G, Jenkins M, McLean KM, Griesser HJ, Kwak J, et al. Peptoid-containing collagen mimetics with cell binding activity. J. Biomed. Mater. Res. 2000;51:612–624.

140. Cejas MA, Chen C, Kinney WA, Maryanoff BE. Nanoparticles that display short collagen-related peptides. Potent stimulation of human platelet aggregation by triple helical motifs. Bioconjug. Chem. 2007;18:1025–1027.

141. Smethurst PA, Onley DJ, Jarvis GE, O’Connor MN, Knight CG, et al. Structural basis for the platelet-collagen interaction. J. Biol. Chem. 2007;282:1296–1304.

142. Mo X, An Y, Yun C-S, Yu SM. Nanoparticle-assisted visualization of binding interactions between collagen mimetic peptides and collagen fibers. Angew. Chem. Int. Ed. Engl. 2006;45:2267–2270.

143. Wang AY, Mo X, Chen CS, Yu SM. Facile modification of collagen directed by collagen mimetic peptides. J. Am. Chem. Soc. 2005;127:4130–4131.

144. Wang AY, Foss CA, Leong S, Mo X, Pomper MG, Yu SM. Spatio-temporal modification of collagen scaffolds mediated by triple helical propensity. Biomacromolecules. 2008;9:1755–1763.

145. Dobson CM. Protein folding and misfolding. Nature. 2003;426:884–890.

146. Nelson R, Sawaya MR, Balbirnie M, Madsen AØ, Riekel C, et al. Structure of the cross-ß spine of amyloid-like fibrils. Nature. 2005;435:773–778.

147. Kim CA, Berg JM. Thermodynamic ß-sheet propensities measured using a zinc-finger host peptide. Nature. 1993;362:267–270.

148. Minor DL, Jr, Kim PS. Measurement of the ß-sheet-forming propensities of amino acids. Nature. 1994;367:660–663.

149. Chiti F, Stefani M, Taddei N, Ramponi G, Dobson CM. Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature. 2003;424:805–808.

150. Rauscher S, Baud S, Miao M, Keeley FW, Pomès R. Proline and glycine control protein self-organization into elastomeric or amyloid fibrils. Structure. 2006;14:1667–1676.

151. https://www.ncbi.nlm.nih.gov/pubmed/25156668

152. http://www.tandfonline.com/doi/abs/10.1185/030079908X291967

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