Mechanics of molecular collagen is influenced by hydroxyapatite in natural bone
Source abstract
Abstract
As often seen in biological structural materials, bone exhibits complex hierarchical structure. The primary constituents of bone are collagen and hydroxyapatite (HAP). HAP mineralizes at specific locations at collagen, in such a way that the c-axis of HAP aligns parallel to collagen molecule. The collagen molecule is helical overall with non-helical ends that are N- or C-telopeptides. The collagen molecule with telopeptides interacts with specific surfaces of mineralized HAP. When subjected to load, the interactions at the interface between HAP and collagen may significantly affect the overall mechanics of the collagen molecule. Here, we have performed molecular dynamics (MD) and steered MD (SMD) simulations in order to understand the load carrying behavior of collagen in the proximity of HAP. Our simulations indicate that the load-deformation response of collagen is different when it interacts with HAP as compared to its response in the absence of HAP. The interface between HAP and collagen affects the overall load-deformation response of collagen. Further, bone also has considerable amount of water and we have observed that water significantly influences the load-deformation response of collagen due to collagen-water-HAP interactions.
Source: openaire · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Bone health and osteoporosis research · Collagen: Extraction and Characterization · Calcium Carbonate Crystallization and Inhibition
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (78)
Show source-provided references
1. Marieb EN (1998) In: Human anatomy & physiology, 4th edn. Benjamin/Cummings Science Publishing, Menlo Park, California
2. Tortora GJ (1989) In: Principles of human anatomy, 5th edn. Harper & Row Publishers, New York
3. Boyle WJ, Simonet WS, Lacey DL (2003) Nature 423:33710.1038/nature01658 ↗
4. Von Recum AF (1998) In: Handbook of biomaterials evaluation. CRC Publisher
5. Ramakrishna S, Mayer J, Wintermantel E, Leong WK (2001) Comp Sci Tech 61:118910.1016/S0266-3538(00)00241-4 ↗
6. Black J (1992) In: Biological performance of materials: fundamentals of biocompatibility. Marcel Dekker, New York
7. Weiner S, Wagner HD (1998) Ann Rev Mater Res 28:271
8. Weiner S, Traub W (1992) FASEB 6:87910.1096/fasebj.6.3.1740237 ↗
9. Landis WJ (1995) Bone 16:53310.1016/8756-3282(95)00076-P ↗
10. Katti KS, Gujjula P (2002) In: Proceedings of 15th ASCE engineering mechanics conference, New York, NY
11. Verma D, Katti K, Katti D (2006) J Biomed Mater Res 77:5910.1002/jbm.a.30592 ↗
12. Verma D, Katti K, Katti D (2006) J Biomed Mater Res 78A:77210.1002/jbm.a.30774 ↗
13. Katti KS, Turlapati P, Verma D, Bhowmik R, Gujjula P, Katti DR (2006) Am J Biochem Biotech 2:7310.3844/ajbbsp.2006.73.79 ↗
14. Katti KS (2004) Colloids Interfaces B 39:13310.1016/j.colsurfb.2003.12.002 ↗
15. Gao H, Ji B, Jäger IL, Arzt E, Fratzl P (2003) Proc Natl Acad Sci USA 100:559710.1073/pnas.0631609100 ↗
16. Gao H, Chen S (2005) J Appl Mech 72:73210.1115/1.1988348 ↗
17. Ji B, Gao H (2004) Mater Sci Eng A 366:9610.1016/j.msea.2003.08.121 ↗
18. Ji B, Gao H (2004) J Mech Phys Solids 52:196310.1016/j.jmps.2004.03.006 ↗
19. Ji B, Gao H, Hsia KJ (2004) Phil Mag Lett 84:63110.1080/09500830512331329141 ↗
20. Gao H, Ji B (2003) Eng Frac Mech 70:177710.1016/S0013-7944(03)00124-3 ↗
21. Ji B, Gao H (2006) Comp Sci & Tech 66:121210.1016/j.compscitech.2005.10.017 ↗
22. Buehler MJ (2006) PNAS 103:1228510.1073/pnas.0603216103 ↗
23. Buehler MJ (2006) J Mat Sci 21:1947
24. Hellmich C, Barthélémy J-F, Dormieux L (2004) Eur J Mech A/Solids 23:78310.1016/j.euromechsol.2004.05.004 ↗
25. Fritsch A, Hellmich C (2007) J Theor Biol 244:59710.1016/j.jtbi.2006.09.013 ↗
26. Reilly DT, Burstein AH, Frankel VH (1974) J Biomech 7:27110.1016/0021-9290(74)90018-9 ↗
27. Rho JY, Tsui TY, Pharr GM (1997) Biomaterials 18:132510.1016/S0142-9612(97)00073-2 ↗
28. Murugan R, Ramakrishna S (2005) Comp Sci & Tech 65:238510.1016/j.compscitech.2005.07.022 ↗
29. Jae-Young Rho L. Kuhn-Spearing, Zioupos P (1998) Med Eng & Phy 20:9210.1016/S1350-4533(98)00007-1 ↗
30. Landis WJ (1995) Bone 16:53310.1016/8756-3282(95)00076-P ↗
31. Ziv V, Weiner S (1994) Conn Tissue Res 30:16510.3109/03008209409061969 ↗
32. Ghosh P, Katti DR, Katti KS (2007) Biomacromolecules 8:85110.1021/bm060942h ↗
33. Legeros RZ (1994) In: Biological and synthetic apatites. CRC Press, Boca Raton
34. Park JB (1984) In: Biomaterials science and engineering. Plenum Press, New York10.1007/978-1-4613-2769-1 ↗
35. Murugan R, Ramakrishna S (2004) In: Encyclopedia of nanoscience and nanotechnology, vol 7. American Scientific Publishers, California, p 595
36. Dempster WT, Liddicoat RT (1952) Am J Anatomy 91:33110.1002/aja.1000910302 ↗
37. Evans FG (1973) Mechanical properties of bone. Thomas, Springfield
38. Evans FG, Lebow M (1951) J Appl Physiol 3:56310.1152/jappl.1951.3.9.563 ↗
39. Sedlin ED, Hirsch C (1966) Acta Orthopaedica Scandinavica 37:2910.3109/17453676608989401 ↗
40. Smith JW, Walmsley R (1959) J Anatomy 93:503
41. Yamada H, Evans FG (1970) Strength of biological materials. Williams & Wilkins, Baltimore
42. Nyman JS, Roy A, Shen X, Acuna RL, Tyler JH Wang X (2006) J Biomech 39:93110.1016/j.jbiomech.2005.01.012 ↗
43. Currey JD (1965) J Exp Biol 43:27910.1242/jeb.43.2.279 ↗
44. Fitton-Jackson S (1957) Proc R Soc London Ser B 146:27010.1098/rspb.1957.0010 ↗
45. Nylen MU, Scott DB, Mosley VM (1960) In: Sognnaes RF (ed) Calcification in Biological Systems. Am Assoc Adv Sci p 129
46. Itoha S, Masanori K, Koyamac Y, Takakudac K, Shinomiyaa K, Tanaka J (2002) Biomaterials 23:391910.1016/S0142-9612(02)00126-6 ↗
47. Kadler KE, Holmes DF, Trotter JA, Chapman JA (1996) Biochem J 316:110.1042/bj3160001 ↗
48. Malone JP, Alvares K, Veis A (2005) Biochem 44:1526910.1021/bi0508338 ↗
49. Malone JP, George A, Veis A (2004) Proteins: Struct Funct & Biol 54:20610.1002/prot.10526 ↗
50. Kale L, Skeel R, Bhandarkar M, Brunner R, Gursoy A, Krawetz N, Phillips J, Shinozaki A, Varadarajan K, Schulten KJ (1999) Comput Phys 151:283 http://www.ks.uiuc.edu/Research/namd/ , as on 16 January 2007
51. Brooks BR, Bruccoleri RE, Olafson BD, States DJ, Swaminathan S, Karplus MJ (1983) J Comput Chem 4:18710.1002/jcc.540040211 ↗
52. Humphrey W, Dalke A, Schulten KJ (1996) J Mol Graphics 14:33, http://www.ks.uiuc.edu/Research/vmd/, as on 16 January 2007
53. Feller SE, Zhang Y, Pastor RW, Brooks BR (1995) J Chem Phys 103:461310.1063/1.470648 ↗
54. Martyna GJ, Tobias DJ, Klein ML (1994) J Chem Phys 101:417710.1063/1.467468 ↗
55. Beck K, Brodsky B (1998) J Struct Biol 122:1710.1006/jsbi.1998.3965 ↗
56. Berisio R, Vitagliano L, Mazzarella L, Zagari A (2002) Protein Sci 11:26210.1110/ps.32602 ↗
57. Jones EY, Miller A (1987) Biopolymers 26:46310.1002/bip.360260403 ↗
58. Otter A, Kotovych G, Scott PG (1989) Biochemistry 28:800310.1021/bi00446a006 ↗
59. Sudarsanan K, Young RA (1969) Acta Crystallographica B 25:153410.1107/S0567740869004298 ↗
60. Bhowmik R, Katti KS, Verma D, Katti DR (2007) Mater Sci Eng C 27:35210.1016/j.msec.2006.05.048 ↗
61. Bhowmik R, Katti KS, Katti D (2006) Polymer 48:66410.1016/j.polymer.2006.11.015 ↗
62. Tasker PW (1979) J Phys C Solid State Phys 12:497710.1088/0022-3719/12/22/036 ↗
63. Bertaut FCR (1958) Acad Sci Paris 246:3447
64. Izrailev S, Stepaniants S, Balsera M, Oono Y, Schulten K (1997) Biophys J 72:156810.1016/S0006-3495(97)78804-0 ↗
65. Isralewitz B, Izrailev S, Schulten K (1997) Biophys J 73:297210.1016/S0006-3495(97)78326-7 ↗
66. Wriggers W, Schulten K (1999) Proteins Struct Funct Genet 35:26210.1002/(SICI)1097-0134(19990501)35:2<262::AID-PROT11>3.0.CO;2-N ↗
67. Kosztin D, Izrailev S, Schulten K (1999) Biophys J 76:18810.1016/S0006-3495(99)77188-2 ↗
68. Molnar F, Ben-Nun M, Marti´Nez TJ, Schulten K (2000) J Mol Struct (THEOCHEM) 506:16910.1016/S0166-1280(00)00410-3 ↗
69. Lu H, Isralewitz B, Krammer A, Vogel V, Schulten K (1998) Biophys J 75:66210.1016/S0006-3495(98)77556-3 ↗
70. Krammer A, Lu H, Isralewitz B, Schulten K, Vogel V (1999) Proc Natl Acad Sci USA 96:135110.1073/pnas.96.4.1351 ↗
71. Lu H, Schulten K (1999) Proteins Struct Funct Genet 35:45310.1002/(SICI)1097-0134(19990601)35:4<453::AID-PROT9>3.0.CO;2-M ↗
72. Lu H, Schulten K (1999) Chem Phys 247:14110.1016/S0301-0104(99)00164-0 ↗
73. Izrailev S, Stepaniants S, Isralewitz B, Kosztin D, Lu H, Molnar F, Wriggers W, Schulten K (1998) In: Computational molecular dynamics: challenges, methods, ideas. volume 4 of Lecture Notes in Computational Science and Engineering, Springer-Verlag, Berlin p 39
74. Schulten K, Schulten Z, Szabo A (1981) J Chem Phys 74:442610.1063/1.441684 ↗
75. Lu H, Krammer A, Isralewitz B, Vogel V, Schulten K (2000) In: Elastic filaments of the cell. Academic/Plenum Publishers, New York, p 14310.1007/978-1-4615-4267-4_9 ↗
76. Grubmüller H, Heymann B, Tavan P (1996) Science 271:99710.1126/science.271.5251.997 ↗
77. Balsera M, Stepaniants S, Oono Y, Schulten K (1997) Biophys J 73:128110.1016/S0006-3495(97)78161-X ↗
78. Gao M, Wilmanns M, Schulten K (2002) Biophysical J 83:343510.1016/S0006-3495(02)75343-5 ↗