Pair your accounts.

Export articles to Mendeley

Get article recommendations from ACS based on references in your Mendeley library.

Pair your accounts.

Export articles to Mendeley

Get article recommendations from ACS based on references in your Mendeley library.

You’ve supercharged your research process with ACS and Mendeley!

STEP 1:
Click to create an ACS ID

Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

MENDELEY PAIRING EXPIRED
Your Mendeley pairing has expired. Please reconnect
ACS Publications. Most Trusted. Most Cited. Most Read
In situ AFM Study of Amelogenin Assembly and Disassembly Dynamics on Charged Surfaces Provides Insights on Matrix Protein Self-Assembly

OR SEARCH CITATIONS

My Activity
Publications

Figure 1Loading Img
Download Hi-Res ImageDownload to MS-PowerPointCite This:J. Am. Chem. Soc. 2011, 133, 43, 17406-17413
    Article

    In situ AFM Study of Amelogenin Assembly and Disassembly Dynamics on Charged Surfaces Provides Insights on Matrix Protein Self-Assembly
    Click to copy article linkArticle link copied!

    View Author Information
    † The Molecular Foundry, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, California 94720, United States
    ‡ Center for Craniofacial Molecular Biology, Herman Ostrow School of Dentistry, University of Southern California, Los Angeles, California 90033, United States
    [email protected]; [email protected]
    Other Access OptionsSupporting Information (1)

    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2011, 133, 43, 17406–17413
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ja206849c
    Published September 14, 2011
    Copyright © 2011 American Chemical Society
    Request reuse permissions

    Abstract

    Click to copy section linkSection link copied!
    Abstract Image

    Because self-assembly of matrix proteins is a key step in hard tissue mineralization, developing an understanding of the assembly pathways and underlying mechanisms is likely to be important for successful hard tissue engineering. While many studies of matrix protein assembly have been performed on bulk solutions, in vivo these proteins are likely to be in contact with charged biological surfaces composed of lipids, proteins, or minerals. Here we report the results of an in situ atomic force microscopy (AFM) study of self-assembly by amelogenin—the principal protein of the extracellular matrix in developing enamel—in contact with two different charged substrates: hydrophilic negatively charged bare mica and positively charged 3-aminopropyl triethoxysilane (APS) silanized mica. First we demonstrate an AFM-based protocol for determining the size of both amelogenin monomers and oligomers. Using this protocol, we find that, although amelogenin exists primarily as ∼26 nm in diameter nanospheres in bulk solution at a pH of 8.0 studied by dynamic light scattering, it behaves dramatically differently upon interacting with charged substrates at the same pH and exhibits complex substrate-dependent assembly pathways and dynamics. On positively charged APS-treated mica surfaces, amelogenin forms a relatively uniform population of decameric oligomers, which then transform into two main populations: higher-order assemblies of oligomers and amelogenin monomers, while on negatively charged bare mica surfaces, it forms a film of monomers that exhibits tip-induced desorption and patterning. The present study represents a successful attempt to identify the size of amelogenin oligomers and to directly monitor assembly and disassembly dynamics on surfaces. The findings have implications for amelogenin-controlled calcium phosphate mineralization in vitro and may offer new insights into in vivo self-assembly of matrix proteins as well as their control over hard tissue formation.

    Copyright © 2011 American Chemical Society

    Subjects

    what are subjects

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.

    Recommended

    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. Add or change your institution or let them know you’d like them to include access.

    Supporting Information

    Click to copy section linkSection link copied!

    Supporting figures (Figures S1–S4) and Table S1. This material is available free of charge via the Internet at http://pubs.acs.org.

    Terms & Conditions

    Electronic Supporting Information files are available without a subscription to ACS Web Editions. The American Chemical Society holds a copyright ownership interest in any copyrightable Supporting Information. Files available from the ACS website may be downloaded for personal use only. Users are not otherwise permitted to reproduce, republish, redistribute, or sell any Supporting Information from the ACS website, either in whole or in part, in either machine-readable form or any other form without permission from the American Chemical Society. For permission to reproduce, republish and redistribute this material, requesters must process their own requests via the RightsLink permission system. Information about how to use the RightsLink permission system can be found at http://pubs.acs.org/page/copyright/permissions.html.

    Cited By

    Click to copy section linkSection link copied!

    This article is cited by 64 publications.

    1. Yingying Zhang, Yongchun Liu, Yonggang Liu, Ping Zuo, Shuting Miao, Bowen Hu, Yu Kang, Wei Liu, Qingmin Yang, Hao Ren, Peng Yang. α-Helix-Mediated Protein Adhesion. Journal of the American Chemical Society 2023, 145 (31) , 17125-17135. https://doi.org/10.1021/jacs.3c03581
    2. Changyu Shao, Rucha Arun Bapat, Jingtan Su, Janet Moradian-Oldak. Regulation of Hydroxyapatite Nucleation In Vitro through Ameloblastin–Amelogenin Interactions. ACS Biomaterials Science & Engineering 2023, 9 (4) , 1834-1842. https://doi.org/10.1021/acsbiomaterials.1c01113
    3. Garry W. Buchko, Sebastian T. Mergelsberg, Barbara J. Tarasevich, Wendy J. Shaw. Residue-Specific Insights into the Intermolecular Protein–Protein Interfaces Driving Amelogenin Self-Assembly in Solution. Biochemistry 2022, 61 (24) , 2909-2921. https://doi.org/10.1021/acs.biochem.2c00522
    4. Zhiliang Li, Bin Cai, Wenchao Yang, Chun-Long Chen. Hierarchical Nanomaterials Assembled from Peptoids and Other Sequence-Defined Synthetic Polymers. Chemical Reviews 2021, 121 (22) , 14031-14087. https://doi.org/10.1021/acs.chemrev.1c00024
    5. Wenchao Yang, Qiuxiang Yin, Chun-Long Chen. Designing Sequence-Defined Peptoids for Biomimetic Control over Inorganic Crystallization. Chemistry of Materials 2021, 33 (9) , 3047-3065. https://doi.org/10.1021/acs.chemmater.1c00243
    6. Jinhui Tao, Andreas Fijneman, Jiaqi Wan, Saumya Prajapati, Kaushik Mukherjee, Alejandro Fernandez-Martinez, Janet Moradian-Oldak, James J. De Yoreo. Control of Calcium Phosphate Nucleation and Transformation through Interactions of Enamelin and Amelogenin Exhibits the “Goldilocks Effect”. Crystal Growth & Design 2018, 18 (12) , 7391-7400. https://doi.org/10.1021/acs.cgd.8b01066
    7. Sarah A. Engelberth, Margot S. Bacino, Shaiba Sandhu, Wu Li, Johan Bonde, Stefan Habelitz. Progression of Self-Assembly of Amelogenin Protein Supramolecular Structures in Simulated Enamel Fluid. Biomacromolecules 2018, 19 (10) , 3917-3924. https://doi.org/10.1021/acs.biomac.8b00808
    8. Kaushik Mukherjee, Qichao Ruan, Steven Nutt, Jinhui Tao, James J. De Yoreo, and Janet Moradian-Oldak . Peptide-Based Bioinspired Approach to Regrowing Multilayered Aprismatic Enamel. ACS Omega 2018, 3 (3) , 2546-2557. https://doi.org/10.1021/acsomega.7b02004
    9. Shanshan Wu, Menghan Yu, Meng Li, Lijun Wang, Christine V. Putnis, and Andrew Putnis . In Situ Atomic Force Microscopy Imaging of Octacalcium Phosphate Crystallization and Its Modulation by Amelogenin’s C-Terminus. Crystal Growth & Design 2017, 17 (4) , 2194-2202. https://doi.org/10.1021/acs.cgd.7b00129
    10. Chun-Long Chen, Ronald N. Zuckermann, and James J. DeYoreo . Surface-Directed Assembly of Sequence-Defined Synthetic Polymers into Networks of Hexagonally Patterned Nanoribbons with Controlled Functionalities. ACS Nano 2016, 10 (5) , 5314-5320. https://doi.org/10.1021/acsnano.6b01333
    11. Jinhui Tao, Garry W. Buchko, Wendy J. Shaw, James J. De Yoreo, and Barbara J. Tarasevich . Sequence-Defined Energetic Shifts Control the Disassembly Kinetics and Microstructure of Amelogenin Adsorbed onto Hydroxyapatite (100). Langmuir 2015, 31 (38) , 10451-10460. https://doi.org/10.1021/acs.langmuir.5b02549
    12. Shanshan Wu, Hang Zhai, Wenjun Zhang, and Lijun Wang . Monomeric Amelogenin’s C-Terminus Modulates Biomineralization Dynamics of Calcium Phosphate. Crystal Growth & Design 2015, 15 (9) , 4490-4497. https://doi.org/10.1021/acs.cgd.5b00754
    13. Hongcheng Sun, Lu Miao, Jiaxi Li, Shuang Fu, Guo An, Chengye Si, Zeyuan Dong, Quan Luo, Shuangjiang Yu, Jiayun Xu, and Junqiu Liu . Self-Assembly of Cricoid Proteins Induced by “Soft Nanoparticles”: An Approach To Design Multienzyme-Cooperative Antioxidative Systems. ACS Nano 2015, 9 (5) , 5461-5469. https://doi.org/10.1021/acsnano.5b01311
    14. M. Tavafoghi Jahromi and M. Cerruti . Amino Acid/Ion Aggregate Formation and Their Role in Hydroxyapatite Precipitation. Crystal Growth & Design 2015, 15 (3) , 1096-1104. https://doi.org/10.1021/cg501369q
    15. Nitinun Varongchayakul, Sara Johnson, Trina Quabili, Joseph Cappello, Hamidreza Ghandehari, Santiago De Jesus Solares, Wonmuk Hwang, and Joonil Seog . Direct Observation of Amyloid Nucleation under Nanomechanical Stretching. ACS Nano 2013, 7 (9) , 7734-7743. https://doi.org/10.1021/nn402322k
    16. Yushi Bai, Quan Luo, Wei Zhang, Lu Miao, Jiayun Xu, Hongbin Li, and Junqiu Liu . Highly Ordered Protein Nanorings Designed by Accurate Control of Glutathione S-Transferase Self-Assembly. Journal of the American Chemical Society 2013, 135 (30) , 10966-10969. https://doi.org/10.1021/ja405519s
    17. Ye Li, Xianren Zhang, and Dapeng Cao . Self-Assembly of Patterned Nanoparticles on Cellular Membranes: Effect of Charge Distribution. The Journal of Physical Chemistry B 2013, 117 (22) , 6733-6740. https://doi.org/10.1021/jp312124x
    18. Wei Li, Amitabha Chakrabarti, and James D. Gunton . Self-Assembly of a Bipolar Model of Biomacromolecules. Langmuir 2013, 29 (14) , 4470-4476. https://doi.org/10.1021/la4002994
    19. Olga Martinez-Avila, Shenping Wu, Seung Joong Kim, Yifan Cheng, Feroz Khan, Ram Samudrala, Andrej Sali, Jeremy A. Horst, and Stefan Habelitz . Self-Assembly of Filamentous Amelogenin Requires Calcium and Phosphate: From Dimers via Nanoribbons to Fibrils. Biomacromolecules 2012, 13 (11) , 3494-3502. https://doi.org/10.1021/bm300942c
    20. Keith M. Bromley, Rajamani Lakshminarayanan, Mitchell Thompson, Sowmya Bekshe Lokappa, Victoria A. Gallon, Kang Rae Cho, S. Roger Qiu, and Janet Moradian-Oldak . Amelogenin Processing by MMP-20 Prevents Protein Occlusion Inside Calcite Crystals. Crystal Growth & Design 2012, 12 (10) , 4897-4905. https://doi.org/10.1021/cg300754a
    21. Brenna M. Knight, Christina A. McCutchin. Modulating ion-binding at macromolecular interfaces during (bio)mineralization: A snapshot review for calcium carbonate and calcium phosphate systems. MRS Advances 2024, 9 (13) , 1039-1047. https://doi.org/10.1557/s43580-024-00860-x
    22. Haibin Li, Zhiheng Sun, Yue Liu, Yi Xing, Jing Gao, Aihong Shi, Yadong Yu, Jin Long, Dong‐Po Song, Chao Jin, Marc D. McKee, Jun‐An Ma, Wenge Jiang. Chiral gypsum with high‐performance mechanical properties induced by self‐assembly of chiral amino acid on an amorphous mineral. SmartMat 2024, 14 https://doi.org/10.1002/smm2.1302
    23. Zhaoyi Zhai, Sakshi Yadav Schmid, Zhixing Lin, Shuai Zhang, Fang Jiao. Unveiling the nanoscale architectures and dynamics of protein assembly with in situ atomic force microscopy. Aggregate 2024, 9 https://doi.org/10.1002/agt2.604
    24. Wenwu Zou, Yutao Lin, Zhenze Xie, Yingxin Lin, Chang Du. Phosphorylated amelogenin N-terminal peptides regulate calcite crystal cluster formation in a water–acetonitrile system. CrystEngComm 2023, 25 (36) , 5150-5159. https://doi.org/10.1039/D3CE00165B
    25. Jing Dong, Wenyan Ruan, Xiaohong Duan. Molecular‐based phenotype variations in amelogenesis imperfecta. Oral Diseases 2023, 29 (6) , 2334-2365. https://doi.org/10.1111/odi.14599
    26. Daniela Gachova, Bretislav Lipovy, Tereza Deissova, Lydie Izakovicova Holla, Zdenek Danek, Petra Borilova Linhartova. Polymorphisms in genes expressed during amelogenesis and their association with dental caries: a case–control study. Clinical Oral Investigations 2023, 27 (4) , 1681-1695. https://doi.org/10.1007/s00784-022-04794-2
    27. Paulette Spencer, Qiang Ye, Anil Misra, Josephine R. Chandler, Charles M. Cobb, Candan Tamerler. Engineering peptide-polymer hybrids for targeted repair and protection of cervical lesions. Frontiers in Dental Medicine 2022, 3 https://doi.org/10.3389/fdmed.2022.1007753
    28. Zeina Alraawi, Nayan Banerjee, Srujana Mohanty, Thallapuranam Krishnaswamy Suresh Kumar. Amyloidogenesis: What Do We Know So Far?. International Journal of Molecular Sciences 2022, 23 (22) , 13970. https://doi.org/10.3390/ijms232213970
    29. S. Habelitz, Y. Bai. Mechanisms of Enamel Mineralization Guided by Amelogenin Nanoribbons. Journal of Dental Research 2021, 100 (13) , 1434-1443. https://doi.org/10.1177/00220345211012925
    30. Wu Li, Yan Zhang, Sylvie Babajko, Pamela Den Besten. Enamel Matrix Biomineralization: The Role of pH Cycling. 2021, 271-293. https://doi.org/10.1007/978-3-030-76283-4_11
    31. Vaibhav Sharma, Alagiri Srinivasan, Fredrik Nikolajeff, Saroj Kumar. Biomineralization process in hard tissues: The interaction complexity within protein and inorganic counterparts. Acta Biomaterialia 2021, 120 , 20-37. https://doi.org/10.1016/j.actbio.2020.04.049
    32. Wendy J. Shaw, Barbara J. Tarasevich, Garry W. Buchko, Rajith M.J. Arachchige, Sarah D. Burton. Controls of nature: Secondary, tertiary, and quaternary structure of the enamel protein amelogenin in solution and on hydroxyapatite. Journal of Structural Biology 2020, 212 (3) , 107630. https://doi.org/10.1016/j.jsb.2020.107630
    33. Dong Wang, Jingjing Deng, Xuliang Deng, Changqing Fang, Xu Zhang, Peng Yang. Controlling Enamel Remineralization by Amyloid‐Like Amelogenin Mimics. Advanced Materials 2020, 32 (31) https://doi.org/10.1002/adma.202002080
    34. Wenge Jiang, Dimitra Athanasiadou, Shaodong Zhang, Raffaella Demichelis, Katarzyna B. Koziara, Paolo Raiteri, Valentin Nelea, Wenbo Mi, Jun-An Ma, Julian D. Gale, Marc D. McKee. Homochirality in biomineral suprastructures induced by assembly of single-enantiomer amino acids from a nonracemic mixture. Nature Communications 2019, 10 (1) https://doi.org/10.1038/s41467-019-10383-x
    35. Rajith Jayasinha Arachchige, Sarah D. Burton, Jun-Xia Lu, Bojana Ginovska, Larisa K. Harding, Megan E. Taylor, Jinhui Tao, Alice Dohnalkova, Barbara J. Tarasevich, Garry W. Buchko, Wendy J. Shaw. Solid-State NMR Identification of Intermolecular Interactions in Amelogenin Bound to Hydroxyapatite. Biophysical Journal 2018, 115 (9) , 1666-1672. https://doi.org/10.1016/j.bpj.2018.08.027
    36. Jamoliddin Razzokov, Saber Naderi, Paul van der Schoot. Nanoscale insight into silk-like protein self-assembly: effect of design and number of repeat units. Physical Biology 2018, 15 (6) , 066010. https://doi.org/10.1088/1478-3975/aadb5e
    37. Garima Thakur, Kovur Prashanthi, Keren Jiang, Thomas Thundat. Self-Assembly of Human Serum Albumin: A Simplex Phenomenon. Biomolecules 2017, 7 (3) , 69. https://doi.org/10.3390/biom7030069
    38. Rodrigo S. Lacruz, Stefan Habelitz, J. Timothy Wright, Michael L. Paine. Dental Enamel Formation and Implications for Oral Health and Disease. Physiological Reviews 2017, 97 (3) , 939-993. https://doi.org/10.1152/physrev.00030.2016
    39. Claire E. L. Smith, James A. Poulter, Agne Antanaviciute, Jennifer Kirkham, Steven J. Brookes, Chris F. Inglehearn, Alan J. Mighell. Amelogenesis Imperfecta; Genes, Proteins, and Pathways. Frontiers in Physiology 2017, 8 https://doi.org/10.3389/fphys.2017.00435
    40. Christopher Connelly, Thomas Cicuto, Jason Leavitt, Alexander Petty, Amy Litman, Henry C. Margolis, Aren E. Gerdon. Dynamic interactions of amelogenin with hydroxyapatite surfaces are dependent on protein phosphorylation and solution pH. Colloids and Surfaces B: Biointerfaces 2016, 148 , 377-384. https://doi.org/10.1016/j.colsurfb.2016.09.010
    41. Samuel J. Butler, Leif Bülow, Johan Bonde. Functionalization of Recombinant Amelogenin Nanospheres Allows Their Binding to Cellulose Materials. Biotechnology Journal 2016, 11 (10) , 1343-1351. https://doi.org/10.1002/biot.201600381
    42. Kaushik Mukherjee, Qichao Ruan, David Liberman, Shane N. White, Janet Moradian-Oldak. Repairing human tooth enamel with leucine-rich amelogenin peptide–chitosan hydrogel. Journal of Materials Research 2016, 31 (5) , 556-563. https://doi.org/10.1557/jmr.2016.64
    43. Chengye Si, Jiaxi Li, Quan Luo, Chunxi Hou, Tiezheng Pan, Hongbin Li, Junqiu Liu. An ion signal responsive dynamic protein nano-spring constructed by high ordered host–guest recognition. Chemical Communications 2016, 52 (14) , 2924-2927. https://doi.org/10.1039/C5CC10373H
    44. S. P. Qiao, C. Lang, R. D. Wang, X. M. Li, T. F. Yan, T. Z. Pan, L. L. Zhao, X. T. Fan, X. Zhang, C. X. Hou, Q. Luo, J. Y. Xu, J. Q. Liu. Metal induced self-assembly of designed V-shape protein into 2D wavy supramolecular nanostructure. Nanoscale 2016, 8 (1) , 333-341. https://doi.org/10.1039/C5NR06378G
    45. Sowmya Bekshe Lokappa, Karthik Balakrishna Chandrababu, Janet Moradian-Oldak. Tooth enamel protein amelogenin binds to ameloblast cell membrane-mimicking vesicles via its N-terminus. Biochemical and Biophysical Research Communications 2015, 464 (3) , 956-961. https://doi.org/10.1016/j.bbrc.2015.07.082
    46. Melika Sarem, Steffen Lüdeke. Circular dichroism: A powerful tool for studying biomineralization promoter proteins. MRS Bulletin 2015, 40 (6) , 490-498. https://doi.org/10.1557/mrs.2015.116
    47. Sowmya Bekshe Lokappa, Karthik Balakrishna Chandrababu, Kaushik Dutta, Iva Perovic, John Spencer Evans, Janet Moradian‐Oldak. Interactions of amelogenin with phospholipids. Biopolymers 2015, 103 (2) , 96-108. https://doi.org/10.1002/bip.22573
    48. Xiao Yang, Hui Shang, Chunmei Ding, Jianshu Li. Recent developments and applications of bioinspired dendritic polymers. Polymer Chemistry 2015, 6 (5) , 668-680. https://doi.org/10.1039/C4PY01537A
    49. Qichao Ruan, Janet Moradian-Oldak. Amelogenin and enamel biomimetics. Journal of Materials Chemistry B 2015, 3 (16) , 3112-3129. https://doi.org/10.1039/C5TB00163C
    50. Y. Lei, T. Wang, J.W. Mitchell, J. Qiu, L. Kilpatrick-Liverman. Synthesis of Carboxylic Block Copolymers via Reversible Addition Fragmentation Transfer Polymerization for Tooth Erosion Prevention. Journal of Dental Research 2014, 93 (12) , 1264-1269. https://doi.org/10.1177/0022034514551609
    51. Felicitas B. Bidlack, Chuong Huynh, Jeffrey Marshman, Bernhard Goetze. Helium ion microscopy of enamel crystallites and extracellular tooth enamel matrix. Frontiers in Physiology 2014, 5 https://doi.org/10.3389/fphys.2014.00395
    52. Roberto de la Rica, Ernest Mendoza, Lesley W. Chow, Kristy L. Cloyd, Sergio Bertazzo, Hannah C. Watkins, Joseph A. M. Steele, Molly M. Stevens. Self‐Assembly of Collagen Building Blocks Guided by Electric Fields. Small 2014, 10 (19) , 3876-3879. https://doi.org/10.1002/smll.201400424
    53. Shilpa Sen, Sudeshna Mukherjee, Atreyee Chaudhuri, Sumit Homechaudhuri. Temporal changes in brachyuran crab diversity along heterogeneous habitat in a mangrove ecosystem of Indian Sundarbans. Scientia Marina 2014, 78 (3) , 433-442. https://doi.org/10.3989/scimar.03931.04A
    54. Li Zhu, Haichuan Liu, H. Ewa Witkowska, Yulei Huang, Kataro Tanimoto, Wu Li. Preferential and selective degradation and removal of amelogenin adsorbed on hydroxyapatites by MMP20 and KLK4 in vitro. Frontiers in Physiology 2014, 5 https://doi.org/10.3389/fphys.2014.00268
    55. Karthik Balakrishna Chandrababu, Kaushik Dutta, Sowmya Bekshe Lokappa, Moise Ndao, John Spencer Evans, Janet Moradian‐Oldak. Structural adaptation of tooth enamel protein amelogenin in the presence of SDS micelles. Biopolymers 2014, 101 (5) , 525-535. https://doi.org/10.1002/bip.22415
    56. Garima Thakur, Kovur Prashanthi, Thomas Thundat. Self-Assembly of Proteins into Three-Dimensional Structures Using Bio-Conjugation. MRS Proceedings 2014, 1663 https://doi.org/10.1557/opl.2014.416
    57. Kayla B. Vasconcellos, Sean M. McHugh, Katherine J. Dapsis, Alexander R. Petty, Aren E. Gerdon. Biomimetic nanoparticles with polynucleotide and PEG mixed-monolayers enhance calcium phosphate mineralization. Journal of Nanoparticle Research 2013, 15 (9) https://doi.org/10.1007/s11051-013-1942-5
    58. Rajagopalan Thiruvengadathan, Venumadhav Korampally, Arkasubhra Ghosh, Nripen Chanda, Keshab Gangopadhyay, Shubhra Gangopadhyay. Nanomaterial processing using self-assembly-bottom-up chemical and biological approaches. Reports on Progress in Physics 2013, 76 (6) , 066501. https://doi.org/10.1088/0034-4885/76/6/066501
    59. Lijun Wang, Marit Nilsen-Hamilton. Biomineralization proteins: from vertebrates to bacteria. Frontiers in Biology 2013, 8 (2) , 234-246. https://doi.org/10.1007/s11515-012-1205-3
    60. Lisheng Ni, Nam K. Tonthat, Nagababu Chinnam, Maria A. Schumacher. Structures of the Escherichia coli transcription activator and regulator of diauxie, XylR: an AraC DNA-binding family member with a LacI/GalR ligand-binding domain. Nucleic Acids Research 2013, 41 (3) , 1998-2008. https://doi.org/10.1093/nar/gks1207
    61. Jiaojiao Yang, Shuqin Cao, Jiahui Li, Jianyu Xin, Xingyu Chen, Wei Wu, Fujian Xu, Jianshu Li. Staged self-assembly of PAMAM dendrimers into macroscopic aggregates with a microribbon structure similar to that of amelogenin. Soft Matter 2013, 9 (31) , 7553. https://doi.org/10.1039/c3sm51510a
    62. Yuwei Fan, Zezhang T Wen, Sumei Liao, Thomas Lallier, Joseph L Hagan, Jefferson T Twomley, Jian-Feng Zhang, Zhi Sun, Xiaoming Xu. Novel amelogenin-releasing hydrogel for remineralization of enamel artificial caries. Journal of Bioactive and Compatible Polymers 2012, 27 (6) , 585-603. https://doi.org/10.1177/0883911512458050
    63. E. Beniash, J.P. Simmer, H.C. Margolis. Structural Changes in Amelogenin upon Self-assembly and Mineral Interactions. Journal of Dental Research 2012, 91 (10) , 967-972. https://doi.org/10.1177/0022034512457371
    64. Sara Johnson, Young Koan Ko, Nitinun Varongchayakul, Sunhee Lee, Joseph Cappello, Hamidreza Ghandehari, Sang Bok Lee, Santiago D. Solares, Joonil Seog. Directed patterning of the self-assembled silk-elastin-like nanofibers using a nanomechanical stimulus. Chemical Communications 2012, 48 (86) , 10654. https://doi.org/10.1039/c2cc35384a
    Download PDF
    Go to Journal of the American Chemical Society
    Get e-Alerts
    Get e-Alerts

    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2011, 133, 43, 17406–17413
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ja206849c
    Published September 14, 2011
    Copyright © 2011 American Chemical Society
    Request reuse permissions

    Article Views

    2203

    Altmetric

    -

    Citations

    64
    Learn about these metrics

    Article Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.

    Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.

    The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated.