Polyproline-II helix in proteins: structure and function

AA Adzhubei, MJE Sternberg, AA Makarov - Journal of molecular biology, 2013 - Elsevier
The poly-l-proline type II (PPII) helix in recent years has emerged clearly as a structural class
not only of fibrillar proteins (in collagen, PPII is a dominant conformation) but also of the …

Large potentials of small heat shock proteins

EV Mymrikov, AS Seit-Nebi… - Physiological …, 2011 - journals.physiology.org
Modern classification of the family of human small heat shock proteins (the so-called HSPB)
is presented, and the structure and properties of three members of this family are analyzed …

[HTML][HTML] Protein-mediated enamel mineralization

J Moradian-Oldak - Frontiers in bioscience: a journal and virtual …, 2012 - ncbi.nlm.nih.gov
Enamel is a hard nanocomposite bioceramic with significant resilience that protects the
mammalian tooth from external physical and chemical damages. The remarkable …

Biomineralization process in hard tissues: The interaction complexity within protein and inorganic counterparts

V Sharma, A Srinivasan, F Nikolajeff, S Kumar - Acta biomaterialia, 2021 - Elsevier
Biomineralization can be considered as nature's strategy to produce and sustain
biominerals, primarily via creation of hard tissues for protection and support. This review …

Amelogenin and enamel biomimetics

Q Ruan, J Moradian-Oldak - Journal of Materials Chemistry B, 2015 - pubs.rsc.org
Mature tooth enamel is acellular and does not regenerate itself. Developing technologies
that rebuild tooth enamel and preserve tooth structure is therefore of great interest …

Application of isothermal titration calorimetry for characterizing thermodynamic parameters of biomolecular interactions: peptide self-assembly and protein adsorption …

M Kabiri, LD Unsworth - Biomacromolecules, 2014 - ACS Publications
The complex nature of macromolecular interactions usually makes it very hard to identify the
molecular-level mechanisms that ultimately dictate the result of these interactions. This is …

The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form

K Delak, C Harcup, R Lakshminarayanan, Z Sun… - Biochemistry, 2009 - ACS Publications
Amelogenins make up a class of proteins associated with the formation of mineralized
enamel in vertebrates, possess highly conserved N-and C-terminal sequence regions, and …

Enamel Matrix Derivative: A Review of Cellular Effects In Vitro and a Model of Molecular Arrangement and Functioning

HM Grandin, AC Gemperli, M Dard - Tissue Engineering Part B …, 2012 - liebertpub.com
Background: Enamel matrix derivative (EMD), the active component of Emdogain®, is a
viable option in the treatment of periodontal disease owing to its ability to regenerate lost …

Peptide-based bioinspired approach to regrowing multilayered aprismatic enamel

K Mukherjee, Q Ruan, S Nutt, J Tao, JJ De Yoreo… - Acs Omega, 2018 - ACS Publications
The gradual discovery of functional domains in native enamel matrix proteins has enabled
the design of smart bioinspired peptides for tooth enamel mimetics and repair. In this study …

How amelogenin orchestrates the organization of hierarchical elongated microstructures of apatite

X Yang, L Wang, Y Qin, Z Sun… - The Journal of …, 2010 - ACS Publications
Amelogenin (Amel) accelerates the nucleation of hydroxyapatite (HAP) in supersaturated
solutions of calcium phosphate (Ca− P), shortening the induction time (delay period), under …