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Protein Organization01:13

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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy
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Hydroxyapatite Formation on Self-Assembling Peptides with Differing Secondary Structures and Their Selective

Suzuka Kojima1, Hitomi Nakamura2, Sungho Lee3

  • 1National Institute of Advanced Industrial Science and Technology, 2266-98, Anagahora, Shimo-Shidami, Moriyama-ku, Nagoya, Aichi 463-8560, Japan. suzuka-kojima@aist.go.jp.

International Journal of Molecular Sciences
|September 25, 2019
PubMed
Summary

Self-assembling peptides control hydroxyapatite biomineralization. Beta-sheet peptides enhance protein adsorption for biosensing and bioseparation applications.

Keywords:
biotemplatehydroxyapatitepeptidesecondary structureselective protein adsorptionsolid-phase peptide synthesis

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Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Biomineralization

Background:

  • Self-assembling peptides offer tunable templates for controlled biomineralization.
  • Peptide secondary structures influence the morphology and size of inorganic materials.
  • Hydroxyapatite (HAp) formation is crucial in various biomedical applications.

Purpose of the Study:

  • To investigate the effect of peptide secondary structures (β-sheet vs. α-helix) on hydroxyapatite (HAp) biomineralization.
  • To evaluate the protein adsorption capacity of peptide-HAp composites.
  • To explore potential applications in biosensing and bioseparation.

Main Methods:

  • Synthesis of two types of highly ordered self-assembling peptides with distinct secondary structures.
  • Hydroxyapatite (HAp) biomineralization using peptide templates.
  • Selective protein adsorption assays using cytochrome c and lysozyme.

Main Results:

  • Both β-sheet and α-helix peptide templates successfully formed HAp.
  • All synthesized HAp-peptide composites exhibited selective adsorption for basic proteins.
  • HAp templated on β-sheet peptides showed significantly higher adsorption of cytochrome c compared to α-helix templated HAp.
  • Increased peptide amounts enhanced protein adsorption selectivity.
  • Higher carboxyl group density on β-sheet peptide surfaces contributed to increased cytochrome c adsorption.

Conclusions:

  • Peptide secondary structure critically influences HAp biomineralization and subsequent protein adsorption.
  • Self-assembled peptide-templated HAp demonstrates potential as a carrier for protein immobilization.
  • These materials could be valuable in biosensing, bioseparation, and as enzyme-stabilizing agents.