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Updated: Jan 19, 2026

Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy
Published on: March 6, 2017
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.
Abstract:
Self-assembling peptides have been employed as biotemplates for biomineralization, as the morphologies and sizes of the inorganic materials can be easily controlled. We synthesized two types of highly ordered self-assembling peptides with different secondary structures and investigated the effects of secondary structures on hydroxyapatite (HAp) biomineralization of peptide templates. All as-synthesized HAp-peptides have a selective protein adsorption capacity for basic protein (e.g., cytochrome c and lysozyme). Moreover, the selectivity was improved as peptide amounts increased. In particular, peptide-HAp templated on β-sheet peptides adsorbed more cytochrome c than peptide-HAp with α-helix structures, due to the greater than 2-times carboxyl group density at their surfaces. It can be expected that self-assembled peptide-templated HAp may be used as carriers for protein immobilization in biosensing and bioseparation applications and as enzyme-stabilizing agents.
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