Molecular design for specific peptides binding to inorganic material

2016 Fiscal Year Final Research Report

• Project/Area Number: 25249117
• Research Category: Grant-in-Aid for Scientific Research (A)
• Allocation Type: Single-year Grants
• Section: 一般
• Research Field: Biofunction/Bioprocess
• Research Institution: Hiroshima University
• Principal Investigator: Kuroda Akio 広島大学, 先端物質科学研究科, 教授 (50205241)
• Co-Investigator(Renkei-kenkyūsha): TATE Shinichi 広島大学, 理学研究科, 教授 (20216998)
• Project Period (FY): 2013-04-01 – 2017-03-31
• Keywords: アスベスト / バイオアッセイ / ペプチド / 結合

Outline of Final Research Achievements

Fluorescence microscopy-based assay with affinity probes could enable highly sensitive and selective detection of airborne asbestos, an inorganic environmental pollutant that can cause mesothelioma and lung cancer. We have selected a 31 amino acids peptide that specifically binds to amphibole asbestos, amosite. In order to clarify the binding mechanism, we identify the amino acid residues contributing to the probe’s affinity to amosite fibers by using a number of substituted peptides. We found that the probable binding mechanism is electrostatic interaction, with positively charged side chains of lysine residues being primarily responsible for the probe’s affinity to asbestos. We carried out structural analysis of the peptide using NMR and binding simulation between the peptide and the surface of asbestos.

Free Research Field

応用生物工学