TY - JOUR
T1 - Identification of indium tin oxide nanoparticle-binding peptides via phage display and biopanning under various buffer conditions
AU - Nakazawa, Hikaru
AU - Umetsu, Mitsuo
AU - Hirose, Tatsuya
AU - Hattori, Takamitsu
AU - Kumagai, Izumi
N1 - Funding Information:
This work was supported by Scientific Research Grants from the Ministry of Education, Culture, Sports, Science and Technology of Japan (H.N., 16K18296, 18K04842; M.U., 16H04570, 16K14483; and I.K., 24000011), and by Precursory Research for Embryonic Science and Technology from the Japan Science and Technology Agency (M.U.).
Publisher Copyright:
© 2020 Bentham Science Publishers.
PY - 2020
Y1 - 2020
N2 - Background: By recent advances in phage-display approaches, many oligopeptides exhibiting binding affinities for metal oxides have been identified. Indium tin oxide is one of the most widely used conductive oxides, because it has a large band gap of 3.7–4.0 eV. In recent years, there have been reports about several ITO-based biosensors. Development of an ITO binding interface for the clustering of sensor proteins without complex bioconjugates is required. Objective: In this article, we aimed to identify peptides that bind to indium tin oxide nanoparticles via different binding mechanisms. Methods: Indium tin oxide nanoparticles binding peptide ware selected using phage display and biopanning against indium tin oxide, under five different buffer conditions and these peptides characterized about binding affinity and specificity. Results: Three types of indium tin oxide nanoparticles-binding peptides were selected from 10 types of peptide candidates identified in phage display and biopanning. These included ITOBP8, which had an acidic isoelectric point, and was identified when a buffer containing guanidine was used, and ITOBP6 and ITOBP7, which contained a His-His-Lys sequence at their N-termini, and were identified when a highly concentrated phosphate elution buffer with a low ionic strength was used. Among these peptides, ITOBP6 exhibited the strongest indium tin oxide nanoparticles-binding affinity (dissociation constant, 585 nmol/L; amount of protein bound at saturation, 17.5 nmol/m 2-particles). Conclusion: These results indicate that peptides with specific binding properties can be obtained through careful selection of the buffer conditions in which the biopanning procedure is performed.
AB - Background: By recent advances in phage-display approaches, many oligopeptides exhibiting binding affinities for metal oxides have been identified. Indium tin oxide is one of the most widely used conductive oxides, because it has a large band gap of 3.7–4.0 eV. In recent years, there have been reports about several ITO-based biosensors. Development of an ITO binding interface for the clustering of sensor proteins without complex bioconjugates is required. Objective: In this article, we aimed to identify peptides that bind to indium tin oxide nanoparticles via different binding mechanisms. Methods: Indium tin oxide nanoparticles binding peptide ware selected using phage display and biopanning against indium tin oxide, under five different buffer conditions and these peptides characterized about binding affinity and specificity. Results: Three types of indium tin oxide nanoparticles-binding peptides were selected from 10 types of peptide candidates identified in phage display and biopanning. These included ITOBP8, which had an acidic isoelectric point, and was identified when a buffer containing guanidine was used, and ITOBP6 and ITOBP7, which contained a His-His-Lys sequence at their N-termini, and were identified when a highly concentrated phosphate elution buffer with a low ionic strength was used. Among these peptides, ITOBP6 exhibited the strongest indium tin oxide nanoparticles-binding affinity (dissociation constant, 585 nmol/L; amount of protein bound at saturation, 17.5 nmol/m 2-particles). Conclusion: These results indicate that peptides with specific binding properties can be obtained through careful selection of the buffer conditions in which the biopanning procedure is performed.
KW - Biopanning
KW - Evolution
KW - Indium tin oxide
KW - Inorganic material
KW - Peptide
KW - Phage display
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U2 - 10.2174/0929866526666191113151934
DO - 10.2174/0929866526666191113151934
M3 - Review article
C2 - 31729292
AN - SCOPUS:85086420346
VL - 27
SP - 557
EP - 566
JO - Protein and Peptide Letters
JF - Protein and Peptide Letters
SN - 0929-8665
IS - 6
ER -