Protein Conjugation to Nanoparticles by Designer Affinity Tags. / Ma, W.; Aboagye-Mensaha, D. ; Soloviev, Mikhail; Davletov, Bazbek; Ferrari, Enrico.

In: Materials Today: Proceedings, Vol. 4, No. 7, 2017, p. 6923–6929.

Research output: Contribution to journalArticlepeer-review

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Protein Conjugation to Nanoparticles by Designer Affinity Tags. / Ma, W.; Aboagye-Mensaha, D. ; Soloviev, Mikhail; Davletov, Bazbek; Ferrari, Enrico.

In: Materials Today: Proceedings, Vol. 4, No. 7, 2017, p. 6923–6929.

Research output: Contribution to journalArticlepeer-review

Harvard

Ma, W, Aboagye-Mensaha, D, Soloviev, M, Davletov, B & Ferrari, E 2017, 'Protein Conjugation to Nanoparticles by Designer Affinity Tags', Materials Today: Proceedings, vol. 4, no. 7, pp. 6923–6929. https://doi.org/10.1016/j.matpr.2017.07.021

APA

Ma, W., Aboagye-Mensaha, D., Soloviev, M., Davletov, B., & Ferrari, E. (2017). Protein Conjugation to Nanoparticles by Designer Affinity Tags. Materials Today: Proceedings, 4(7), 6923–6929. https://doi.org/10.1016/j.matpr.2017.07.021

Vancouver

Ma W, Aboagye-Mensaha D, Soloviev M, Davletov B, Ferrari E. Protein Conjugation to Nanoparticles by Designer Affinity Tags. Materials Today: Proceedings. 2017;4(7):6923–6929. https://doi.org/10.1016/j.matpr.2017.07.021

Author

Ma, W. ; Aboagye-Mensaha, D. ; Soloviev, Mikhail ; Davletov, Bazbek ; Ferrari, Enrico. / Protein Conjugation to Nanoparticles by Designer Affinity Tags. In: Materials Today: Proceedings. 2017 ; Vol. 4, No. 7. pp. 6923–6929.

BibTeX

@article{cc73dfc5a8164ded94099f51a7cc28d6,
title = "Protein Conjugation to Nanoparticles by Designer Affinity Tags",
abstract = "For the purpose of proteins bio-conjugation to Gold Nano-Particles (GNPs), we designed and synthesized a polypeptide named NanoLock, derived from SNARE (Soluble NSF Attachment protein REceptor) proteins and able to form a remarkably stable complex with the SNARE protein SNAP25 (Synaptosome Associated Protein of 25 kDa). We also characterized the adsorption of a SNAP25 recombinant fusion to Glutathione S-Transferases (GST) named GST-SNAP25 onto GNPs and found that it forms a stable protein corona surrounding GNPs. Using GST-SNAP25 as an intermediate protein, passively adsorbed on GNPs, we were able to stably bind NanoLock to GNPs.By fusing an arbitrary protein of interest to the affinity tag NanoLock, it would be in principle possible to bind any protein to GST-SNAP25 coated GNPs by simple mixing, in a site-oriented way. Therefore, we propose the pair NanoLock/GST-SNAP25 as a universal tool for the easy bio-conjugation of recombinant proteins to GNPs and possibly other gold surfaces. Further engineered versions of SNAP25, able to bind surfaces other than gold, could be used to decorate with proteins other materials, taking advantage of the same modular approach of the system described here in the case of GNPs.",
author = "W. Ma and D. Aboagye-Mensaha and Mikhail Soloviev and Bazbek Davletov and Enrico Ferrari",
year = "2017",
doi = "10.1016/j.matpr.2017.07.021",
language = "English",
volume = "4",
pages = "6923–6929",
journal = "Materials Today: Proceedings",
issn = "2214-7853",
publisher = "Elsevier",
number = "7",

}

RIS

TY - JOUR

T1 - Protein Conjugation to Nanoparticles by Designer Affinity Tags

AU - Ma, W.

AU - Aboagye-Mensaha, D.

AU - Soloviev, Mikhail

AU - Davletov, Bazbek

AU - Ferrari, Enrico

PY - 2017

Y1 - 2017

N2 - For the purpose of proteins bio-conjugation to Gold Nano-Particles (GNPs), we designed and synthesized a polypeptide named NanoLock, derived from SNARE (Soluble NSF Attachment protein REceptor) proteins and able to form a remarkably stable complex with the SNARE protein SNAP25 (Synaptosome Associated Protein of 25 kDa). We also characterized the adsorption of a SNAP25 recombinant fusion to Glutathione S-Transferases (GST) named GST-SNAP25 onto GNPs and found that it forms a stable protein corona surrounding GNPs. Using GST-SNAP25 as an intermediate protein, passively adsorbed on GNPs, we were able to stably bind NanoLock to GNPs.By fusing an arbitrary protein of interest to the affinity tag NanoLock, it would be in principle possible to bind any protein to GST-SNAP25 coated GNPs by simple mixing, in a site-oriented way. Therefore, we propose the pair NanoLock/GST-SNAP25 as a universal tool for the easy bio-conjugation of recombinant proteins to GNPs and possibly other gold surfaces. Further engineered versions of SNAP25, able to bind surfaces other than gold, could be used to decorate with proteins other materials, taking advantage of the same modular approach of the system described here in the case of GNPs.

AB - For the purpose of proteins bio-conjugation to Gold Nano-Particles (GNPs), we designed and synthesized a polypeptide named NanoLock, derived from SNARE (Soluble NSF Attachment protein REceptor) proteins and able to form a remarkably stable complex with the SNARE protein SNAP25 (Synaptosome Associated Protein of 25 kDa). We also characterized the adsorption of a SNAP25 recombinant fusion to Glutathione S-Transferases (GST) named GST-SNAP25 onto GNPs and found that it forms a stable protein corona surrounding GNPs. Using GST-SNAP25 as an intermediate protein, passively adsorbed on GNPs, we were able to stably bind NanoLock to GNPs.By fusing an arbitrary protein of interest to the affinity tag NanoLock, it would be in principle possible to bind any protein to GST-SNAP25 coated GNPs by simple mixing, in a site-oriented way. Therefore, we propose the pair NanoLock/GST-SNAP25 as a universal tool for the easy bio-conjugation of recombinant proteins to GNPs and possibly other gold surfaces. Further engineered versions of SNAP25, able to bind surfaces other than gold, could be used to decorate with proteins other materials, taking advantage of the same modular approach of the system described here in the case of GNPs.

U2 - 10.1016/j.matpr.2017.07.021

DO - 10.1016/j.matpr.2017.07.021

M3 - Article

VL - 4

SP - 6923

EP - 6929

JO - Materials Today: Proceedings

JF - Materials Today: Proceedings

SN - 2214-7853

IS - 7

ER -