Labeling ribonuclease S with a 3 nm Au nanoparticle by two-step assembly

Marie Eve Aubin; Diana G. Morales; Kimberly Hamad-Schifferli

doi:10.1021/nl0479031

Labeling ribonuclease S with a 3 nm Au nanoparticle by two-step assembly

Marie Eve Aubin
, Diana G. Morales
, Kimberly Hamad-Schifferli

Engineering

Massachusetts Institute of Technology
Massachusetts Institute of Technology

Research output: Contribution to journal › Article › peer-review

Abstract

We label ribonuclease S with a 3 nm Au nanoparticle (NP) by utilizing its two-piece structure. One portion, S-peptide, is mutated with a unique NP attachment site. NP-peptide self-assembles with the other portion, S-protein, to form an active enzyme. NP mobility decreases with peptide labeling and S-protein association. Surface plasmon shifts support conjugation. Higher S-peptide coverages on the NP surface reduce nonspecific adsorption, while sterically hindering assembly of RNaseS. Thiols displace nonspecific adsorption, maximizing site-specific labeling.

Original language	English
Pages (from-to)	519-522
Number of pages	4
Journal	Nano Letters
Volume	5
Issue number	3
DOIs	https://doi.org/10.1021/nl0479031
State	Published - Mar 2005

ASJC Scopus Subject Areas

Bioengineering
General Chemistry
General Materials Science
Condensed Matter Physics
Mechanical Engineering

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10.1021/nl0479031

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abstract = "We label ribonuclease S with a 3 nm Au nanoparticle (NP) by utilizing its two-piece structure. One portion, S-peptide, is mutated with a unique NP attachment site. NP-peptide self-assembles with the other portion, S-protein, to form an active enzyme. NP mobility decreases with peptide labeling and S-protein association. Surface plasmon shifts support conjugation. Higher S-peptide coverages on the NP surface reduce nonspecific adsorption, while sterically hindering assembly of RNaseS. Thiols displace nonspecific adsorption, maximizing site-specific labeling.",

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AB - We label ribonuclease S with a 3 nm Au nanoparticle (NP) by utilizing its two-piece structure. One portion, S-peptide, is mutated with a unique NP attachment site. NP-peptide self-assembles with the other portion, S-protein, to form an active enzyme. NP mobility decreases with peptide labeling and S-protein association. Surface plasmon shifts support conjugation. Higher S-peptide coverages on the NP surface reduce nonspecific adsorption, while sterically hindering assembly of RNaseS. Thiols displace nonspecific adsorption, maximizing site-specific labeling.

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Labeling ribonuclease S with a 3 nm Au nanoparticle by two-step assembly

Abstract

ASJC Scopus Subject Areas

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