Literature DB >> 16342975

Gold nanoparticle-cytochrome C complexes: the effect of nanoparticle ligand charge on protein structure.

Marie-Eve Aubin-Tam1, Kimberly Hamad-Schifferli.   

Abstract

We report the effect of nanoparticle ligand charge on the structure of a covalently, site-specifically linked protein. Au nanoparticles with positive, negative, and neutral ligands were appended to a specific cysteine, C102, of Saccharomyces cerevisiae cytochrome c. Conjugates were purified by HPLC or gel electrophoresis. Circular dichroism spectroscopy shows that changing the nanoparticle ligand dramatically influences the attached cytochrome c structure. The protein retains its structure with neutral ligands but denatures in the presence of charged species. This is rationalized by the electrostatic interaction of amino acids in the local vicinity of C102 with the endgroups of the ligand.

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Year:  2005        PMID: 16342975     DOI: 10.1021/la052102e

Source DB:  PubMed          Journal:  Langmuir        ISSN: 0743-7463            Impact factor:   3.882


  43 in total

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Review 8.  Radiosensitization by gold nanoparticles.

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9.  Protein Interactions with Nanoparticle Surfaces: Highlighting Solution NMR Techniques.

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10.  Gold nanoparticle size controlled by polymeric Au(I) thiolate precursor size.

Authors:  Raymond P Briñas; Minghui Hu; Luping Qian; Elena S Lymar; James F Hainfeld
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