l‑Cysteine Interaction with Au55 Nanoparticle

Simulations of l-cysteine molecules attaching on Au nanoparticles provide insight on how larger biomolecules (such as proteins and peptides) can interact with Au nanoparticles. The attaching mode is still in debate and of strong impact on the fundamental research in biosensors and biomedicine. We us...

Full description

Saved in:
Bibliographic Details
Published in:Journal of physical chemistry. C 2012-12, Vol.116 (49), p.25816-25823
Main Authors: Carr, Jessica A, Wang, Hong, Abraham, Anuji, Gullion, Terry, Lewis, James P
Format: Article
Language:English
Subjects:
Condensed matter: structure, mechanical and thermal properties
Cross-disciplinary physics: materials science
rheology
Exact sciences and technology
General equipment and techniques
Instruments, apparatus, components and techniques common to several branches of physics and astronomy
Low-dimensional structures (superlattices, quantum well structures, multilayers): structure, and nonelectronic properties
Materials science
Nanopowders
Nanoscale materials and structures: fabrication and characterization
Physics
Sensors (chemical, optical, electrical, movement, gas, etc.)
remote sensing
Surfaces and interfaces
thin films and whiskers (structure and nonelectronic properties)
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Simulations of l-cysteine molecules attaching on Au nanoparticles provide insight on how larger biomolecules (such as proteins and peptides) can interact with Au nanoparticles. The attaching mode is still in debate and of strong impact on the fundamental research in biosensors and biomedicine. We used a density functional theory (DFT) approach to calculate the interactions between l-cysteine molecules and the quantum sized Au nanoparticle Au55. Our results support the attaching mode recognized in solid-state NMR studies, which indicate that a double layer of l-cysteine molecules is the likely configuration. A strong electronic interaction between gold and sulfur atoms establishes a strong-bonding inner layer, while a hydrogen-bond network between zwitterion-structured cysteine molecules stabilizes the existence of a second layer with thiol (−SH) groups oriented outward. Such a structure has high potential for further biofunctionalization.
ISSN:1932-7447
1932-7455
DOI:10.1021/jp308215n