ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

Studying Hemoglobin and a Bare Metal-Porphyrin Complex Immobilized on Functionalized Silicon Surfaces Using Synchrotron X-ray Reflectivity

Samajdar, Rudra N and Kumar, Chandan and Viswanath, P and Bhattacharyya, Aninda J (2019) Studying Hemoglobin and a Bare Metal-Porphyrin Complex Immobilized on Functionalized Silicon Surfaces Using Synchrotron X-ray Reflectivity. In: JOURNAL OF PHYSICAL CHEMISTRY B, 123 (35, SI). pp. 7492-7503.

[img] PDF
jou_phy_che_123-35_7492_2019.pdf - Published Version
Restricted to Registered users only

Download (3MB) | Request a copy
[img]
Preview
PDF
jp9b03085_si_001.pdf - Published Supplemental Material

Download (1MB) | Preview
Official URL: https://dx.doi.org/10.1021/acs.jpcb.9b03085

Abstract

We evaluate here, using synchrotron X-ray reflectivity, hemoglobin adsorption characteristics on silicon substrates with varying chemical functionalities. Hemoglobin at isoelectronic point and at negative charge is immobilized on functionalized hydrophilic (hydroxyl, carboxylic, amine) and hydrophobic (alkylated) silicon surfaces for the study. As a control, the bare cofactor hemin (containing only the metal and porphyrin with no amino acid residues) is also studied under similar conditions. Ordered layers (grown using the Langmuir-Blodgett technique) are observed to be less affected by the surface chemistry compared to the multilayers formed by physical absorption. Surface chemistry and charge of the proteins are critical in controlling the protein adsorption characteristics on silicon, such as thickness (correlated to molecule size) and roughness. In this study, this is very well realized by varying both the hydrophobicity and hydrophilicity of the substrate. The fundamental studies discussed here provide us with a set of important guidelines as to how electrode surface functionalization can control molecular conformation/orientation, especially protein adsorption on the substrate. This in turn is expected to have a significant impact on the protein electrochemical function and response of biomolecular devices.

Item Type: Journal Article
Additional Information: copyright for this article belongs to AMER CHEMICAL SOC
Department/Centre: Division of Chemical Sciences > Solid State & Structural Chemistry Unit
Depositing User: Id for Latest eprints
Date Deposited: 18 Oct 2019 07:39
Last Modified: 18 Oct 2019 07:39
URI: http://eprints.iisc.ac.in/id/eprint/63685

Actions (login required)

View Item View Item