2010•Unpublished venueRequires access

The Interaction between Tricyclazole and Bovine Serum Albumin by UV and Circular Dichroism

Ying Zhou

Abstract

The interaction between tricyclazole and bovine serum albumin (BSA) and the effect of different tricyclazole concentration to bovine serum albumin (BSA) had been studied by ultraviolet (UV) and circular dichroism (CD) spectroscopy. The results showed that the effect of tricyclazole to bovine serum albumin was multifaceted. The absorption spectra of UV showed that tricyclazole and bovine serum albumin (BSA) form the ground-state supramolecular complex with intermolecular forces. At the same time, hydrophobic interactions lead to a gradual increase intensity of UV absorption. The CD spectra showed that the peptide chain of BSA occurs contraction and rearrangement because of hydrophobic interactions and intramolecular hydrogen bonds. The conformation of BSA had been changed.

About this research paper

What this paper is about

Why it matters

OpenAlex reports 1 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

Key concepts: Bovine serum albumin, Circular dichroism, Chemistry, Intramolecular force, Hydrogen bond, Serum albumin, Hydrophobic effect, Absorption (acoustics)