Interaction of Schiff Base with Bovine Serum Albumin: Site-Specific Photocleavage

Shrivastava, H. Yamini; Kanthimathi, M.S.; Nair, Balachandran Unni

doi:10.1006/bbrc.1999.1675

Cited by 47 publications

(16 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The binding of FQ was also confirmed by circular dichroism (CD) spectra. As expected the ␣-helices of protein show a strong double minimum at 220 and 209 nm [9]. The intensities of this double minimum reflect the amount of helicity of BSA and further these indicate that BSA contains more than 50% of ␣-helical structure.…”

Section: Conformation Investigationsupporting

confidence: 70%

Study of the interaction between fluoroquinolones and bovine serum albumin

Kamat¹

2005

Journal of Pharmaceutical and Biomedical Analysis

110

View full text Add to dashboard Cite

Section: Conformation Investigationsupporting

confidence: 70%

Study of the interaction between fluoroquinolones and bovine serum albumin

Kamat¹

2005

Journal of Pharmaceutical and Biomedical Analysis

110

View full text Add to dashboard Cite

“…Hence it is clear that the photoexcited state of the cobalt(III) complex is responsible for the observed DNA cleavage. Photoexcited states of cobalt(III) complexes have previously been shown to bring about protein cleavage [52] and hence it is not surprising that complex 2 is able to bring about DNA cleavage under photolytic conditions.…”

Section: Photocleavage Of Pbr 322 Dnamentioning

confidence: 99%

Cobalt complexes of terpyridine ligand: Crystal structure and photocleavage of DNA

Indumathy

Srinivasan

Kanthimathi

et al. 2007

Journal of Inorganic Biochemistry

Self Cite

210

View full text Add to dashboard Cite

“…The interaction of the BSA and the HOSalenCo could be assessed by following the ellipticity change of the BSA [28]. In the PBS, the BSA showed a maximum negative absorption signal around 216 and 208 nm [29].…”

Section: Circular Dichroism Spectramentioning

confidence: 99%

Preparation and antioxidant activity of albumin binding Salen Schiff-base metal complexes

Zhang

Wang

et al. 2013

Chin. Sci. Bull.

View full text Add to dashboard Cite

A kind of novel biopolymer antioxidant (BSA/HOSalenM, M=Co, Mn, Zn) is prepared with conjugation, which increases the antioxidant activity of the bovine serum albumin (BSA). The conjugations have been characterized by IR spectra, UV-Vis spectra, Fluorescence spectra, Circular dichroism (CD) spectra and Native-PAGE. The BSA is used as a biopolymer scaffold, and the insoluble Salen Schiff-base metal complexes HOSalenM make axial coordination with the amino acid residues of the BSA. The structure of the BSA is unchanged when the binding rate of HOSalenCo is less than 10. The HOSalenCo conjugations show an excellent hydroxyl radical (·OH) scavenging activity, and the activity (EC 50 ) of BSA/HOSalenCo(10) (BSA : HOSalenCo=1 : 10) is improved by two orders of magnitude compared with the BSA, while the activity of the BSA/HOSalenMn is weak and the BSA/HOSalenZn shows no scavenging activity. The reactive oxygen species (ROSs) are associated with the carcinogenesis, the coronary heart disease and many health problems which are related to advancing age [1][2][3]. The hydroxyl radical (·OH) is one of the most damaging radicals produced under the physiological conditions. Epidemiological and clinical studies indicate that the effective antioxidants can protect the human body from the free radicals and retard the progress of many chronic diseases [4,5]. Many ROS-scavenging materials, including natural and synthetic antioxidants, are used to reduce the damage to the human body [6,7]. As synthetic antioxidants, Schiff-base metal complexes have been widely studied as the effective scavengers of the ROS [8][9][10][11]. However, the majority of Schiffbase metal complexes are insoluble in the aqueous solutions, which limits their applications.The serum albumin is a versatile protein, principally characterized by its remarkable ability of binding a wide range of insoluble endogenous and exogenous compounds [12][13][14][15]. Since the serum albumin was considered to be nonantigenic and biodegradable, and was readily available [16], the albumin has been used as a bio-material, such as drug delivery and novel hydrophilic carriers [17][18][19][20]. However, the bovine serum albumin (BSA) has not been used for ROS-scavenging materials because the ROS-scavenging activity of the BSA is very weak [21]. Recently, the macromolecules conjugation has been proved to be an effective method to improve their bioactivity [22]. In this paper, a biopolymer BSA and Salen Schiff-base metal complexes were integrated together, which afforded a new kind of water-soluble biopolymer conjugation. The specific affinity between the small molecule and the protein was proved to be one of the most straightforward and applicable approaches

show abstract

Interaction of Schiff Base with Bovine Serum Albumin: Site-Specific Photocleavage

Cited by 47 publications

References 22 publications

Study of the interaction between fluoroquinolones and bovine serum albumin

Study of the interaction between fluoroquinolones and bovine serum albumin

Cobalt complexes of terpyridine ligand: Crystal structure and photocleavage of DNA

Preparation and antioxidant activity of albumin binding Salen Schiff-base metal complexes

Contact Info

Product

Resources

About