2019
DOI: 10.1016/j.rechem.2019.100012
|View full text |Cite
|
Sign up to set email alerts
|

Preparation, spectral characterization and biological applications of Schiff base ligand and its transition metal complexes

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2

Citation Types

1
23
0

Year Published

2021
2021
2024
2024

Publication Types

Select...
8
1

Relationship

2
7

Authors

Journals

citations
Cited by 57 publications
(24 citation statements)
references
References 24 publications
1
23
0
Order By: Relevance
“…Any changes in these conditions result in physical instabilities resulting in the making or breaking of the interactions between different amino acids to maintain structural integrity causing a denaturation [22]. Furthermore, proteins demonstrate aqueous solubility depending of various factors such as pH, temperature, isoelectric point, presence of metallic ions and hydrophobicity that are measured using modern analytical methods such as X-ray diffraction, dynamic light scattering, size exclusion chromatography, mass spectroscopy (MS), circular dichroism spectroscopy, nuclear magnetic resonance spectroscopy, and Fourier transform infrared (FTIR) spectroscopy [26]. A formulation of therapeutic proteins should consider the fact that phenomena such as association, aggregation and hydrogen bonding between amino acids occur that likely change the properties of that protein [27].…”
Section: Emphasis On the Importance Of Physicochemical Propertiesmentioning
confidence: 99%
See 1 more Smart Citation
“…Any changes in these conditions result in physical instabilities resulting in the making or breaking of the interactions between different amino acids to maintain structural integrity causing a denaturation [22]. Furthermore, proteins demonstrate aqueous solubility depending of various factors such as pH, temperature, isoelectric point, presence of metallic ions and hydrophobicity that are measured using modern analytical methods such as X-ray diffraction, dynamic light scattering, size exclusion chromatography, mass spectroscopy (MS), circular dichroism spectroscopy, nuclear magnetic resonance spectroscopy, and Fourier transform infrared (FTIR) spectroscopy [26]. A formulation of therapeutic proteins should consider the fact that phenomena such as association, aggregation and hydrogen bonding between amino acids occur that likely change the properties of that protein [27].…”
Section: Emphasis On the Importance Of Physicochemical Propertiesmentioning
confidence: 99%
“…Excipients and covalent modifications that are possible in order to enhance the stability of the protein should be assessed by various analytical and bioinformatic methods. Instrumentations such as UV-visible spectroscopy, fluorescence measurements, circular dichroism (CD), FTIRspectroscopy are used for the assessment of influence of excipients on the protein stability whereas differential scanning calorimetry is used for thermal stability assessment [26]. The microenvironment of the protein is determined by the UV absorption range between 250-320 nm that primarily originate because of the presence of aromatic amino acids.…”
Section: Physicochemical Properties Assessmentmentioning
confidence: 99%
“…It has been proved that the cause and cure of many diseases is chelation. Many metal complexes of Schiff bases have been examined for their biological activities like antimicrobial [13], DNA interaction [14], anticarcinogenic [15], herbicidal [16], antineoplastic [17], COX-inhibitor [18], antiepileptic [19], antiviral [20], antioxidant [21] and analgesic [22]. However, important biological properties like antipathogenic [23], anticancer [24], fungicidal [25] and antidiabetic [26] are more pronounced for transition metal chelates of ethylene-1,2-diamine.…”
Section: Introductionmentioning
confidence: 99%
“…(De et al, 1970) Schiff bases play crucial role as chelating agents in complexes of transition metal (Hayashi et al, 2002;Temel & Hosgoren, 2002). Various reagents (Chang et al,2019;Feig, 1949;Gili et al, 1997;Husaain et al,2019;Holloway & Melnik ,1996;Nath et al, 1974;Scott, 1939;;Sayed et al, 2010;Shaheen et al, 2019;Vinusha et al,2019) are available for the spectrophotometric determination of Manganese (II).…”
Section: Introductionmentioning
confidence: 99%