Lysozyme–luteolin binding: molecular insights into the complexation process and the inhibitory effects of luteolin towards protein modification

Abstract

Luteolin shows inhibitory effects towards fibrillation and d-ribose mediated glycation of HEWL.

Interaction properties of biosynthesized cadmium sulphide quantum dots with human serum albumin: further investigation of antibacterial activities and sensing applications

“…This could occur through various molecular interactions such as collision quenching, ground‐state complex formation, excited state reactions, or rearrangements and excited state energy transfer from donor to acceptor molecules. [ 31,52 ] These interaction processes are classified as static quenching or dynamic quenching and can be identified using different studies such as temperature variation studies, viscosity, ground‐state complex formation, or precisely by executing the excited state lifetime measurements of protein and its complexes.…”

Thermal Reversibility and Structural Stability in Lysozyme Induced by Epirubicin Hydrochloride

“…9,10 Lysozyme is a small globular protein consisting of 129 amino acid residues, which comprise six tryptophan (Trp) residues, three tyrosine residues, and four disulfide bonds (Scheme 1a). 18,19 It has already been reported that the tryptophan residues W62 and W108 are responsible for the intrinsic fluorescence in Lyz. 2,7,18,20 Lyz can hydrolyze β-1,4-glycosidic linkages between N-acetylmuramic acid and N-acetyl glucosamine present in the peptidoglycan cell wall of bacteria, leading to bacterial cell lyses.…”

“…EPR, the 4′-epimer of Doxorubicin, displayed a similar tumor response during clinical trials of its application to breast cancer and the therapeutic effects . Hence, these properties of EPR are important as they have direct consequences in clinical research. , Lysozyme is a small globular protein consisting of 129 amino acid residues, which comprise six tryptophan (Trp) residues, three tyrosine residues, and four disulfide bonds (Scheme a). , It has already been reported that the tryptophan residues W62 and W108 are responsible for the intrinsic fluorescence in Lyz. ,,, Lyz can hydrolyze β-1,4-glycosidic linkages between N -acetylmuramic acid and N -acetyl glucosamine present in the peptidoglycan cell wall of bacteria, leading to bacterial cell lyses . The protein consists of two domains, namely α-domain (mainly comprising the α-helix) and β-domain (mainly comprising the β-sheet). , The substrate binding site (also known as “cleft”) is enclosed by these two domains .…”

“…The protein consists of two domains, namely α-domain (mainly comprising the α-helix) and β-domain (mainly comprising the β-sheet). , The substrate binding site (also known as “cleft”) is enclosed by these two domains . Lyz is mostly found in several secretions, e.g, saliva, tears, human milk, and mucus, and also in various tissues. , In addition to the pharmaceutical roles of Lyz, it is also used to carry the drug molecules to the target receptors due to the property of its reversible binding with many exogenous and endogenous compounds. , This is essential for the metabolism as well as transportation of the drug to the targeted receptor. , Recently, the interactions of a large number of anticancer drugs with several proteins have been well documented. − The Hen Egg White Lysozyme (with ∼60% similarity to its human variant) shows a high thermal stability and natural availability. Hence, it has been proficiently used as a model protein for studying the interaction with small molecules (drugs, dyes etc.).…”

Interaction of Carrier Protein with Potential Metallic Drug Candidate N-Glycoside ‘GATPT’: Validation by Multi-Spectroscopic and Molecular Docking Approaches

“…Lysozyme exhibits diverse pharmacological properties like anti-bacterial, anti-cancer, anti-viral, anti-septic, and anti-inflammatory. It is also known to bind reversibly with small molecules and has been reported to be used as a carrier in drug delivery [13][14][15][16][17].…”