Delving into the Latest Updates on Lysozyme with Synapse

Overview

Basic Info

Drug Type

Chemical drugs

Synonyms-

Target

Peptidoglycan

Mechanism

Peptidoglycan inhibitors, Cell wall inhibitors

Therapeutic Areas

Infectious DiseasesEye Diseases

Active Indication

BlepharitisConjunctivitisCorneal Ulcer+ [1]

Inactive Indication-

Originator Organization

Shenyang Xingqi Pharmaceutical Co., Ltd.

Active Organization

Shenyang Xingqi Pharmaceutical Co., Ltd.

Inactive Organization-

Drug Highest PhaseApproved

First Approval Date

CN (03 Apr 2019),

BlepharitisConjunctivitisCorneal Ulcer+ [1]

Regulation-

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Structure/Sequence

Sequence Code 1493357

Source: *****

Microcrystal electron diffraction (MicroED) is an emerging method for the structure determination of proteins and peptides, enzyme-inhibitor complexes. Several structures of biomolecules, including lysozyme, proteinase K, adenosine receptor A2A, insulin, xylanase, thermolysin, DNA, and Granulovirus occlusion bodies, have been successfully determined through MicroED. As MicroED uses very small crystals for structure determination, therefore, it has several advantages over conventional X-ray diffraction methods. In this review article, we discussed the most recent developments in the field of MicroED and its applications for the structural determination of different types of peptides, proteins, enzymes, DNA, and enzyme-inhibitor-complexed structures.

01 Mar 2025·International Journal of Biological Macromolecules

Core-shell gelatin-chitosan nanoparticles with lysozyme responsiveness formed via pH-drive and transglutaminase cross-linking

Article

Author: Nardin, Corinne ; Zhang, Yi ; Zhao, Yongqiang ; Li, Jilong

Lysozyme-responsive nanoparticles were fabricated using a hydrophilic protein (gelatin type A) as the core and a hydrophobic polysaccharide (chitosan) as the shell. In this study, curcumin was used as a model molecule for encapsulation and promoted the aggregation of gelatin nanoparticles. Transglutaminase catalyzed both intra-molecular cross-linking within gelatin and inter-molecular cross-linking between gelatin and chitosan. The formation mechanism of gelatin nanoparticles was investigated by molecular docking simulations, circular dichroism spectroscopy, UV-vis spectroscopy, turbidity analysis, and dynamic light scattering. Results indicated that pH-driven processes can induce molecular conformational changes of gelatin. However, these alone are insufficient to induce nanoparticle formation. Hydrogen bonding, Pi-alkyl interactions, Pi-Pi interactions, and van der Waals forces between gelatin and curcumin are crucial for the core formation. The coating mechanism of chitosan involved covalent bonds catalyzed by transglutaminase and electrostatic interactions, verified by dynamic light scattering and Fourier transform infrared spectroscopy. Physicochemical properties characterization revealed that the core-shell nanoparticles exhibited a maximum encapsulation efficiency of 97.2 ± 0.3 % and an average particle size of 120 ± 21 nm. The core-shell nanoparticles exhibited high thermal and pH stability, with curcumin retention rates exceeding 80 % under acidic, neutral, and weakly alkaline conditions, and detained thermal degradation up to 90 °C. Additionally, lysozyme responsiveness was evaluated by controlled curcumin release with varying lysozyme concentrations, through which enzymatic hydrolysis of chitosan by lysozyme triggered an increased release rate. In summary, core-shell nanoparticles synthesized from gelatin and chitosan may be effective target delivery systems for curcumin.

01 Feb 2025·Chemosphere

Evaluation of the effects of amitraz on the enzyme activity and stability of lysozyme: Spectroscopic and MD simulation approach

Article

Author: Shareghi, Behzad ; Farhadian, Sadegh ; Asgharzadeh, Sanaz

The binding interaction of food preservatives and pesticides has emerged as a matter of paramount importance as it not only presents potential health hazards but also carries substantial consequences for food processing and preservation. Herein, the mechanism of interaction between lysozyme and Amitraz was explored through spectroscopic and computational techniques. Spectral investigations indicated the spontaneous nature and stability of the lysozyme-Amitraz complex. The corresponding CD and FT-IR studies proved the structural changes of lysozyme. The presence of amitraz led to a notable decrease in both the enzymatic activity and thermal stability of lysozyme. Molecular docking demonstrated the preferred mode of interaction, and molecular dynamics simulations confirmed the stability of the resultant complex. In conclusion, the alarming findings of the lysozyme-Amitraz interaction underscore its detrimental impact on food safety and human health. Accordingly, urgent measures are imperative to address and mitigate the potential hazards posed by such interactions in food production.

100 Deals associated with Lysozyme

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External Link

KEGG	Wiki	ATC	Drug Bank
-	Lysozyme	-	DB13260

R&D Status

10 top approved records.

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Indication	Country/Location	Organization	Date
Blepharitis	CN	Shenyang Xingqi Pharmaceutical Co., Ltd.	03 Apr 2019
Conjunctivitis	CN	Shenyang Xingqi Pharmaceutical Co., Ltd.	03 Apr 2019
Corneal Ulcer	CN	Shenyang Xingqi Pharmaceutical Co., Ltd.	03 Apr 2019
Dacryocystitis	CN	Shenyang Xingqi Pharmaceutical Co., Ltd.	03 Apr 2019

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Clinical Result

Indication

Phase

Evaluation

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Study	Phase	Population	Analyzed Enrollment	Group	Results	Evaluation	Publication Date


ARVO2010	Not Applicable	-	-	EOBO alone	eoodivaele(uxidsfeqzf) = uxuypvcwet hrmhwpqqqb (wzpjselllj ) View more	-	01 Apr 2010
				Di-Block Copolymer, Poly(oxyethylene)-Poly(oxybutylene)lysozymelymer, Poly(oxyethylene)-Poly(oxybutylene) (EOBO-lysozyme mixture)	eoodivaele(uxidsfeqzf) = nlfksjzlpm hrmhwpqqqb (wzpjselllj ) View more