Lysozyme

Swaminathan, Rajaram; Ravi, Vijay; Kumar, Satish; Mattaparthi, Venkata Satish Kumar; Chandra, Nividh

doi:10.1016/b978-0-12-386483-3.00003-3

Cited by 230 publications

(130 citation statements)

References 158 publications

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“…[25–28] Hen egg white lysozyme has been a popular choice in computational studies of thermal unfolding, where MD simulations were performed at a range of temperatures from 300–500 K to accelerate unfolding. [29–33] There is evidence from computational and experimental studies that proteins unfold following the same pathway at higher temperatures, [34, 35] which rationalizes such an approach.…”

Section: Introductionmentioning

confidence: 99%

Computational study of aggregation mechanism in human lysozyme[D67H]

Patel

Kuyucak

2017

PLoS ONE

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Aggregation of proteins is an undesired phenomena that affects both human health and bioengineered products such as therapeutic proteins. Finding preventative measures could be facilitated by a molecular-level understanding of dimer formation, which is the first step in aggregation. Here we present a molecular dynamics (MD) study of dimer formation propensity in human lysozyme and its D67H variant. Because the latter protein aggregates while the former does not, they offer an ideal system for testing the feasibility of the proposed MD approach which comprises three stages: i) partially unfolded conformers involved in dimer formation are generated via high-temperature MD simulations, ii) potential dimer structures are searched using docking and refined with MD, iii) free energy calculations are performed to find the most stable dimer structure. Our results provide a detailed explanation for how a single mutation (D67H) turns human lysozyme from non-aggregating to an aggregating protein. Conversely, the proposed method can be used to identify the residues causing aggregation in a protein, which can be mutated to prevent it.

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Section: Introductionmentioning

confidence: 99%

Computational study of aggregation mechanism in human lysozyme[D67H]

Patel

Kuyucak

2017

PLoS ONE

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“…HEWL is a small size, 129 amino acid residues long protein that has been used as a model to study the mechanism of amyloid formation and inhibition6. Further, HEWL is homologous to human lysozyme which is responsible for non-neuropathic systemic amyloidosis resulting in deposition of amyloids in liver and kidney in humans.…”

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confidence: 99%

Vitamin k3 inhibits protein aggregation: Implication in the treatment of amyloid diseases

Alam

Chaturvedi

Siddiqi

et al. 2016

Sci Rep

158

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Protein misfolding and aggregation have been associated with several human diseases such as Alzheimer’s, Parkinson’s and familial amyloid polyneuropathy etc. In this study, anti-fibrillation activity of vitamin k3 and its effect on the kinetics of amyloid formation of hen egg white lysozyme (HEWL) and Aβ-42 peptide were investigated. Here, in combination with Thioflavin T (ThT) fluorescence assay, circular dichroism (CD), transmission electron microscopy and cell cytotoxicity assay, we demonstrated that vitamin k3 significantly inhibits fibril formation as well as the inhibitory effect is dose dependent manner. Our experimental studies inferred that vitamin k3 exert its neuro protective effect against amyloid induced cytotoxicity through concerted pathway, modifying the aggregation formation towards formation of nontoxic aggregates. Molecular docking demonstrated that vitamin k3 mediated inhibition of HEWL and Aβ-42 fibrillogenesis may be initiated by interacting with proteolytic resistant and aggregation prone regions respectively. This work would provide an insight into the mechanism of protein aggregation inhibition by vitamin k3; pave the way for discovery of other small molecules that may exert similar effect against amyloid formation and its associated neurodegenerative diseases.

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“…Lysozyme is an antimicrobial peptide that is part of the innate immune response and can be produced by neutrophils, monocytes, and macrophages [24] and it appears to participate in microbial mechanisms for parasite destruction [25]. In L. ( L. ) amazonensis- infected primates, increase in the density of lysozyme + cells was directly correlated with the increase in the number of iNOS + cells at 60 days PI, suggesting that parasite elimination could have occurred by both of these activation mechanisms.…”

Section: Discussionmentioning

confidence: 99%

Dynamic of the Cellular Immune Response at the Dermal Site ofLeishmania (L.) amazonensisandLeishmania (V.) braziliensisInfection inSapajus apellaPrimate

Laurenti

Passero

Tomokane

et al. 2014

BioMed Research International

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The purpose of this study was to characterize the immunopathological response in the skin of S. apella infected with Leishmania (L.) amazonensis and L. (V.) braziliensis parasites, the main causative agents of localized cutaneous leishmaniasis in South America. In infected animals, amastigote forms of L. (L.) amazonensis could be detected till 120 days postinfection (PI), while, in L. (V.) braziliensis infection, parasites could be detected until 180 days PI in the skin sections. CD20+ cells were detected throughout the experimental time in both groups as well as in CD3+ cells, which appeared to be activated because high densities of inducible nitric oxide synthase (iNOS+) cells were detected at 60 and 90 days PI in both studied groups. After 60 and 120 days PI, decrease in iNOS+ cells was observed in L. (L.) amazonensis and L. (V.) braziliensis, respectively, which was associated with parasite clearance. Increase in lysozyme+ cells was observed during the experimental infections, which also can be associated with parasite killing.

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Lysozyme

Cited by 230 publications

References 158 publications

Computational study of aggregation mechanism in human lysozyme[D67H]

Computational study of aggregation mechanism in human lysozyme[D67H]

Vitamin k3 inhibits protein aggregation: Implication in the treatment of amyloid diseases

Dynamic of the Cellular Immune Response at the Dermal Site ofLeishmania (L.) amazonensisandLeishmania (V.) braziliensisInfection inSapajus apellaPrimate

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