Dataset Information

Proteomics analysis of octapeptide from Lingzhi mushroom with anti-tyrosinase and anti-oxidative activity

ABSTRACT: Study the effect of novel octapeptide isolated from Lingzhi mushroom on skin melanocyte cell (Mus Musculus) by gel-free based proteomics

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Melanocyte, Cell Culture

DISEASE(S): Chronic Bronchitis,Skin Melanoma

SUBMITTER: Sucheewin Krobthong

LAB HEAD: Sucheewin Krobthong

PROVIDER: PXD017234 | Pride | 2022-08-11

REPOSITORIES: Pride

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Publications

Discovery of a Multifunctional Octapeptide from Lingzhi with Antioxidant and Tyrosinase Inhibitory Activity.

Yingchutrakul Yodying Y Krobthong Sucheewin S Choowongkomon Kiattawee K Papan Phakorn P Samutrtai Pawitrabhorn P Mahatnirunkul Thanisorn T Chomtong Thitikorn T Srimongkolpithak Nitipol N Jaroenchuensiri Theeranuch T Aonbangkhen Chanat C

Pharmaceuticals (Basel, Switzerland) 20220530 6

<i>Ganoderma lucidum</i> or Lingzhi is a fungus species widely known as a traditional medicine. Exploring the beneficial peptides by hydrolysis using pepsin and trypsin has been extensively performed to identify new bioactive natural products. A multifunctional peptide that expresses potential scavenging activity and tyrosinase inhibition is valuable in therapeutic and cosmetic applications. This study aimed to identify and investigate the effects of a novel multifunctional peptide from Lingzhi ...[more]

PMID: 35745603

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Project description:Background: Respiratory allergy triggered by pollen allergens is increasing at an alarming rate worldwide. Sunflower pollen is thought to be an important source of inhalant allergens. Present study aims to identify the prevalence of sunflower pollinosis among the Indian allergic population and characterizes the pollen allergens using immuno-proteomic tools. Methodology: Clinico-immunological tests were performed to understand the prevalence of sensitivity towards sunflower pollen among the atopic population. Sera from selected sunflower positive patients were used as probe to detect the IgE-reactive proteins from the one and two dimensionally separated proteome of sunflower pollen. The antigenic nature of the sugar moiety of the glycoprotein allergens was studied by meta-periodate modification of IgE-immunoblot. Finally, these allergens were identified by mass-spectrometry (MALDI TOF/TOF and LC ESI qTOF). MASCOT searching was performed against NCBInr database. However, Helianthus annuus genome is not fully sequenced and partially annotated. So in case of low confidence (p> 0.05) protein identification, searching was performed against EST library of Helianthus annuus. Results: Prevalence of sunflower pollen allergy was observed among 21% of the atopic population and associated with elevated level of specific IgE and histamine in the sera of these patients. Immunoscreening of sunflower pollen proteome with patient serum detected seven IgE-reactive proteins with varying molecular weight and pI. Hierarchical clustering of 2D-immunoblot data highlighted three allergens characterized by a more frequent immuno-reactivity and increased levels of IgE antibodies in the sera of susceptible patients. These allergens were considered as the major allergens of sunflower pollen and were found to have their glycan moiety critical for inducing IgE response. Homology driven search of MS/MS data of these IgE-reactive proteins identified seven previously unreported allergens from sunflower pollen. Three major allergenic proteins were identified as two non-isoformic pectate lyases and a cystein protease. Conclusion: Novelty of the present report is the identification of a panel of seven sunflower pollen allergens for the first time at immuno-biochemical and proteomic level, which substantiated the clinical evidence of sunflower allergy. Further purification and recombinant expression of these allergens will improve component-resolved diagnosis and therapy of pollen allergy.

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