2015
DOI: 10.1016/j.peptides.2015.03.001
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Structure and antimicrobial activity relationship of royalisin, an antimicrobial peptide from royal jelly of Apis mellifera

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Cited by 91 publications
(78 citation statements)
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“…The major protein components of both species had different molecular weights, isoelectric points, and immunological characteristics (Takenaka & Takenaka, 1996). Many studies have shown the effect of royalisin against Gramnegative bacteria and some Gram-positive (Ilyasov et al, 2012) including the agent causing AFB (Bíliková et al, 2001;Bachanová et al, 2002;Yoshiyama & Kimura, 2010;Bílikova et al, 2015). In this study, we used royal jelly collected from A. mellifera therefore this might affect the AFB resistance of A. cerana as it may be somewhat different when compared in nature.…”
Section: Discussionmentioning
confidence: 99%
“…The major protein components of both species had different molecular weights, isoelectric points, and immunological characteristics (Takenaka & Takenaka, 1996). Many studies have shown the effect of royalisin against Gramnegative bacteria and some Gram-positive (Ilyasov et al, 2012) including the agent causing AFB (Bíliková et al, 2001;Bachanová et al, 2002;Yoshiyama & Kimura, 2010;Bílikova et al, 2015). In this study, we used royal jelly collected from A. mellifera therefore this might affect the AFB resistance of A. cerana as it may be somewhat different when compared in nature.…”
Section: Discussionmentioning
confidence: 99%
“…It has been reported that RJ has shown different pharmacological activities such as antimicrobial (Bílikova et al, 2015), antiviral (Hashemipour et al, 2014), antitumor (Guo et Royal jelly (RJ) is one of the most attractive bee products. RJ has long been used in traditional medicine.…”
Section: Introductionmentioning
confidence: 99%
“…Royal jelly is a secretion of honeybee hypopharynx and mandibular salivary glands. Royalisin, which is a potent antimicrobial protein composed of 51 amino acid residues in royal jelly, has extensive sequence homology with sapecin and phormicins, both of which are composed of 40 amino acids . Nevertheless, the role of the extra stretch of 11 amino acid residues at the C‐terminus of royalisin (positions 41‐51), termed royalisin P11 (Figure ), remains unknown.…”
Section: Introductionmentioning
confidence: 99%