DSpace-CRIS

Now showing 1 - 3 of 3

Some of the metrics are blocked by your
consent settings
Stable Nanoemulsion System Development Enabling the Topical Delivery of Synechococcus-Derived Peptides
(2026-03-01)
Keawbankrud, Wannisa
;
Nakyai, Wongnapa
;
Phunpruch, Saranya
;
Sangtanoo, Papassara
;
Karnchanatat, Aphichart
Marine microalgae including Synechococcus sp. VDW offer the potential to serve as a source of bioactive peptides offering valuable antioxidant and antimelanogenic qualities for use in the pharmaceutical and cosmetics industries. At present, however, the use of such peptides is challenging due to their poor physicochemical stability. This research therefore sought to achieve the production and characterization of a stable nanoemulsion system based upon the use of synthetic Synechococcus-derived peptides through the process of high-pressure homogenization (HPH). Preparation of the nanoemulsions involved the use of Tween-80 and caprylic/capric triglyceride at a pressure of 7,500 psi to perform homogenization for varying durations of 15, 30 and 45 min. Using the optimized formulation with 0.1% w/w peptide for a time of 45 min resulted in 122.16 nm droplets while the zeta potential was −80.09 mV and the PDI (polydispersity index) value was 0.13. Colloidal stability could be considered high, while physical stability under thermal cycling, centrifugation and freeze-thaw cycles was very good, with no phase separation. For all testing intervals, the viscosity and refractive index were stable. It can thus be argues that the HPH approach is suitable to produce peptide-loaded nanoemulsions offering good stability and useful physicochemical characteristics. The developed nanoemulsion system has been optimized to offer potential for applications involving the transdermal delivery of marine peptides in the cosmeceutical sector and for a range of dermal therapies.
Some of the metrics are blocked by your
consent settings
Bee pollen peptides as potent tyrosinase inhibitors with anti-melanogenesis effects in murine b16f10 melanoma cells and zebrafish embryos
(2024-12-01)
Sangtanoo, Papassara
;
Srimongkol, Piroonporn
;
Saisavoey, Tanatorn
;
Puthong, Songchan
;
Buakeaw, Anumart
One important functional food ingredient today, valued for its health properties and ability to prevent disease, is bee pollen, which comprises a combination of nectar, pollen from plants, and the secretions of bees. In this research, the tyrosinase (TYR) inhibiting abilities of the peptides derived from bee pollen protein hydrolysates are investigated. Various proteases were utilized to generate these peptides, followed by testing at different concentrations. Tyrosinase inhibition activity was detected in all cases, while the hydrolysate drawn from 5.0% w/v neutrase exhibited the best IC<inf>50</inf> value and was thus investigated further via ultrafiltration to separate the active fractions. The highest potential for tyrosinase inhibition was recorded for the fractions below 0.65 kDa. Subsequent purification steps via SEC and RP-HPLC led to the identification of the VDGYPAAGY (named VY-9) peptide via LC-Q-TOF-MS/MS in fraction F<inf>1–2</inf>, known for its non-toxic and hydrophobic characteristics albeit poor water solubility. The synthesized VY-9 peptide demonstrated competitive inhibition, with IC<inf>50</inf> values of 0.55 ± 0.03 µM for mono-phenolase and 2.54 ± 0.06 µM for di-phenolase activities, as confirmed by molecular docking analysis revealing dominant hydrogen bond interactions with TYR. Effective concentrations of 0.2–1.6 µM of VY-9 showed negligible cytotoxicity in B16F10 cells. Melanin synthesis suppression was examined via qRT-PCR, and western blot in MITF, TYR, TRP-1, and TRP-2. Cell death in zebrafish embryos was evaluated in vivo using a toxicity assay which revealed no significant influence from VY-9, while anti-melanogenic effects were observed when the concentration was 4 µM, suggesting bee pollen-derived peptides’ potential in cosmetic and pharmaceutical depigmentation applications.
Some of the metrics are blocked by your
consent settings
Synechococcus marine microalgae peptide: Melanogenesis inhibition in cellular and zebrafish models
(2024-08-01)
Srimongkol, Piroonporn
;
Sangtanoo, Papassara
;
Saisavoey, Tanatorn
;
Puthong, Songchan
;
Buakeaw, Anumart
In this study, the AILQSYSAGKTK (named AK-12) peptide, also known as AK-12, from the Synechococcus marine microalgae cell extract is examined to determine the mechanism by which tyrosinase inhibition takes place. According to the docking simulation, it is expected that the peptides bind and interact at the tyrosinase active site, with the potential to support the inhibition of tyrosinase. For testing, the required peptides were first synthesized, before the results revealed tyrosinase inhibitory activity for which the respective IC<inf>50</inf> values for mono- and di-phenolase activities were 489.71 ± 0.01 μM, and 765.57 ± 0.01 μM. The characteristics of the different competitive types were shown in a Lineweaver-Burk plot. For the treatment of B16F10 cells, peptide concentrations of 50–400 μM were selected, confirming the absence of cytotoxicity. When the peptide was introduced, both tyrosinase activity and the production of melanin were significantly inhibited. Quantitative reverse transcription polymerase chain reaction (qRT-PCR) was then used to assess the suppression of melanin synthesis in MITF (microphthalmia-associated transcription factor, TYR (tyrosinase), TRP-1 (tyrosinase-related protein-1) and TRP-2 (tyrosinase-related protein-2). An in vivo toxicity assay was also carried out to evaluate zebrafish embryo cell death, revealing that AK-12 did not significantly affect cell death, while strong anti-melanogenic activity was observed for the concentration of 50 μM. From these findings it could be concluded that the peptide in question may offer potential in future hyperpigmentation treatments.

KMITL

Browse

Filters

Settings

Sort By

Results per page

Search Results