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Functional Fragments of AIMP1-Derived Peptide (AdP) and Optimized Hydrosol for Their Topical Deposition by Box-Behnken Design
Aminoacyl-tRNA synthetase complex-interacting multifunctional protein 1 (AIMP1)-derived peptide (AdP) has been developed as a cosmeceutical ingredient for skin anti-aging given its fibroblast-activating (FA) and melanocyte-inhibiting (MI) functions. However, a suitable strategy for the topical deliv...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6572189/ https://www.ncbi.nlm.nih.gov/pubmed/31121831 http://dx.doi.org/10.3390/molecules24101967 |
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author | Lee, Jeong-Jun Han, Young-Min Kwon, Tae-Wan Kim, Dong Hyun Lee, Han Sol Jung, Woo Jin Kim, Jina Kang, Sujin Kim, Sang Kyum Cho, Cheong-Weon Lee, Keong-Ryoon Kim, Dae-Duk Park, Min Chul Lee, Jae-Young |
author_facet | Lee, Jeong-Jun Han, Young-Min Kwon, Tae-Wan Kim, Dong Hyun Lee, Han Sol Jung, Woo Jin Kim, Jina Kang, Sujin Kim, Sang Kyum Cho, Cheong-Weon Lee, Keong-Ryoon Kim, Dae-Duk Park, Min Chul Lee, Jae-Young |
author_sort | Lee, Jeong-Jun |
collection | PubMed |
description | Aminoacyl-tRNA synthetase complex-interacting multifunctional protein 1 (AIMP1)-derived peptide (AdP) has been developed as a cosmeceutical ingredient for skin anti-aging given its fibroblast-activating (FA) and melanocyte-inhibiting (MI) functions. However, a suitable strategy for the topical delivery of AdP was required due to its low-permeable properties. In this study, FA and MI domains of AdP (FA-AdP and MI-AdP, respectively) were determined by functional domain mapping, where the activities of several fragments of AdP on fibroblast and melanocyte were tested, and a hydrosol-based topical delivery system for these AdP fragments was prepared. The excipient composition of the hydrosol was optimized to maximize the viscosity and drying rate by using Box-Behnken design. The artificial skin deposition of FA-AdP-loaded hydrosol was evaluated using Keshary-Chien diffusion cells equipped with Strat-M membrane (STM). The quantification of the fluorescent dye-tagged FA-AdP in STM was carried out by near-infrared fluorescence imaging. The optimized hydrosol showed 127-fold higher peptide deposition in STM than free FA-AdP (p < 0.05). This work suggests that FA- and MI-AdP are active-domains for anti-wrinkle and whitening activities, respectively, and the hydrosol could be used as a promising cosmetic formulation for the delivery of AdPs to the skin. |
format | Online Article Text |
id | pubmed-6572189 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-65721892019-06-18 Functional Fragments of AIMP1-Derived Peptide (AdP) and Optimized Hydrosol for Their Topical Deposition by Box-Behnken Design Lee, Jeong-Jun Han, Young-Min Kwon, Tae-Wan Kim, Dong Hyun Lee, Han Sol Jung, Woo Jin Kim, Jina Kang, Sujin Kim, Sang Kyum Cho, Cheong-Weon Lee, Keong-Ryoon Kim, Dae-Duk Park, Min Chul Lee, Jae-Young Molecules Article Aminoacyl-tRNA synthetase complex-interacting multifunctional protein 1 (AIMP1)-derived peptide (AdP) has been developed as a cosmeceutical ingredient for skin anti-aging given its fibroblast-activating (FA) and melanocyte-inhibiting (MI) functions. However, a suitable strategy for the topical delivery of AdP was required due to its low-permeable properties. In this study, FA and MI domains of AdP (FA-AdP and MI-AdP, respectively) were determined by functional domain mapping, where the activities of several fragments of AdP on fibroblast and melanocyte were tested, and a hydrosol-based topical delivery system for these AdP fragments was prepared. The excipient composition of the hydrosol was optimized to maximize the viscosity and drying rate by using Box-Behnken design. The artificial skin deposition of FA-AdP-loaded hydrosol was evaluated using Keshary-Chien diffusion cells equipped with Strat-M membrane (STM). The quantification of the fluorescent dye-tagged FA-AdP in STM was carried out by near-infrared fluorescence imaging. The optimized hydrosol showed 127-fold higher peptide deposition in STM than free FA-AdP (p < 0.05). This work suggests that FA- and MI-AdP are active-domains for anti-wrinkle and whitening activities, respectively, and the hydrosol could be used as a promising cosmetic formulation for the delivery of AdPs to the skin. MDPI 2019-05-22 /pmc/articles/PMC6572189/ /pubmed/31121831 http://dx.doi.org/10.3390/molecules24101967 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Lee, Jeong-Jun Han, Young-Min Kwon, Tae-Wan Kim, Dong Hyun Lee, Han Sol Jung, Woo Jin Kim, Jina Kang, Sujin Kim, Sang Kyum Cho, Cheong-Weon Lee, Keong-Ryoon Kim, Dae-Duk Park, Min Chul Lee, Jae-Young Functional Fragments of AIMP1-Derived Peptide (AdP) and Optimized Hydrosol for Their Topical Deposition by Box-Behnken Design |
title | Functional Fragments of AIMP1-Derived Peptide (AdP) and Optimized Hydrosol for Their Topical Deposition by Box-Behnken Design |
title_full | Functional Fragments of AIMP1-Derived Peptide (AdP) and Optimized Hydrosol for Their Topical Deposition by Box-Behnken Design |
title_fullStr | Functional Fragments of AIMP1-Derived Peptide (AdP) and Optimized Hydrosol for Their Topical Deposition by Box-Behnken Design |
title_full_unstemmed | Functional Fragments of AIMP1-Derived Peptide (AdP) and Optimized Hydrosol for Their Topical Deposition by Box-Behnken Design |
title_short | Functional Fragments of AIMP1-Derived Peptide (AdP) and Optimized Hydrosol for Their Topical Deposition by Box-Behnken Design |
title_sort | functional fragments of aimp1-derived peptide (adp) and optimized hydrosol for their topical deposition by box-behnken design |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6572189/ https://www.ncbi.nlm.nih.gov/pubmed/31121831 http://dx.doi.org/10.3390/molecules24101967 |
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